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Conserved domains on  [gi|1774021274|ref|WP_153387277|]
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SDR family NAD(P)-dependent oxidoreductase [Companilactobacillus halodurans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06182 super family cl32126
short chain dehydrogenase; Validated
 3-240 5.05e-104

short chain dehydrogenase; Validated


The actual alignment was detected with superfamily member PRK06182:

Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 303.42  E-value: 5.05e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAG 82
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVNNAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  83 YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDSE 162
Cdd:PRK06182   84 YGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDALRLE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 163 VKRFGIRSIIDQPGLTKSEWSKIGFENARKNSlDNSPYDELVDKVEKLFSKLGTGATSED---LAQVFYHAATDAHPKRR 239
Cdd:PRK06182  164 VAPFGIDVVVIEPGGIKTEWGDIAADHLLKTS-GNGAYAEQAQAVAASMRSTYGSGRLSDpsvIADAISKAVTARRPKTR 242


                  .
gi 1774021274 240 Y 240
Cdd:PRK06182  243 Y 243
 
Name Accession Description Interval E-value
PRK06182 PRK06182
short chain dehydrogenase; Validated
 3-240 5.05e-104

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 303.42  E-value: 5.05e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAG 82
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVNNAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  83 YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDSE 162
Cdd:PRK06182   84 YGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDALRLE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 163 VKRFGIRSIIDQPGLTKSEWSKIGFENARKNSlDNSPYDELVDKVEKLFSKLGTGATSED---LAQVFYHAATDAHPKRR 239
Cdd:PRK06182  164 VAPFGIDVVVIEPGGIKTEWGDIAADHLLKTS-GNGAYAEQAQAVAASMRSTYGSGRLSDpsvIADAISKAVTARRPKTR 242


                  .
gi 1774021274 240 Y 240
Cdd:PRK06182  243 Y 243
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 3-241 3.21e-74

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: 226.73  E-value: 3.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARR---VERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNpdkLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVL 159
Cdd:cd05374    81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 160 DSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKNSLDnSPYDELVDKVEKLFSKLGTGATS-EDLAQVFYHAATDAHPKR 238
Cdd:cd05374   161 RLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPEI-SPYAPERKEIKENAAGVGSNPGDpEKVADVIVKALTSESPPL 239


                  ...
gi 1774021274 239 RYY 241
Cdd:cd05374   240 RYF 242
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-268 5.03e-68

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 210.88  E-value: 5.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK------GIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:COG0300     4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAElraagaRVEVVALDVTDPDAVAALAEAVLARFGPI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:COG0300    84 DVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSEWskigFENARknsldnspydelvdkveklFSKLGTGATSEDLAQVFYHAAtdA 234
Cdd:COG0300   164 FSESLRAELAPTGVRVTAVCPGPVDTPF----TARAG-------------------APAGRPLLSPEEVARAILRAL--E 218

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1774021274 235 HPKRRYYNSVVDHRMVMIARTMPNTYRIVLNKLM 268
Cdd:COG0300   219 RGRAEVYVGWDARLLARLLRLLPRLFDRLLRRAL 252
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-181 2.78e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 158.55  E-value: 2.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLeavaKELGALGgkALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180
                  ....*....|....*....|....*
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTD 185
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 4-176 9.91e-06

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 45.67  E-value: 9.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYF----KQQGFEVYGGARRVERLTDLRE--------KGIHTQKLDVTDKFSIRQLVdRTVSEQ 71
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELakclKSPGSVLVLSARNDEALRQLKAeigaersgLRVVRVSLDLGAEAGLEQLL-KALREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  72 GRID-----VLINNAG-YGEYGPLEEV--PIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGR--IINVSSIGAnvYSPL 141
Cdd:TIGR01500  81 PRPKglqrlLLINNAGtLGDVSKGFVDlsDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGLNrtVVNISSLCA--IQPF 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1774021274 142 GGW--YHATKASLNMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:TIGR01500 159 KGWalYCAGKAARDMLFQVLALEEKNPNVRVLNYAPG 195
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-91 1.73e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 38.23  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274    6 IITGISSGMGRAAALYFKQQgfevygGARRV--------------ERLTDLREKG--IHTQKLDVTDKFSIRQLVDRTVS 69
Cdd:smart00822   4 LITGGLGGLGRALARWLAER------GARRLvllsrsgpdapgaaALLAELEAAGarVTVVACDVADRDALAAVLAAIPA 77

                           90       100
                   ....*....|....*....|..
gi 1774021274   70 EQGRIDVLINNAGYGEYGPLEE 91
Cdd:smart00822  78 VEGPLTGVIHAAGVLDDGVLAS 99
 
Name Accession Description Interval E-value
PRK06182 PRK06182
short chain dehydrogenase; Validated
 3-240 5.05e-104

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 303.42  E-value: 5.05e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAG 82
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVNNAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  83 YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDSE 162
Cdd:PRK06182   84 YGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDALRLE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 163 VKRFGIRSIIDQPGLTKSEWSKIGFENARKNSlDNSPYDELVDKVEKLFSKLGTGATSED---LAQVFYHAATDAHPKRR 239
Cdd:PRK06182  164 VAPFGIDVVVIEPGGIKTEWGDIAADHLLKTS-GNGAYAEQAQAVAASMRSTYGSGRLSDpsvIADAISKAVTARRPKTR 242


                  .
gi 1774021274 240 Y 240
Cdd:PRK06182  243 Y 243
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 3-241 3.21e-74

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: 226.73  E-value: 3.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARR---VERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNpdkLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVL 159
Cdd:cd05374    81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 160 DSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKNSLDnSPYDELVDKVEKLFSKLGTGATS-EDLAQVFYHAATDAHPKR 238
Cdd:cd05374   161 RLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPEI-SPYAPERKEIKENAAGVGSNPGDpEKVADVIVKALTSESPPL 239


                  ...
gi 1774021274 239 RYY 241
Cdd:cd05374   240 RYF 242
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-268 5.03e-68

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 210.88  E-value: 5.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK------GIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:COG0300     4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAElraagaRVEVVALDVTDPDAVAALAEAVLARFGPI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:COG0300    84 DVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSEWskigFENARknsldnspydelvdkveklFSKLGTGATSEDLAQVFYHAAtdA 234
Cdd:COG0300   164 FSESLRAELAPTGVRVTAVCPGPVDTPF----TARAG-------------------APAGRPLLSPEEVARAILRAL--E 218

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1774021274 235 HPKRRYYNSVVDHRMVMIARTMPNTYRIVLNKLM 268
Cdd:COG0300   219 RGRAEVYVGWDARLLARLLRLLPRLFDRLLRRAL 252
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 3-240 8.42e-66

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 205.91  E-value: 8.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRekGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAG 82
Cdd:PRK06179    5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIP--GVELLELDVTDDASVQAAVDEVIARAGRIDVLVNNAG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  83 YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDSE 162
Cdd:PRK06179   83 VGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEGYSESLDHE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 163 VKRFGIRSIIDQPGLTKSewskiGFEnarKNSLD-NSP---YDELVDKVEKLFSK-LGTGATSEDLAQVFYHAATDAHPK 237
Cdd:PRK06179  163 VRQFGIRVSLVEPAYTKT-----NFD---ANAPEpDSPlaeYDRERAVVSKAVAKaVKKADAPEVVADTVVKAALGPWPK 234


                  ...
gi 1774021274 238 RRY 240
Cdd:PRK06179  235 MRY 237
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-233 1.90e-65

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: 203.88  E-value: 1.90e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MT---RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK---GIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:COG4221     1 MSdkgKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAElggRALAVPLDVTDEAAVEAAVAAAVAEFGRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:COG4221    81 DVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENarknslDNSPYDELVDKVEKLfsklgtgaTSEDLAQVFYHAATD 233
Cdd:COG4221   161 LSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDG------DAEAAAAVYEGLEPL--------TPEDVAEAVLFALTQ 225
PRK06914 PRK06914
SDR family oxidoreductase;
1-240 1.75e-58

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 187.54  E-value: 1.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKG--------IHTQKLDVTDKFSIrQLVDRTVSEQG 72
Cdd:PRK06914    2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlqqnIKVQQLDVTDQNSI-HNFQLVLKEIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:PRK06914   81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPGLTKSE-WSKiGFENARKNSLDNSPYDELVDKVEKLFSKLG-TGATSEDLAQVFYHA 230
Cdd:PRK06914  161 EGFSESLRLELKPFGIDVALIEPGSYNTNiWEV-GKQLAENQSETTSPYKEYMKKIQKHINSGSdTFGNPIDVANLIVEI 239

                         250
                  ....*....|
gi 1774021274 231 ATDAHPKRRY 240
Cdd:PRK06914  240 AESKRPKLRY 249
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 1-209 4.53e-55

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 178.69  E-value: 4.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRA---AALyfkQQGFEVYGGARRVERLTDLREK---GIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK08263    2 MEKVWFITGASRGFGRAwteAAL---ERGDRVVATARDTATLADLAEKygdRLLPLALDVTDRAAVFAAVETAVEHFGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK08263   79 DIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFenarKNSLDNSPYDELVDKVEK 209
Cdd:PRK08263  159 MSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSA----KRATPLDAYDTLREELAE 209
PRK05693 PRK05693
SDR family oxidoreductase;
4-238 3.89e-54

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 176.13  E-value: 3.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAGY 83
Cdd:PRK05693    3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHGGLDVLINNAGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  84 GEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRqNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDSEV 163
Cdd:PRK05693   83 GAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRR-SRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDALRLEL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774021274 164 KRFGIRSIIDQPGLTKSEWSKIGFENARKNSLDNSPYDELVDKVEKLFSKLGTGATS-EDLAQVFYHAATDAHPKR 238
Cdd:PRK05693  162 APFGVQVMEVQPGAIASQFASNASREAEQLLAEQSPWWPLREHIQARARASQDNPTPaAEFARQLLAAVQQSPRPR 237
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 3-234 4.69e-53

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: 172.66  E-value: 4.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:COG1028     7 KVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALeaaaAELRAAGgrALAVAADVTDEAAVEALVAAAVAAFGRLDI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGAnvYSPLGGW--YHATKASLNM 154
Cdd:COG1028    87 LVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAG--LRGSPGQaaYAASKAAVVG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 155 WSDVLDSEVKRFGIR--SIidQPGLTKSEWSK--IGFENARKNSLDNSPydelvdkveklfskLGTGATSEDLAQVFYHA 230
Cdd:COG1028   165 LTRSLALELAPRGIRvnAV--APGPIDTPMTRalLGAEEVREALAARIP--------------LGRLGTPEEVAAAVLFL 228


                  ....
gi 1774021274 231 ATDA 234
Cdd:COG1028   229 ASDA 232
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-207 3.29e-52

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 171.25  E-value: 3.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRA---AALyfkQQGFEVYGGARRVERLTDLREKG---IHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK06180    3 SMKTWLITGVSSGFGRAlaqAAL---AAGHRVVGTVRSEAARADFEALHpdrALARLLDVTDFDAIDAVVADAEATFGPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK06180   80 DVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSEWSkiGFENAR-KNSLDNspYDELVDKV 207
Cdd:PRK06180  160 ISESLAKEVAPFGIHVTAVEPGSFRTDWA--GRSMVRtPRSIAD--YDALFGPI 209
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-234 2.80e-50

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: 165.15  E-value: 2.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARRVERL---TDLREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALaelAAIEALGgnAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVL 159
Cdd:cd05233    81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774021274 160 DSEVKRFGIRSIIDQPGLTKSE-WSKIGFENARKNSLDNSPydelvdkveklfskLGTGATSEDLAQVFYHAATDA 234
Cdd:cd05233   161 ALELAPYGIRVNAVAPGLVDTPmLAKLGPEEAEKELAAAIP--------------LGRLGTPEEVAEAVVFLASDE 222
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-181 2.78e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 158.55  E-value: 2.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLeavaKELGALGgkALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180
                  ....*....|....*....|....*
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTD 185
PRK05993 PRK05993
SDR family oxidoreductase;
1-269 1.37e-46

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 156.73  E-value: 1.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDrTVSEQ--GRIDVLI 78
Cdd:PRK05993    3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAEGLEAFQLDYAEPESIAALVA-QVLELsgGRLDALF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDV 158
Cdd:PRK05993   82 NNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFAIEGLSLT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 159 LDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKN-SLDNSP----YDELVDKVEKLFS----KLGtgatSEDLAQVFYH 229
Cdd:PRK05993  162 LRMELQGSGIHVSLIEPGPIETRFRANALAAFKRWiDIENSVhraaYQQQMARLEGGGSksrfKLG----PEAVYAVLLH 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1774021274 230 AATDAHPKRRYYNSVVDHRMVMIARTMPNTyriVLNKLMK 269
Cdd:PRK05993  238 ALTAPRPRPHYRVTTPAKQGALLKRLLPAR---WLYRLLR 274
PRK08017 PRK08017
SDR family oxidoreductase;
1-257 2.34e-45

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 152.93  E-value: 2.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVS-EQGRIDVLIN 79
Cdd:PRK08017    1 MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNSLGFTGILLDLDDPESVERAADEVIAlTDNRLYGLFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVL 159
Cdd:PRK08017   81 NAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWSDAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 160 DSEVKRFGIRSIIDQPGLTKSEWSkigfENARKNSLDnspydelvdkveKLFSKLGTGA----TSEDLAQVFYHAATDAH 235
Cdd:PRK08017  161 RMELRHSGIKVSLIEPGPIRTRFT----DNVNQTQSD------------KPVENPGIAArftlGPEAVVPKLRHALESPK 224

                         250       260
                  ....*....|....*....|..
gi 1774021274 236 PKRRYYNSVVDHRMVMIARTMP 257
Cdd:PRK08017  225 PKLRYPVTLVTHAVMVLKRLLP 246
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 3-235 2.29e-44

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: 150.00  E-value: 2.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK------GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:cd08934     4 KVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADEleaeggKALVLELDVTDEQQVDAAVERTVEALGRLDI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:cd08934    84 LVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFS 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKNSldnspYDELVDKVEKLfsklgtgaTSEDLAQVFYHAATDAH 235
Cdd:cd08934   164 EGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEA-----YEERISTIRKL--------QAEDIAAAVRYAVTAPH 229
PRK06482 PRK06482
SDR family oxidoreductase;
1-203 1.46e-41

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 143.72  E-value: 1.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK---GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK06482    1 MSKTWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARygdRLWVLQLDVTDSAAVRAVVDRAFAALGRIDVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSD 157
Cdd:PRK06482   81 VSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1774021274 158 VLDSEVKRFGIRSIIDQPGLTKSEWSKiGFENARK-NSLDNSPYDEL 203
Cdd:PRK06482  161 AVAQEVAPFGIEFTIVEPGPARTNFGA-GLDRGAPlDAYDDTPVGDL 206
PRK07454 PRK07454
SDR family oxidoreductase;
1-176 2.97e-41

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 142.02  E-value: 2.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL----REKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK07454    5 SMPRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALaaelRSTGvkAAAYSIDLSNPEAIAPGIAELLEQFGCP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK07454   85 DVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAA 164

                         170       180
                  ....*....|....*....|..
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK07454  165 FTKCLAEEERSHGIRVCTITLG 186
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 6-257 5.07e-39

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: 137.41  E-value: 5.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQGFEVY--------GGARRVERLTDLRekgIHTQKLDVTDKFSIR---QLVDRTVSEQGrI 74
Cdd:cd09805     4 LITGCDSGFGNLLAKKLDSLGFTVLagcltkngPGAKELRRVCSDR---LRTLQLDVTKPEQIKraaQWVKEHVGEKG-L 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEE-VPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNsGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:cd09805    80 WGLVNNAGILGFGGDEElLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAK-GRVVNVSSMGGRVPFPAGGAYCASKAAVE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGL--TKSEWSKIGFENARKNSLDNSP-----------YDELVDKVEKLFSKLgtgatS 220
Cdd:cd09805   159 AFSDSLRRELQPWGVKVSIIEPGNfkTGITGNSELWEKQAKKLWERLPpevkkdygedyIDELKNKMLKYCSRA-----S 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1774021274 221 EDLAQV---FYHAATDAHPKRRYYNSVVDHRMVMIARTMP 257
Cdd:cd09805   234 PDLSPVidsIEHALTSRHPRTRYYPGKDAKLLYIPASYLP 273
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 5-232 1.70e-38

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: 135.10  E-value: 1.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK-------GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:cd05346     3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADElgakfpvKVLPLQLDVSDRESIEAALENLPEEFRDIDIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGeYG--PLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:cd05346    83 VNNAGLA-LGldPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQF 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274 156 SDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENarknslDNSPYDELVDKVEKLfsklgtgaTSEDLAQVFYHAAT 232
Cdd:cd05346   162 SLNLRKDLIGTGIRVTNIEPGLVETEFSLVRFHG------DKEKADKVYEGVEPL--------TPEDIAETILWVAS 224
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-195 3.73e-38

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 134.20  E-value: 3.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVY--------GGARRVERLtdlREKGIHTQ--KLDVTDKFSIRQLVDRTVSE 70
Cdd:PRK05565    4 MGKVAIVTGASGGIGRAIAELLAKEGAKVViaydineeAAQELLEEI---KEEGGDAIavKADVSSEEDVENLVEQIVEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  71 QGRIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKA 150
Cdd:PRK05565   81 FGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1774021274 151 SLNMWSDVLDSEVKRFGIRSIIDQPGLTK-SEWSKigFENARKNSL 195
Cdd:PRK05565  161 AVNAFTKALAKELAPSGIRVNAVAPGAIDtEMWSS--FSEEDKEGL 204
PRK09291 PRK09291
SDR family oxidoreductase;
1-192 8.10e-38

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 133.58  E-value: 8.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK------GIHTQKLDVTDKFsirqlvDRTVSEQGRI 74
Cdd:PRK09291    1 MSKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEaarrglALRVEKLDLTDAI------DRAQAAEWDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK09291   75 DVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEA 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARK 192
Cdd:PRK09291  155 IAEAMHAELKPFGIQVATVNPGPYLTGFNDTMAETPKR 192
FabG-like PRK07231
SDR family oxidoreductase;
3-169 2.10e-36

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 129.56  E-value: 2.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLT----DLREKG-IHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK07231    6 KVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAErvaaEILAGGrAIAVAADVSDEADVEAAVAAALERFGSVDIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGE-YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK07231   86 VNNAGTTHrNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLT 165

                         170
                  ....*....|...
gi 1774021274 157 DVLDSEVKRFGIR 169
Cdd:PRK07231  166 KALAAELGPDKIR 178
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 3-225 2.39e-35

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: 126.93  E-value: 2.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL-------TDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05332     4 KVVIITGASSGIGEELAYHLARLGARLVLSARREERLeevksecLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFGGLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:cd05332    84 ILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGF 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 156 SDVLDSEVKRFGIRSIIDQPGLTKSewskigfeNARKNSLDNSpydelVDKVEKLFSKLGTGATSEDLAQ 225
Cdd:cd05332   164 FDSLRAELSEPNISVTVVCPGLIDT--------NIAMNALSGD-----GSMSAKMDDTTANGMSPEECAL 220
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 3-180 2.95e-35

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: 125.94  E-value: 2.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL--TDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINN 80
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLaaLSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  81 AGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLD 160
Cdd:cd08932    81 AGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALR 160

                         170       180
                  ....*....|....*....|....*.
gi 1774021274 161 SEVKRFGIR------SIIDQPGLTKS 180
Cdd:cd08932   161 QEGWDHGVRvsavcpGFVDTPMAQGL 186
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-226 2.96e-35

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: 126.39  E-value: 2.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  12 SGMGRAAALYFKQQGFEV---YGGARRVERLTDLREK-GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAGYG--E 85
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVvltDLNEALAKRVEELAEElGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFApkL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  86 YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQnsGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDSEVKR 165
Cdd:pfam13561  86 KGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGP 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774021274 166 FGIR--SIIdqPGLTKSE-WSKI-GFENARKNSLDNSPydelvdkveklfskLGTGATSEDLAQV 226
Cdd:pfam13561 164 RGIRvnAIS--PGPIKTLaASGIpGFDELLAAAEARAP--------------LGRLGTPEEVANA 212
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 5-181 5.19e-34

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: 123.21  E-value: 5.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE------KGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAellnpnPSVEVEILDVTDEERNQLVIAELEAELGGLDLVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDV 158
Cdd:cd05350    81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAES 160

                         170       180
                  ....*....|....*....|...
gi 1774021274 159 LDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:cd05350   161 LRYDVKKRGIRVTVINPGFIDTP 183
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-226 7.76e-33

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 120.36  E-value: 7.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARR--------VERLTDLREKgIHTQKLDVTDKFSIRQLVDRTVSEQG 72
Cdd:PRK12825    5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRSdeeaaeelVEAVEALGRR-AQAVQADVTDKAALEAAVAAAVERFG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGAnvyspLGGW-----YHA 147
Cdd:PRK12825   84 RIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAG-----LPGWpgrsnYAA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274 148 TKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKNSLDNSPydelvdkveklfskLGTGATSEDLAQV 226
Cdd:PRK12825  159 AKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETP--------------LGRSGTPEDIARA 223
PRK12826 PRK12826
SDR family oxidoreductase;
1-169 7.96e-33

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 120.41  E-value: 7.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK------GIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK12826    5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELveaaggKARARQVDVRDRAALKAAVAAGVEDFGRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIgANVYSPLGGW--YHATKASL 152
Cdd:PRK12826   85 DILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSV-AGPRVGYPGLahYAASKAGL 163

                         170
                  ....*....|....*..
gi 1774021274 153 NMWSDVLDSEVKRFGIR 169
Cdd:PRK12826  164 VGFTRALALELAARNIT 180
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 7-164 1.34e-32

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 119.50  E-value: 1.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   7 ITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK--GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAGYG 84
Cdd:COG3967    10 ITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAAnpGLHTIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  85 EYGPL--EEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVL--- 159
Cdd:COG3967    90 RAEDLldEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYTQSLrhq 169


                  ....*..
gi 1774021274 160 --DSEVK 164
Cdd:COG3967   170 lkDTSVK 176
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 3-181 1.57e-32

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: 118.88  E-value: 1.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGF-EVYGGARRVER----LTDLREKGIHTQ--KLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERgqaaVEKLRAEGLSVRfhQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAG--YGEYGPLEEvPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIganvYSPLGGWYHATKASLN 153
Cdd:cd05324    81 ILVNNAGiaFKGFDDSTP-TREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSG----LGSLTSAYGVSKAALN 155

                         170       180
                  ....*....|....*....|....*...
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:cd05324   156 ALTRILAKELKETGIKVNACCPGWVKTD 183
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 3-226 7.12e-32

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: 117.76  E-value: 7.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKGI--HTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:cd05344     2 KVALVTAASSGIGLAIARALAREGARVAICARNRENLeraaSELRAGGAgvLAVVADLTDPEDIDRLVEKAGDAFGRVDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:cd05344    82 LVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSE-WSKIGFENARKNSLDnspydelVDKVEKLFSK---LGTGATSEDLAQV 226
Cdd:cd05344   162 KTLSRELAPDGVTVNSVLPGYIDTErVRRLLEARAEKEGIS-------VEEAEKEVASqipLGRVGKPEELAAL 228
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 3-163 1.17e-31

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: 116.71  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKGihTQKL----DVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd05360     1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALhelaREVRELG--GEAIavvaDVADAAQVERAADTAVERFGRI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:cd05360    79 DTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRG 158


                  ....*....
gi 1774021274 155 WSDVLDSEV 163
Cdd:cd05360   159 FTESLRAEL 167
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 3-207 1.36e-31

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: 116.64  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK--GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINN 80
Cdd:cd05370     6 NTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKElpNIHTIVLDVGDAESVEALAEALLSEYPNLDILINN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  81 AGYG---EYGPLEEVPiENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSD 157
Cdd:cd05370    86 AGIQrpiDLRDPASDL-DKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAALHSYTL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1774021274 158 VLDSEVKRFGIRSIIDQPGLTKSEWSKiGFENARKNSLDNSPYDELVDKV 207
Cdd:cd05370   165 ALRHQLKDTGVEVVEIVPPAVDTELHE-ERRNPDGGTPRKMPLDEFVDEV 213
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 5-246 3.95e-31

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: 115.64  E-value: 3.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGgARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAGYG 84
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIA-LDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAGVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  85 EYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDSEVK 164
Cdd:cd05331    80 RPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 165 RFGIRSIIDQPGLTKS--EWSKIGFENARKNSLDNSPYDelvdkvEKLFSKLGTGATSEDLAQVFYHAATDAHPKRRYYN 242
Cdd:cd05331   160 PYGVRCNVVSPGSTDTamQRTLWHDEDGAAQVIAGVPEQ------FRLGIPLGKIAQPADIANAVLFLASDQAGHITMHD 233


                  ....
gi 1774021274 243 SVVD 246
Cdd:cd05331   234 LVVD 237
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-176 7.42e-31

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 114.87  E-value: 7.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKGIHTQ--KLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK05653    4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAealaAELRAAGGEARvlVFDVSDEAAVRALIEAAVEAFGAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK05653   84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIG 163

                         170       180
                  ....*....|....*....|....*...
gi 1774021274 155 WSDVLDSEVKRFGIR------SIIDQPG 176
Cdd:PRK05653  164 FTKALALELASRGITvnavapGFIDTDM 191
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-169 1.13e-30

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 114.40  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK----GIHT--QKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07666    8 KNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEveayGVKVviATADVSDYEEVTAAIEQLKNELGSIDI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK07666   88 LINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLT 167

                         170
                  ....*....|...
gi 1774021274 157 DVLDSEVKRFGIR 169
Cdd:PRK07666  168 ESLMQEVRKHNIR 180
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 7-181 1.80e-30

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: 113.70  E-value: 1.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   7 ITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLR-EKG---IHTQKLDVTDKFSIRQ-LVDRTVSEQGRIDVLINNA 81
Cdd:cd08931     5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAaELGaenVVAGALDVTDRAAWAAaLADFAAATGGRLDALFNNA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  82 GYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDS 161
Cdd:cd08931    85 GVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEALDV 164

                         170       180
                  ....*....|....*....|....*.
gi 1774021274 162 EVKRFGIR------SIIDQPGLTKSE 181
Cdd:cd08931   165 EWARHGIRvadvwpWFVDTPILTKGE 190
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 3-193 2.73e-30

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: 113.50  E-value: 2.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKGIHT-QKL-----DVTDKFSIRQLVDRTVSEQG 72
Cdd:cd08939     2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLeeavEEIEAEANASgQKVsyisaDLSDYEEVEQAFAQAVEKGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANV----YSPlggwYHAT 148
Cdd:cd08939    82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVgiygYSA----YCPS 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774021274 149 KASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEwskiGFENARKN 193
Cdd:cd08939   158 KFALRGLAESLRQELKPYNIRVSVVYPPDTDTP----GFEEENKT 198
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 3-178 8.64e-30

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 112.28  E-value: 8.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRekgIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAG 82
Cdd:PRK08220    9 KTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP---FATFVLDVSDAAAVAQVCQRLLAETGPLDVLVNAAG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  83 YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDSE 162
Cdd:PRK08220   86 ILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKCVGLE 165

                         170
                  ....*....|....*.
gi 1774021274 163 VKRFGIRSIIDQPGLT 178
Cdd:PRK08220  166 LAPYGVRCNVVSPGST 181
PRK08267 PRK08267
SDR family oxidoreductase;
7-266 1.17e-29

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 112.34  E-value: 1.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   7 ITGISSGMGRAAALYFKQQGFEV--Y----GGARRVERltDLREKGIHTQKLDVTDKFSIRQ-LVDRTVSEQGRIDVLIN 79
Cdd:PRK08267    6 ITGAASGIGRATALLFAAEGWRVgaYdineAGLAALAA--ELGAGNAWTGALDVTDRAAWDAaLADFAAATGGRLDVLFN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVL 159
Cdd:PRK08267   84 NAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEAL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 160 DSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKNSLDNspydelvdkveklfskLGTGATSEDLAQVFYHAATdaHPKR- 238
Cdd:PRK08267  164 DLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTKR----------------LGVRLTPEDVAEAVWAAVQ--HPTRl 225

                         250       260
                  ....*....|....*....|....*...
gi 1774021274 239 RYYNSVVDHRMVMIARTMPNTYRIVLNK 266
Cdd:PRK08267  226 HWPVGKQAKLLAFLARLSPGFVRRLINK 253
PRK05650 PRK05650
SDR family oxidoreductase;
7-228 1.32e-29

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 112.44  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   7 ITGISSGMGRAAALYFKQQGFEVYGG----ARRVERLTDLREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINN 80
Cdd:PRK05650    5 ITGAASGLGRAIALRWAREGWRLALAdvneEGGEETLKLLREAGgdGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVNN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  81 AGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLD 160
Cdd:PRK05650   85 AGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETLL 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 161 SEVKRFGIRSIIDQPGLTKSewskigfenarkNSLDN--SPYDELVDKVEKLFSKlgTGATSEDLAQVFY 228
Cdd:PRK05650  165 VELADDEIGVHVVCPSFFQT------------NLLDSfrGPNPAMKAQVGKLLEK--SPITAADIADYIY 220
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 3-196 1.33e-29

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: 111.54  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL----REKG---IHTQKLDVTDKFSIRQLVdRTVSEQGRID 75
Cdd:cd05356     2 TWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVakeiEEKYgveTKTIAADFSAGDDIYERI-EKELEGLDIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEY--GPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:cd05356    81 ILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIgfenaRKNSLD 196
Cdd:cd05356   161 FFSRALYEEYKSQGIDVQSLLPYLVATKMSKI-----RKSSLF 198
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-181 2.43e-29

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 111.01  E-value: 2.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEV-------YGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK12824    1 MKKIALVTGAKRGIGSAIARELLNDGYRViatyfsgNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:PRK12824   81 VDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMI 160

                         170       180
                  ....*....|....*....|....*...
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK12824  161 GFTKALASEGARYGITVNCIAPGYIATP 188
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 3-169 4.25e-29

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


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 110.53  E-value: 4.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLtDLREKGIHTQ-------KLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05347     6 KVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKA-EEAQQLIEKEgveatafTCDVSDEEAIKAAVEAIEEDFGKID 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:cd05347    85 ILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAGL 164

                         170
                  ....*....|....
gi 1774021274 156 SDVLDSEVKRFGIR 169
Cdd:cd05347   165 TKALATEWARHGIQ 178
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 3-234 4.36e-29

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 110.45  E-value: 4.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD----LREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK12939    8 KRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARElaaaLEAAGgrAHAIAADLADPASVQRFFDAAAAALGGLDG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK12939   88 LVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMT 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSEwskiGFENArknsldnsPYDELVDKVEKLfSKLGTGATSEDLAQVFYHAATDA 234
Cdd:PRK12939  168 RSLARELGGRGITVNAIAPGLTATE----ATAYV--------PADERHAYYLKG-RALERLQVPDDVAGAVLFLLSDA 232
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 3-240 1.43e-28

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: 109.47  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYF---KQQGFEVYG-------GARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTvsEQG 72
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLasdPSKRFKVYAtmrdlkkKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERV--TER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:cd09806    79 HVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKnSLDNSPYDELVDKVEKLFSKLGT------GATSEDLAQV 226
Cdd:cd09806   159 EGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEE-VLDRTADDITTFHFFYQYLAHSKqvfreaAQNPEEVAEV 237

                         250
                  ....*....|....
gi 1774021274 227 FYHAATDAHPKRRY 240
Cdd:cd09806   238 FLTAIRAPKPPLRY 251
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 4-181 2.73e-28

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: 108.10  E-value: 2.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEVY------GGArrVERLTDLREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVildineKGA--EETANNVRKAGgkVHYYKCDVSKREEVYEAAKKIKKEVGDVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:cd05339    79 ILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGF 158

                         170       180
                  ....*....|....*....|....*....
gi 1774021274 156 SDVLDSEVKRF---GIRSIIDQPGLTKSE 181
Cdd:cd05339   159 HESLRLELKAYgkpGIKTTLVCPYFINTG 187
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 3-181 4.42e-28

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 107.59  E-value: 4.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD-----LREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK05557    6 KVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEalvaeIGALGgkALAVQGDVSDAESVERAVDEAKAEFGGVD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:PRK05557   86 ILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVIGF 165

                         170       180
                  ....*....|....*....|....*.
gi 1774021274 156 SDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK05557  166 TKSLARELASRGITVNAVAPGFIETD 191
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 3-169 4.85e-28

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: 107.88  E-value: 4.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLR----EKGIHTQKL-----DVTDKFSIRQLVDRTVSEQGR 73
Cdd:cd05364     4 KVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRqsclQAGVSEKKIllvvaDLTEEEGQDRIISTTLAKFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRqNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:cd05364    84 LDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIK-TKGEIVNVSSVAGGRSFPGVLYYCISKAALD 162

                         170
                  ....*....|....*.
gi 1774021274 154 MWSDVLDSEVKRFGIR 169
Cdd:cd05364   163 QFTRCTALELAPKGVR 178
PRK07775 PRK07775
SDR family oxidoreductase;
3-191 5.05e-28

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 108.30  E-value: 5.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK---------GIHtqkLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK07775   11 RPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKiradggeavAFP---LDVTDPDSVKSFVAQAEEALGE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:PRK07775   88 IEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLE 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKS----------------EWSKIGFenAR 191
Cdd:PRK07775  168 AMVTNLQMELEGTGVRASIVHPGPTLTgmgwslpaevigpmleDWAKWGQ--AR 219
PRK07201 PRK07201
SDR family oxidoreductase;
3-163 5.32e-28

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 112.35  E-value: 5.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL----REKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07201  372 KVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELvaeiRAKGgtAHAYTCDLTDSAAVDHTVKDILAEHGHVDY 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAG----------YGEYGPLEEVpienakkqFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYH 146
Cdd:PRK07201  452 LVNNAGrsirrsvensTDRFHDYERT--------MAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPRFSAYV 523

                         170
                  ....*....|....*..
gi 1774021274 147 ATKASLNMWSDVLDSEV 163
Cdd:PRK07201  524 ASKAALDAFSDVAASET 540
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 3-169 1.03e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 106.97  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL----REKGIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07890    6 KVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVaaeiDDLGRRALAVptDITDEDQCANLVALALERFGRVDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNA-GYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNsGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:PRK07890   86 LVNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPKYGAYKMAKGALLAA 164

                         170
                  ....*....|....
gi 1774021274 156 SDVLDSEVKRFGIR 169
Cdd:PRK07890  165 SQSLATELGPQGIR 178
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-169 2.04e-27

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: 105.94  E-value: 2.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVY------GGARRVERltDLREKGIHTQkLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd05345     4 EGKVAIVTGAGSGFGEGIARRFAQEGARVViadinaDGAERVAA--DIGEAAIAIQ-ADVTKRADVEAMVEAALSKFGRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEY-GPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:cd05345    81 DILVNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVV 160

                         170
                  ....*....|....*.
gi 1774021274 154 MWSDVLDSEVKRFGIR 169
Cdd:cd05345   161 TATKAMAVELAPRNIR 176
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 5-184 2.78e-27

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: 105.46  E-value: 2.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRA-AALYFKQQGFEVYGGARRVERLTDLREKG-----IHTQKLDVTDKF--SIRQLVDRTvsEQGRIDV 76
Cdd:cd05325     1 VLITGASRGIGLElVRQLLARGNNTVIATCRDPSAATELAALGashsrLHILELDVTDEIaeSAEAVAERL--GDAGLDV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAG-YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVS----SIGANvysPLGGW--YHATK 149
Cdd:cd05325    79 LINNAGiLHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISsrvgSIGDN---TSGGWysYRASK 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1774021274 150 ASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSK 184
Cdd:cd05325   156 AALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGG 190
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 3-242 4.43e-27

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: 105.77  E-value: 4.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVER----LTDLREKG----IHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd05327     2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKgeeaAAEIKKETgnakVEVIQLDLSSLASVRQFAEEFLARFPRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEygPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIG------------ANVYSPLG 142
Cdd:cd05327    82 DILINNAGIMA--PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAhragpidfndldLENNKEYS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 143 GW--YHATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSewskigfenarkNSLDNSPYDELVDKVEKLFSKLgtgaTS 220
Cdd:cd05327   160 PYkaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRT------------ELLRRNGSFFLLYKLLRPFLKK----SP 223

                         250       260
                  ....*....|....*....|....*
gi 1774021274 221 EDLAQVFYHAATD---AHPKRRYYN 242
Cdd:cd05327   224 EQGAQTALYAATSpelEGVSGKYFS 248
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 3-181 8.58e-27

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 104.28  E-value: 8.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV---YGGARR-----VERLTDLREKGIHTQKlDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd05362     4 KVALVTGASRGIGRAIAKRLARDGASVvvnYASSKAaaeevVAEIEAAGGKAIAVQA-DVSDPSQVARLFDAAEKAFGGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRqnSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:cd05362    83 DILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRD--GGRIINISSSLTAAYTPNYGAYAGSKAAVEA 160

                         170       180
                  ....*....|....*....|....*..
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:cd05362   161 FTRVLAKELGGRGITVNAVAPGPVDTD 187
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 3-241 9.69e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 106.16  E-value: 9.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLT----DLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07109    9 QVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEalaaEIRAAGGEALAVvaDVADAEAVQAAADRAEEELGPIDT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK07109   89 WVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 157 DVLDSEV--KRFGIR-SIIDQPGLTKSEwskigFENARkNSLDNSP------YD-ELVdkveklfsklgtgatsedlAQV 226
Cdd:PRK07109  169 DSLRCELlhDGSPVSvTMVQPPAVNTPQ-----FDWAR-SRLPVEPqpvppiYQpEVV-------------------ADA 223

                         250
                  ....*....|....*
gi 1774021274 227 FYHAAtdAHPKRRYY 241
Cdd:PRK07109  224 ILYAA--EHPRRELW 236
PRK06181 PRK06181
SDR family oxidoreductase;
3-232 9.69e-27

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 104.68  E-value: 9.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE--KGIHTQKL----DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK06181    2 KVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQelADHGGEALvvptDVSDAEACERLIEAAVARFGGIDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVP-IENAKKQFDVNLFAVGQLTQLVLPVMrRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:PRK06181   82 LVNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHL-KASRGQIVVVSSLAGLTGVPTRSGYAASKHALHGF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274 156 SDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFeNARKNSLDNSPYDElvDKVeklfsklgtgATSEDLAQVFYHAAT 232
Cdd:PRK06181  161 FDSLRIELADDGVAVTVVCPGFVATDIRKRAL-DGDGKPLGKSPMQE--SKI----------MSAEECAEAILPAIA 224
PRK12743 PRK12743
SDR family oxidoreductase;
1-168 1.00e-26

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 104.35  E-value: 1.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVyG--------GARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQG 72
Cdd:PRK12743    1 MAQVAIVTASDSGIGKACALLLAQQGFDI-GitwhsdeeGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQ-NSGRIINVSSIGANVYSPLGGWYHATKAS 151
Cdd:PRK12743   80 RIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAAKHA 159

                         170
                  ....*....|....*..
gi 1774021274 152 LNMWSDVLDSEVKRFGI 168
Cdd:PRK12743  160 LGGLTKAMALELVEHGI 176
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 5-183 1.69e-26

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: 102.97  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGAR---RVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNA 81
Cdd:cd08929     3 ALVTGASRGIGEATARLLHAEGYRVGICARdeaRLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  82 GYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSI-GANVYSPlGGWYHATKASLNMWSDVLD 160
Cdd:cd08929    83 GVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLaGKNAFKG-GAAYNASKFGLLGLSEAAM 161

                         170       180
                  ....*....|....*....|...
gi 1774021274 161 SEVKRFGIRSIIDQPGLTKSEWS 183
Cdd:cd08929   162 LDLREANIRVVNVMPGSVDTGFA 184
PRK06138 PRK06138
SDR family oxidoreductase;
3-234 2.74e-26

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 103.31  E-value: 2.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV----YGGARRVERLTDLREKG-IHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK06138    6 RVAIVTGAGSGIGRATAKLFAREGARVvvadRDAEAAERVAAAIAAGGrAFARQGDVGSAEAVEALVDFVAARWGRLDVL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSD 157
Cdd:PRK06138   86 VNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIASLTR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 158 VLDSEVKRFGIR------SIIDQPGLTKsewskigfenarknSLDNSPYDELVDKVEKLFSKLGTGATSEDLAQVFYHAA 231
Cdd:PRK06138  166 AMALDHATDGIRvnavapGTIDTPYFRR--------------IFARHADPEALREALRARHPMNRFGTAEEVAQAALFLA 231


                  ...
gi 1774021274 232 TDA 234
Cdd:PRK06138  232 SDE 234
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 2-237 2.81e-26

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: 103.24  E-value: 2.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   2 TRVAIITGISSGMGRAAALYFKQQGFEVYG------GARRVERLTDLREKGIhTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd08943     1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVadidpeIAEKVAEAAQGGPRAL-GVQCDVTSEAQVQSAFEQAVLEFGGLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN-SGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:cd08943    80 IVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNAVAPGPNAAAYSAAKAAEAH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPG--LTKSEWSKIGFENARKNSldnspYDELVDKVeKLFSKLGTGATSEDLAQVFYHAAT 232
Cdd:cd08943   160 LARCLALEGGEDGIRVNTVNPDavFRGSKIWEGVWRAARAKA-----YGLLEEEY-RTRNLLKREVLPEDVAEAVVAMAS 233


                  ....*
gi 1774021274 233 DAHPK 237
Cdd:cd08943   234 EDFGK 238
PRK07326 PRK07326
SDR family oxidoreductase;
3-176 4.60e-26

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 102.01  E-value: 4.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD----LREKG-IHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK07326    7 KVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEaaaeLNNKGnVLGLAADVRDEADVQRAVDAIVAAFGGLDVL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRqNSGRIINVSSI-GANVYsPLGGWYHATKASLNMWS 156
Cdd:PRK07326   87 IANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKR-GGGYIINISSLaGTNFF-AGGAAYNASKFGLVGFS 164

                         170       180
                  ....*....|....*....|
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK07326  165 EAAMLDLRQYGIKVSTIMPG 184
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 1-234 6.61e-26

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: 102.07  E-value: 6.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQ-------KLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:cd05366     1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAgynavavGADVTDKDDVEALIDQAVEKFGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN-SGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:cd05366    81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASKFAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPGLTKSE-WSKIGFENARknsLDNSPYDELVDKVEKLFsKLGTGATSEDLAQ-VFYHA 230
Cdd:cd05366   161 RGLTQTAAQELAPKGITVNAYAPGIVKTEmWDYIDEEVGE---IAGKPEGEGFAEFSSSI-PLGRLSEPEDVAGlVSFLA 236


                  ....
gi 1774021274 231 ATDA 234
Cdd:cd05366   237 SEDS 240
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 3-181 6.67e-26

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: 101.86  E-value: 6.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE------KGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEeikalgGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:cd05333    81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160

                         170       180
                  ....*....|....*....|....*
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:cd05333   161 KSLAKELASRGITVNAVAPGFIDTD 185
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 3-176 7.19e-26

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 102.27  E-value: 7.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY------GGARRVERltDLREKGIHTQ--KLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK12429    5 KVALVTGAASGIGLEIALALAKEGAKVViadlndEAAAAAAE--ALQKAGGKAIgvAMDVTDEEAINAGIDYAVETFGGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK12429   83 DILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIG 162

                         170       180
                  ....*....|....*....|..
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK12429  163 LTKVVALEGATHGVTVNAICPG 184
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 3-180 1.31e-25

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: 101.31  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLTDlrekGIHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05341     6 KVAIVTGGARGLGLAHARLLVAEGAKVVlsdildeEGQAAAAELGD----AARFFHLDVTDEDGWTAVVDTAREAFGRLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:cd05341    82 VLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGL 161

                         170       180
                  ....*....|....*....|....*....
gi 1774021274 156 --SDVLDSEVKRFGIR--SIidQPGLTKS 180
Cdd:cd05341   162 tkSAALECATQGYGIRvnSV--HPGYIYT 188
PRK08264 PRK08264
SDR family oxidoreductase;
3-156 1.37e-25

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 100.73  E-value: 1.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQG-FEVYGGARRVERLTDLREkGIHTQKLDVTDKFSIRQLVDRTvseqGRIDVLINNA 81
Cdd:PRK08264    7 KVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDLGP-RVVPLQLDVTDPASVAAAAEAA----SDVTILVNNA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774021274  82 GYGE-YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLnmWS 156
Cdd:PRK08264   82 GIFRtGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAA--WS 155
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 3-233 3.46e-25

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: 99.85  E-value: 3.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL-REKGIHTQKLDVTDKfsirQLVDRTVSEQGRIDVLINNA 81
Cdd:cd05368     3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELeRGPGITTRVLDVTDK----EQVAALAKEEGRIDVLFNCA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  82 GYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGW-YHATKASLNMWSDVLD 160
Cdd:cd05368    79 GFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRFvYSTTKAAVIGLTKSVA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274 161 SEVKRFGIR------SIIDQPGLTKSEWSKIGFENARKNSLDNSPydelvdkveklfskLGTGATSEDLAQVFYHAATD 233
Cdd:cd05368   159 ADFAQQGIRcnaicpGTVDTPSLEERIQAQPDPEEALKAFAARQP--------------LGRLATPEEVAALAVYLASD 223
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 3-234 4.06e-25

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: 99.68  E-value: 4.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARR--VERLTDLREK----GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNenPGAAAELQAInpkvKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAG------YGEYGPLEevpiENAKKQFDVNLFAVGQLTQLVLPVMRRQNS---GRIINVSSIGANVYSPLGGWYHA 147
Cdd:cd05323    81 LINNAGildeksYLFAGKLP----PPWEKTIDVNLTGVINTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAPQFPVYSA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 148 TKASLNMWSDVL-DSEVKRFGIRSIIDQPGLTKSEwskigfenarknsLDNspydELVDKVEKLFSKLGTgATSEDLAQV 226
Cdd:cd05323   157 SKHGVVGFTRSLaDLLEYKTGVRVNAICPGFTNTP-------------LLP----DLVAKEAEMLPSAPT-QSPEVVAKA 218


                  ....*...
gi 1774021274 227 FYHAATDA 234
Cdd:cd05323   219 IVYLIEDD 226
PRK07774 PRK07774
SDR family oxidoreductase;
3-181 4.45e-25

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 99.82  E-value: 4.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLTDLREKGIHTQkLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK07774    7 KVAIVTGAAGGIGQAYAEALAREGASVVvadinaeGAERVAKQIVADGGTAIAVQ-VDVSDPDSAKAMADATVSAFGGID 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAG-YGEY--GPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSplgGWYHATKASL 152
Cdd:PRK07774   86 YLVNNAAiYGGMklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYS---NFYGLAKVGL 162

                         170       180
                  ....*....|....*....|....*....
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK07774  163 NGLTQQLARELGGMNIRVNAIAPGPIDTE 191
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
3-176 6.75e-25

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 99.87  E-value: 6.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGAR--RVERLTD-LREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK08226    7 KTALITGALQGIGEGIARVFARHGANLILLDIspEIEKLADeLCGRGhrCTAVVADVRDPASVAAAIKRAKEKEGRIDIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSI-GANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK08226   87 VNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVtGDMVADPGETAYALTKAAIVGLT 166

                         170       180
                  ....*....|....*....|
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK08226  167 KSLAVEYAQSGIRVNAICPG 186
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 5-234 6.94e-25

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: 99.35  E-value: 6.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARR-----VERLTDLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVINYRKskdaaAEVAAEIEELGGKAVVVraDVSQPQDVEEMFAAVKERFGRLDVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPlgGWYH--ATKASLNMW 155
Cdd:cd05359    81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALP--NYLAvgTAKAALEAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 156 SDVLDSEVKRFGIRSIIDQPGLTKSEWSKI--GFENARKNSLDNSPydelvdkveklfskLGTGATSEDLAQVFYHAATD 233
Cdd:cd05359   159 VRYLAVELGPRGIRVNAVSPGVIDTDALAHfpNREDLLEAAAANTP--------------AGRVGTPQDVADAVGFLCSD 224


                  .
gi 1774021274 234 A 234
Cdd:cd05359   225 A 225
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 3-179 7.56e-25

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: 99.00  E-value: 7.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARR---------------VERLTDL-REKG--IHTQKLDVTDKFSIRQLV 64
Cdd:cd05338     4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKTasegdngsakslpgtIEETAEEiEAAGgqALPIVVDVRDEDQVRALV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  65 DRTVSEQGRIDVLINNAGYGEYGPLEEVPIenakKQFD----VNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSP 140
Cdd:cd05338    84 EATVDQFGRLDILVNNAGAIWLSLVEDTPA----KRFDlmqrVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPAR 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1774021274 141 LGGWYHATKASLNMWSDVLDSEVKRFGI-------RSIIDQPGLTK 179
Cdd:cd05338   160 GDVAYAAGKAGMSRLTLGLAAELRRHGIavnslwpSTAIETPAATE 205
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 4-177 1.14e-24

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 98.51  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGF--EVYGGARRVERLTDLREKG-----IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEELrpglrVTTVKADLSDAAGVEQLLEAIRKLDGERDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAG-YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMR-RQNSGRIINVSSIGANvySPLGGW--YHATKASL 152
Cdd:cd05367    81 LINNAGsLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKkRGLKKTVVNVSSGAAV--NPFKGWglYCSSKAAR 158

                         170       180
                  ....*....|....*....|....*
gi 1774021274 153 NMWSDVLDSEVKrfGIRSIIDQPGL 177
Cdd:cd05367   159 DMFFRVLAAEEP--DVRVLSYAPGV 181
PRK06124 PRK06124
SDR family oxidoreductase;
3-176 2.22e-24

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 98.25  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK06124   12 QVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLeaavAALRAAGGAAEALafDIADEEAVAAAFARIDAEHGRLDI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK06124   92 LVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTGLM 171

                         170       180
                  ....*....|....*....|
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK06124  172 RALAAEFGPHGITSNAIAPG 191
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 3-175 2.32e-24

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 97.56  E-value: 2.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV----YGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:PRK12828    8 KVVAITGGFGGLGRATAAWLAARGARValigRGAAPLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFGRLDALV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDV 158
Cdd:PRK12828   88 NIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTEA 167

                         170       180
                  ....*....|....*....|...
gi 1774021274 159 LDSEVKRFGIR------SIIDQP 175
Cdd:PRK12828  168 LAAELLDRGITvnavlpSIIDTP 190
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 1-149 2.78e-24

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 97.90  E-value: 2.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEV----YGGARRVERLTD--LREKGIHTQKL--DVTDKFSIRQLVDRTVSEQG 72
Cdd:cd08940     1 KGKVALVTGSTSGIGLGIARALAAAGANIvlngFGDAAEIEAVRAglAAKHGVKVLYHgaDLSKPAAIEDMVAYAQRQFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATK 149
Cdd:cd08940    81 GVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAK 157
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
2-237 3.33e-24

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 101.46  E-value: 3.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   2 TRVAIITGISSGMGRAAALYFKQQGFEV------YGGARRVERLTDLREKGIhTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK08324  422 GKVALVTGAAGGIGKATAKRLAAEGACVvladldEEAAEAAAAELGGPDRAL-GVACDVTDEAAVQAAFEEAALAFGGVD 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNS-GRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK08324  501 IVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASKNAVNPGPNFGAYGAAKAAELH 580

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 155 WSDVLDSEVKRFGIRS-------IIDQPGLTKSEWSKigfENARKNSLDnspydelVDKVEKLFSK---LGTGATSEDLA 224
Cdd:PRK08324  581 LVRQLALELGPDGIRVngvnpdaVVRGSGIWTGEWIE---ARAAAYGLS-------EEELEEFYRArnlLKREVTPEDVA 650

                         250
                  ....*....|...
gi 1774021274 225 QVFYHAATDAHPK 237
Cdd:PRK08324  651 EAVVFLASGLLSK 663
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 3-211 3.39e-24

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: 97.09  E-value: 3.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYF-KQQGFEVYGGARRVERLTDLREK---GIHTQKLDVTDKFSIRQLVDrTVSEqgrIDVLI 78
Cdd:cd05354     4 KTVLVTGANRGIGKAFVESLlAHGAKKVYAAVRDPGSAAHLVAKygdKVVPLRLDVTDPESIKAAAA-QAKD---VDVVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAGYGE-YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSD 157
Cdd:cd05354    80 NNAGVLKpATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLTQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1774021274 158 VLDSEVKRFGIRSIIDQPGLTKSEW-SKIGFENARKNSLDNSPYDELVDKVEKLF 211
Cdd:cd05354   160 GLRAELAAQGTLVLSVHPGPIDTRMaAGAGGPKESPETVAEAVLKALKAGEFHVF 214
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 3-169 3.75e-24

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 97.71  E-value: 3.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK----GIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK08213   13 KTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHlealGIDALWIaaDVADEADIERLAEETLERFGHVDI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPV-MRRQNSGRIINVSSIGAnvyspLGG---------WYH 146
Cdd:PRK08213   93 LVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAG-----LGGnppevmdtiAYN 167

                         170       180
                  ....*....|....*....|....
gi 1774021274 147 ATK-ASLNMWSDvLDSEVKRFGIR 169
Cdd:PRK08213  168 TSKgAVINFTRA-LAAEWGPHGIR 190
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 3-189 3.82e-24

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: 97.58  E-value: 3.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLR----EKG---IHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05343     7 RVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAaecqSAGyptLFPYQCDLSNEEQILSMFSAIRTQHQGVD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN--SGRIINVSSIGANVY--SPLGGWYHATKAS 151
Cdd:cd05343    87 VCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGHRVppVSVFHFYAATKHA 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1774021274 152 LNMWSDVLDSEV--KRFGIRSIIDQPGLTKSEWSKIGFEN 189
Cdd:cd05343   167 VTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDN 206
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-149 4.05e-24

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 96.96  E-value: 4.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGgarrverlTDLREKGI-----HTQKLDVTDKfsirqlVDRTVSEQGRID 75
Cdd:PRK06550    4 MTKTVLITGAASGIGLAQARAFLAQGAQVYG--------VDKQDKPDlsgnfHFLQLDLSDD------LEPLFDWVPSVD 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774021274  76 VLINNAG-YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATK 149
Cdd:PRK06550   70 ILCNTAGiLDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASK 144
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 3-169 9.50e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 96.54  E-value: 9.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL----REKGIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07478    7 KVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLvaeiRAEGGEAVALagDVRDEAYAKALVALAVERFGGLDI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAG-YGEYGPLEEVPIENAKKQFDVNLFA--VGQLTQlvLPVMRRQNSGRIINVSS-IGANVYSPLGGWYHATKASL 152
Cdd:PRK07478   87 AFNNAGtLGEMGPVAEMSLEGWRETLATNLTSafLGAKHQ--IPAMLARGGGSLIFTSTfVGHTAGFPGMAAYAASKAGL 164

                         170
                  ....*....|....*..
gi 1774021274 153 NMWSDVLDSEVKRFGIR 169
Cdd:PRK07478  165 IGLTQVLAAEYGAQGIR 181
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 3-181 9.69e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 96.67  E-value: 9.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:PRK12829   12 LRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALaataARLPGAKVTATVADVADPAQVERVFDTAVERFGGLDVLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAG-YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGR-IINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK12829   92 NNAGiAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAGRLGYPGRTPYAASKWAVVGLV 171

                         170       180
                  ....*....|....*....|....*
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK12829  172 KSLAIELGPLGIRVNAILPGIVRGP 196
PRK05866 PRK05866
SDR family oxidoreductase;
6-170 9.81e-24

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 97.12  E-value: 9.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGI------HTQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:PRK05866   44 LLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITraggdaMAVPCDLSDLDAVDALVADVEKRIGGVDILIN 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEV--PIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIG--ANVySPLGGWYHATKASLNMW 155
Cdd:PRK05866  124 NAGRSIRRPLAESldRWHDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGvlSEA-SPLFSVYNASKAALSAV 202

                         170
                  ....*....|....*
gi 1774021274 156 SDVLDSEVKRFGIRS 170
Cdd:PRK05866  203 SRVIETEWGDRGVHS 217
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 3-169 1.40e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 95.88  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY------GGARRVERLTDLREKGIHtqkLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK06841   16 KVAVVTGGASGIGHAIAELFAAKGARVAlldrseDVAEVAAQLLGGNAKGLV---CDVSDSQSVEAAVAAVISAFGRIDI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK06841   93 LVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGMT 172

                         170
                  ....*....|...
gi 1774021274 157 DVLDSEVKRFGIR 169
Cdd:PRK06841  173 KVLALEWGPYGIT 185
PRK06398 PRK06398
aldose dehydrogenase; Validated
 3-137 1.58e-23

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 96.05  E-value: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRverltDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAG 82
Cdd:PRK06398    7 KVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIK-----EPSYNDVDYFKVDVSNKEQVIKGIDYVISKYGRIDILVNNAG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1774021274  83 YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANV 137
Cdd:PRK06398   82 IESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFA 136
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 3-169 1.79e-23

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: 95.59  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD----LREKGIHTQKL--DVTDKFSIRQLVDrTVSEQ--GRI 74
Cdd:cd05329     7 KTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDEclteWREKGFKVEGSvcDVSSRSERQELMD-TVASHfgGKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:cd05329    86 NILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGALNQ 165

                         170
                  ....*....|....*
gi 1774021274 155 WSDVLDSEVKRFGIR 169
Cdd:cd05329   166 LTRSLACEWAKDNIR 180
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-190 2.24e-23

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: 95.25  E-value: 2.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV-----YGGArrVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:cd08944     4 KVAIVTGAGAGIGAACAARLAREGARVvvadiDGGA--AQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGP-LEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:cd08944    82 VNNAGAMHLTPaIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLT 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1774021274 157 DVLDSEVKRFGIRS------IIDQPgLTKSEWSkiGFENA 190
Cdd:cd08944   162 RTLAAELRHAGIRCnalapgLIDTP-LLLAKLA--GFEGA 198
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 2-234 2.41e-23

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 95.19  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   2 TRVAIITGISSGMGRAAALYFKQQGFEV---YGG--ARRVERLTDLREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK12937    5 NKVAIVTGASRGIGAAIARRLAADGFAVavnYAGsaAAADELVAEIEAAGgrAIAVQADVADAAAVTRLFDAAETAFGRI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRrqNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK12937   85 DVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLG--QGGRIINLSTSVIALPLPGYGPYAASKAAVEG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSEWskigFENARKnsldnspyDELVDKVEKLfSKLGTGATSEDLA-QVFYHAATD 233
Cdd:PRK12937  163 LVHVLANELRGRGITVNAVAPGPVATEL----FFNGKS--------AEQIDQLAGL-APLERLGTPEEIAaAVAFLAGPD 229


                  .
gi 1774021274 234 A 234
Cdd:PRK12937  230 G 230
PRK07856 PRK07856
SDR family oxidoreductase;
3-152 2.54e-23

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 95.39  E-value: 2.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRekGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAG 82
Cdd:PRK07856    7 RVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGR--PAEFHAADVRDPDQVAALVDAIVERHGRLDVLVNNAG 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774021274  83 YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNS-GRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:PRK07856   85 GSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSVSGRRPSPGTAAYGAAKAGL 155
PRK08219 PRK08219
SDR family oxidoreductase;
1-162 2.88e-23

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 94.61  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAA--LyfkQQGFEVYGGARRVERLTDLREK--GIHTQKLDVTDKFSIRQlvdrTVSEQGRIDV 76
Cdd:PRK08219    2 ERPTALITGASRGIGAAIAreL---APTHTLLLGGRPAERLDELAAElpGATPFPVDLTDPEAIAA----AVEQLGRLDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRqNSGRIINVSSiGANVYSPlGGW--YHATKASLNM 154
Cdd:PRK08219   75 LVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRA-AHGHVVFINS-GAGLRAN-PGWgsYAASKFALRA 151


                  ....*...
gi 1774021274 155 WSDVLDSE 162
Cdd:PRK08219  152 LADALREE 159
PRK05855 PRK05855
SDR family oxidoreductase;
3-168 7.39e-23

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 97.36  E-value: 7.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY------GGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK05855  316 KLVVVTGAGSGIGRETALAFAREGAEVVasdideAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDI 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAV-------GQltQLVlpvmRRQNSGRIINVSSIGAnvYSPLGGW--YHA 147
Cdd:PRK05855  396 VVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVihgcrlfGR--QMV----ERGTGGHIVNVASAAA--YAPSRSLpaYAT 467

                         170       180
                  ....*....|....*....|.
gi 1774021274 148 TKASLNMWSDVLDSEVKRFGI 168
Cdd:PRK05855  468 SKAAVLMLSECLRAELAAAGI 488
PRK06139 PRK06139
SDR family oxidoreductase;
3-178 1.07e-22

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 95.17  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL----REKGihTQKL----DVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK06139    8 AVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVaeecRALG--AEVLvvptDVTDADQVKALATQAASFGGRI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLfaVGQL--TQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:PRK06139   86 DVWVNNVGVGAVGRFEETPIEAHEQVIQTNL--IGYMrdAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGL 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774021274 153 NMWSDVLDSEVKRF-GIR------SIIDQPGLT 178
Cdd:PRK06139  164 RGFSEALRGELADHpDIHvcdvypAFMDTPGFR 196
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 4-181 1.70e-22

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: 93.02  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEVY------GGARRVerLTDLREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVViadlksEGAEAV--AAAIQQAGgqAIGLECNVTSEQDLEAVVKATVSQFGGIT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPlEEVPI--ENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:cd05365    79 ILVNNAGGGGPKP-FDMPMteEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVN 157

                         170       180
                  ....*....|....*....|....*...
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:cd05365   158 HMTRNLAFDLGPKGIRVNAVAPGAVKTD 185
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-181 2.01e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 93.08  E-value: 2.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK--GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINN 80
Cdd:PRK07825    6 KVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAElgLVVGGPLDVTDPASFAAFLDAVEADLGPIDVLVNN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  81 AGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLD 160
Cdd:PRK07825   86 AGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGFTDAAR 165

                         170       180
                  ....*....|....*....|..
gi 1774021274 161 SEVKRFGIR-SIIdQPGLTKSE 181
Cdd:PRK07825  166 LELRGTGVHvSVV-LPSFVNTE 186
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 4-235 2.55e-22

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 92.51  E-value: 2.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK---GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINN 80
Cdd:PRK10538    2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDElgdNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  81 AGYG-EYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKA-----SLNM 154
Cdd:PRK10538   82 AGLAlGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAfvrqfSLNL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 155 WSDVLDSEVKRFGIrsiidQPGLTK-SEWSKIGFENarknsldnspyDElvDKVEKLFSKlGTGATSEDLAQ-VFYHAAT 232
Cdd:PRK10538  162 RTDLHGTAVRVTDI-----EPGLVGgTEFSNVRFKG-----------DD--GKAEKTYQN-TVALTPEDVSEaVWWVATL 222


                  ...
gi 1774021274 233 DAH 235
Cdd:PRK10538  223 PAH 225
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-181 3.69e-22

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 92.33  E-value: 3.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARR-----VERLTDLREKGIHTQ--KLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK12745    1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRPddeelAATQQELRALGVEVIffPADVADLSAHEAMLDAAQAAWGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYG--EYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGR------IINVSSIGANVYSPLGGWY 145
Cdd:PRK12745   81 IDCLVNNAGVGvkVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSVNAIMVSPNRGEY 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1774021274 146 HATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK12745  161 CISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTD 196
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 3-183 5.91e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 91.31  E-value: 5.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLR-EKGIHTQKLDVTDKFSIrqlvDRTVSEQGRIDVLINNA 81
Cdd:PRK07060   10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAgETGCEPLRLDVGDDAAI----RAALAAAGAFDGLVNCA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  82 GYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN-SGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLD 160
Cdd:PRK07060   86 GIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGrGGSIVNVSSQAALVGLPDHLAYCASKAALDAITRVLC 165

                         170       180
                  ....*....|....*....|....*...
gi 1774021274 161 SEVKRFGIRSIIDQPGLTKSE-----WS 183
Cdd:PRK07060  166 VELGPHGIRVNSVNPTVTLTPmaaeaWS 193
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-178 7.48e-22

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 91.32  E-value: 7.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKG----------IHTQKLDVTDKFSIRQLVDRTVSE 70
Cdd:PRK12827    5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVaagieaaggkALGLAFDVRDFAATRAALDAGVEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  71 QGRIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQ-LVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATK 149
Cdd:PRK12827   85 FGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQaALPPMIRARRGGRIVNIASVAGVRGNRGQVNYAASK 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1774021274 150 ASLNMWSDVLDSEVKRFGIR------SIIDQPGLT 178
Cdd:PRK12827  165 AGLIGLTKTLANELAPRGITvnavapGAINTPMAD 199
PRK06949 PRK06949
SDR family oxidoreductase;
3-181 1.04e-21

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 90.98  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLR-----EKG-IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK06949   10 KVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRaeieaEGGaAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNL---FAVGQLTQLVLpVMRRQNSG------RIINVSSIGANVYSPLGGWYHA 147
Cdd:PRK06949   90 LVNNSGVSTTQKLVDVTPADFDFVFDTNTrgaFFVAQEVAKRM-IARAKGAGntkpggRIINIASVAGLRVLPQIGLYCM 168

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1774021274 148 TKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK06949  169 SKAAVVHMTRAMALEWGRHGINVNAICPGYIDTE 202
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-245 1.22e-21

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 90.61  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV---YGGARrvERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:PRK06463    8 KVALITGGTRGIGRAIAEAFLREGAKVavlYNSAE--NEAKELREKGVFTIKCDVGNRDQVKKSKEVVEKEFGRVDVLVN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSiGANVYSPLGG--WYHATKASLNMWSD 157
Cdd:PRK06463   86 NAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIAS-NAGIGTAAEGttFYAITKAGIIILTR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 158 VLDSEVKRFGIRSIIDQPGltkseWSKIGFENARKNsldnspyDELVDKVEKLF---SKLGTGATSEDLAQVFYHAATDa 234
Cdd:PRK06463  165 RLAFELGKYGIRVNAVAPG-----WVETDMTLSGKS-------QEEAEKLRELFrnkTVLKTTGKPEDIANIVLFLASD- 231

                         250
                  ....*....|.
gi 1774021274 235 hpKRRYYNSVV 245
Cdd:PRK06463  232 --DARYITGQV 240
PRK09072 PRK09072
SDR family oxidoreductase;
6-169 1.26e-21

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 90.77  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKL-----DVTDkFSIRQLVDRTVSEQGRIDVLINN 80
Cdd:PRK09072    9 LLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHrwvvaDLTS-EAGREAVLARAREMGGINVLINN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  81 AGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSS----IGANVYSPlggwYHATKASLNMWS 156
Cdd:PRK09072   88 AGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGStfgsIGYPGYAS----YCASKFALRGFS 163

                         170
                  ....*....|...
gi 1774021274 157 DVLDSEVKRFGIR 169
Cdd:PRK09072  164 EALRRELADTGVR 176
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 3-200 2.32e-21

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: 90.14  E-value: 2.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV---Y-----GGARRVERLTDLREKGIHTQKlDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd05358     4 KVALVTGASSGIGKAIAIRLATAGANVvvnYrskedAAEEVVEEIKAVGGKAIAVQA-DVSKEEDVVALFQSAIKEFGTL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN-SGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:cd05358    83 DILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSSVHEKIPWPGHVNYAASKGGVK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFEN--ARKNSLDNSPY 200
Cdd:cd05358   163 MMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDpeQRADLLSLIPM 211
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 3-168 2.35e-21

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: 90.29  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLT----DLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:cd08945     4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLAttvkELREAGVEADGRtcDVRSVPEIEALVAAAVARYGPIDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPV--MRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:cd08945    84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVG 163

                         170
                  ....*....|....
gi 1774021274 155 WSDVLDSEVKRFGI 168
Cdd:cd08945   164 FTKALGLELARTGI 177
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 3-168 2.61e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 90.12  E-value: 2.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFE-VYGGARR--VER-LTDLREKGI--HTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07097   11 KIALITGASYGIGFAIAKAYAKAGATiVFNDINQelVDKgLAAYRELGIeaHGYVCDVTDEDGVQAMVSQIEKEVGVIDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIganvYSPLG----GWYHATKASL 152
Cdd:PRK07097   91 LVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSM----MSELGretvSAYAAAKGGL 166

                         170
                  ....*....|....*.
gi 1774021274 153 NMWSDVLDSEVKRFGI 168
Cdd:PRK07097  167 KMLTKNIASEYGEANI 182
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 3-169 2.65e-21

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: 89.84  E-value: 2.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL-RE-KGIHTQKLDVTDkfsiRQLVDRTVSEQGRIDVLINN 80
Cdd:cd05351     8 KRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLvREcPGIEPVCVDLSD----WDATEEALGSVGPVDLLVNN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  81 AGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMR-RQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVL 159
Cdd:cd05351    84 AAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIaRGVPGSIVNVSSQASQRALTNHTVYCSTKAALDMLTKVM 163

                         170
                  ....*....|
gi 1774021274 160 DSEVKRFGIR 169
Cdd:cd05351   164 ALELGPHKIR 173
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-157 2.81e-21

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 89.79  E-value: 2.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGA-----RRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK06935   16 KVAIVTGGNTGLGQGYAVALAKAGADIIITThgtnwDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDIL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSI----GANVYSPLGGWYHA----TK 149
Cdd:PRK06935   96 VNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMlsfqGGKFVPAYTASKHGvaglTK 175


                  ....*...
gi 1774021274 150 ASLNMWSD 157
Cdd:PRK06935  176 AFANELAA 183
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 3-169 2.94e-21

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: 90.04  E-value: 2.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV---Y-----GGARRVERLtdLREKGIH--TQKLDVTDKFSIRQLVDRTVSEQG 72
Cdd:cd05355    27 KKALITGGDSGIGRAVAIAFAREGADVainYlpeeeDDAEETKKL--IEEEGRKclLIPGDLGDESFCRDLVKEVVKEFG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGP-LEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRqnSGRIINVSSIGANVYSPLGGWYHATKAS 151
Cdd:cd05355   105 KLDILVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK--GSSIINTTSVTAYKGSPHLLDYAATKGA 182

                         170
                  ....*....|....*...
gi 1774021274 152 LNMWSDVLDSEVKRFGIR 169
Cdd:cd05355   183 IVAFTRGLSLQLAEKGIR 200
PRK06172 PRK06172
SDR family oxidoreductase;
3-149 6.60e-21

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 88.65  E-value: 6.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRV----ERLTDLREKGIHTQ--KLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK06172    8 KVALVTGGAAGIGRATALAFAREGAKVVVADRDAaggeETVALIREAGGEALfvACDVTRDAEVKALVEQTIAAYGRLDY 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774021274  77 LINNAGY-GEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATK 149
Cdd:PRK06172   88 AFNNAGIeIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASK 161
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 3-246 7.25e-21

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: 88.67  E-value: 7.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV-------YGGARRVERLTDLREKGIHTqklDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05326     5 KVAIITGGASGIGEATARLFAKHGARVviadiddDAGQAVAAELGDPDISFVHC---DVTVEADVRAAVDTAVARFGRLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGY-GEYGP-LEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:cd05326    82 IMFNNAGVlGAPCYsILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFenarknSLDNSPYDELVDkveKLFSKLGTGATSEDLAQ-VFYHAAT 232
Cdd:cd05326   162 GLTRSAATELGEHGIRVNCVSPYGVATPLLTAGF------GVEDEAIEEAVR---GAANLKGTALRPEDIAAaVLYLASD 232

                         250
                  ....*....|....*..
gi 1774021274 233 DAhpkrRY---YNSVVD 246
Cdd:cd05326   233 DS----RYvsgQNLVVD 245
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 3-149 9.67e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 88.29  E-value: 9.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07523   11 RRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLaaaaESLKGQGLSAHALafDVTDHDAVRAAIDAFEAEIGPIDI 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATK 149
Cdd:PRK07523   91 LVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATK 163
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 3-177 2.08e-20

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 87.76  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGarrverltDLREKGIHTQKL-----DVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK06171   10 KIIIVTGGSSGIGLAIVKELLANGANVVNA--------DIHGGDGQHENYqfvptDVSSAEEVNHTVAEIIEKFGRIDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAG-------YGEYGPLEEVPIENA--KKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVS-------SIGANVYSpl 141
Cdd:PRK06171   82 VNNAGiniprllVDEKDPAGKYELNEAafDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSseaglegSEGQSCYA-- 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1774021274 142 ggwyhATKASLNMWSDVLDSEVKRFGIRSIIDQPGL 177
Cdd:PRK06171  160 -----ATKAALNSFTRSWAKELGKHNIRVVGVAPGI 190
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 3-176 3.07e-20

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: 86.77  E-value: 3.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD----LREKG-IHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:cd08942     7 KIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADaaeeLSAYGeCIAIPADLSSEEGIEALVARVAERSDRLDVL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRR----QNSGRIINVSSIGANVYSPLGGW-YHATKASL 152
Cdd:cd08942    87 VNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAaataENPARVINIGSIAGIVVSGLENYsYGASKAAV 166

                         170       180
                  ....*....|....*....|....
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:cd08942   167 HQLTRKLAKELAGEHITVNAIAPG 190
PRK07062 PRK07062
SDR family oxidoreductase;
3-135 3.23e-20

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 87.02  E-value: 3.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD----LREK----GIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK07062    9 RVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASaearLREKfpgaRLLAARCDVLDEADVAAFAAAVEARFGGV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGA 135
Cdd:PRK07062   89 DMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLA 149
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 3-200 3.29e-20

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: 87.00  E-value: 3.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV---YGG-ARRVERLTDLREK-GIHTQ--KLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05352     9 KVAIVTGGSRGIGLAIARALAEAGADVaiiYNSaPRAEEKAEELAKKyGVKTKayKCDVSSQESVEKTFKQIQKDFGKID 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIG---ANVYSPLGGwYHATKASL 152
Cdd:cd05352    89 ILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSgtiVNRPQPQAA-YNASKAAV 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1774021274 153 NMWSDVLDSEVKRFGIR--SIidQPGLTKSEWSKIGFENARKNSLDNSPY 200
Cdd:cd05352   168 IHLAKSLAVEWAKYFIRvnSI--SPGYIDTDLTDFVDKELRKKWESYIPL 215
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
3-150 9.80e-20

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 85.46  E-value: 9.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK---GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:PRK07067    7 KVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEigpAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFN 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774021274  80 NAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVM-RRQNSGRIINVSSIGANVYSPLGGWYHATKA 150
Cdd:PRK07067   87 NAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMvEQGRGGKIINMASQAGRRGEALVSHYCATKA 158
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 1-176 1.12e-19

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: 85.46  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE-------KGIHTQKLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:cd08930     1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEeltnlykNRVIALELDITSKESIKELIESYLEKFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGY---GEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSI------------GANVY 138
Cdd:cd08930    81 IDILINNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIygviapdfriyeNTQMY 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1774021274 139 SPLGgwYHATKASLNMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:cd08930   161 SPVE--YSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 3-245 2.26e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 84.71  E-value: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREK---GIHTQKLDVTDKFSIRQLVdrtvSEQGRID 75
Cdd:PRK06125    8 KRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALealaADLRAAhgvDVAVHALDLSSPEAREQLA----AEAGDID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVssIGANVYSPLGGWY--HATKASLN 153
Cdd:PRK06125   84 ILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV--IGAAGENPDADYIcgSAGNAALM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSE-WSKIGFENARKNSLDNSPYDELVDKVeklfsKLGTGATSEDLAQVFyhaAT 232
Cdd:PRK06125  162 AFTRALGGKSLDDGVRVVGVNPGPVATDrMLTLLKGRARAELGDESRWQELLAGL-----PLGRPATPEEVADLV---AF 233

                         250
                  ....*....|...
gi 1774021274 233 DAHPKRRYYNSVV 245
Cdd:PRK06125  234 LASPRSGYTSGTV 246
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 3-134 2.61e-19

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: 84.49  E-value: 2.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVyggarrveRLTDLREKG----------------IHTQKLDVTDKFSIRQLVDR 66
Cdd:cd05330     4 KVVLITGGGSGLGLATAVRLAKEGAKL--------SLVDLNEEGleaakaalleiapdaeVLLIKADVSDEAQVEAYVDA 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274  67 TVSEQGRIDVLINNAGY-GEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIG 134
Cdd:cd05330    76 TVEQFGRIDGFFNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVG 144
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 3-205 4.42e-19

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: 83.73  E-value: 4.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGgARRVERLTDLREKG------IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:cd08937     5 KVVVVTGAAQGIGRGVAERLAGEGARVLL-VDRSELVHEVLAEIlaagdaAHVHTADLETYAGAQGVVRAAVERFGRVDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYG-PLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGA-NVY-SPlggwYHATKASLN 153
Cdd:cd08937    84 LINNVGGTIWAkPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATrGIYrIP----YSAAKGGVN 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKNSLDNSPYDELVD 205
Cdd:cd08937   160 ALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAPMSEQEKVWYQRIVD 211
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 3-181 4.54e-19

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 83.74  E-value: 4.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLTDLREKGIHTqKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK06113   12 KCAIITGAGAGIGKEIAITFATAGASVVvsdinadAANHVVDEIQQLGGQAFAC-RCDITSEQELSALADFALSKLGKVD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEeVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:PRK06113   91 ILVNNAGGGGPKPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHL 169

                         170       180
                  ....*....|....*....|....*.
gi 1774021274 156 SDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK06113  170 VRNMAFDLGEKNIRVNGIAPGAILTD 195
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-180 5.60e-19

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 83.79  E-value: 5.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY------GGARRV-ERLTDLREKGIHTqKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK13394    8 KTAVVTGAASGIGKEIALELARAGAAVAiadlnqDGANAVaDEINKAGGKAIGV-AMDVTNEDAVNAGIDKVAERFGSVD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRR-QNSGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK13394   87 ILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLG 166

                         170       180
                  ....*....|....*....|....*.
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKS 180
Cdd:PRK13394  167 LARVLAKEGAKHNVRSHVVCPGFVRT 192
PRK07074 PRK07074
SDR family oxidoreductase;
1-192 7.06e-19

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 83.28  E-value: 7.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLT----DLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07074    1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAafadALGDARFVPVACDLTDAASLAAALANAAAERGPVDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSI-GANVYS-PLggwYHATKASLNM 154
Cdd:PRK07074   81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVnGMAALGhPA---YSAAKAGLIH 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSE-WSKIG------FENARK 192
Cdd:PRK07074  158 YTKLLAVEYGRFGIRANAVAPGTVKTQaWEARVaanpqvFEELKK 202
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 3-180 1.18e-18

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 82.51  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARR-----VERLTDLREKGIHTQ--KLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05337     2 PVAIVTGASRGIGRAIATELAARGFDIAINDLPdddqaTEVVAEVLAAGRRAIyfQADIGELSDHEALLDQAWEDFGRLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYG--EYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQ------NSGRIINVSSIGANVYSPLGGWYHA 147
Cdd:cd05337    82 CLVNNAGIAvrPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQpdrfdgPHRSIIFVTSINAYLVSPNRGEYCI 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774021274 148 TKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKS 180
Cdd:cd05337   162 SKAGLSMATRLLAYRLADEGIAVHEIRPGLIHT 194
PRK07063 PRK07063
SDR family oxidoreductase;
3-135 1.45e-18

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 82.41  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLT----DLREKG----IHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK07063    8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAEraaaAIARDVagarVLAVPADVTDAASVAAAVAAAEEAFGPL 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774021274  75 DVLINNAGYGEYG-PLeEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGA 135
Cdd:PRK07063   88 DVLVNNAGINVFAdPL-AMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHA 148
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-152 1.63e-18

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 82.08  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARR-----VERLTDLREKGIHT--QKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK06077    7 KVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKraeemNETLKMVKENGGEGigVLADVSTREGCETLAKATIDRYGVAD 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRrqNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:PRK06077   87 ILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMR--EGGAIVNIASVAGIRPAYGLSIYGAMKAAV 161
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 3-169 3.43e-18

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: 81.74  E-value: 3.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:cd08935     6 KVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGdkvaKEITALGGRAIALaaDVLDRASLERAREEIVAQFGTVDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAG--------------YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIgaNVYSPLG 142
Cdd:cd08935    86 LINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSM--NAFSPLT 163

                         170       180
                  ....*....|....*....|....*....
gi 1774021274 143 --GWYHATKASLNMWSDVLDSEVKRFGIR 169
Cdd:cd08935   164 kvPAYSAAKAAVSNFTQWLAVEFATTGVR 192
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-181 3.90e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 83.75  E-value: 3.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK---GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:PRK06484    6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSlgpDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGE--YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGR-IINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK06484   86 NAGVTDptMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAAVISLT 165

                         170       180
                  ....*....|....*....|....*
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK06484  166 RSLACEWAAKGIRVNAVLPGYVRTQ 190
PRK06128 PRK06128
SDR family oxidoreductase;
3-176 4.35e-18

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 81.83  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY--------GGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK06128   56 RKALITGADSGIGRATAIAFAREGADIAlnylpeeeQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGL 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEY-GPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSgrIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:PRK06128  136 DILVNIAGKQTAvKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGAS--IINTGSIQSYQPSPTLLDYASTKAAIV 213

                         170       180
                  ....*....|....*....|...
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK06128  214 AFTKALAKQVAEKGIRVNAVAPG 236
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-176 4.85e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 83.36  E-value: 4.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE--KGIH-TQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:PRK06484  270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEalGDEHlSVQADITDEAAVESAFAQIQARWGRLDVLVN 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGE-YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRqnSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDV 158
Cdd:PRK06484  350 NAGIAEvFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQ--GGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRS 427

                         170
                  ....*....|....*...
gi 1774021274 159 LDSEVKRFGIRSIIDQPG 176
Cdd:PRK06484  428 LACEWAPAGIRVNTVAPG 445
PRK07069 PRK07069
short chain dehydrogenase; Validated
 5-170 5.11e-18

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 80.91  E-value: 5.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVY--------GGARRVERLTDLREKGI-HTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK07069    2 AFITGAAGGLGRAIARRMAEQGAKVFltdindaaGLDAFAAEINAAHGEGVaFAAVQDVTDEAQWQALLAQAADAMGGLS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:PRK07069   82 VLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASL 161

                         170
                  ....*....|....*..
gi 1774021274 156 SD--VLDSEVKRFGIRS 170
Cdd:PRK07069  162 TKsiALDCARRGLDVRC 178
PRK07035 PRK07035
SDR family oxidoreductase;
3-189 5.43e-18

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 80.83  E-value: 5.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKG-------IHTQKLDvtdkfSIRQLVDRTVSEQ 71
Cdd:PRK07035    9 KIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCqavaDAIVAAGgkaealaCHIGEME-----QIDALFAHIRERH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  72 GRIDVLINNAGYGEY-GPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKA 150
Cdd:PRK07035   84 GRLDILVNNAAANPYfGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKA 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1774021274 151 SLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFEN 189
Cdd:PRK07035  164 AVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKN 202
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 3-176 6.09e-18

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 81.04  E-value: 6.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY------GGARRVERltDLREKGIHTQKL---DVTDKFSIRQLVDRTVSEQGR 73
Cdd:cd08933    10 KVVIVTGGSRGIGRGIVRAFVENGAKVVfcargeAAGQALES--ELNRAGPGSCKFvpcDVTKEEDIKTLISVTVERFGR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYG-EYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMrRQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:cd08933    88 IDCLVNNAGWHpPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHL-RKSQGNIINLSSLVGSIGQKQAAPYVATKGAI 166

                         170       180
                  ....*....|....*....|....
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:cd08933   167 TAMTKALAVDESRYGVRVNCISPG 190
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 3-170 6.38e-18

(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: 80.44  E-value: 6.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLD---------VTDKFSIR---QLVDRTVSE 70
Cdd:cd05353     6 RVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKVVDeikaaggkaVANYDSVEdgeKIVKTAIDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  71 QGRIDVLINNAGYgeygpLEEVPIENAKKQ-----FDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSiGANVYSPLG-GW 144
Cdd:cd05353    86 FGRVDILVNNAGI-----LRDRSFAKMSEEdwdlvMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSS-AAGLYGNFGqAN 159

                         170       180
                  ....*....|....*....|....*.
gi 1774021274 145 YHATKASLNMWSDVLDSEVKRFGIRS 170
Cdd:cd05353   160 YSAAKLGLLGLSNTLAIEGAKYNITC 185
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 3-251 8.33e-18

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: 80.19  E-value: 8.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV----YGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVvvnyYRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNA--GYGEYG----PLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINvssIGANVYSPLGGWYH---ATK 149
Cdd:cd05349    81 NNAliDFPFDPdqrkTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVIN---IGTNLFQNPVVPYHdytTAK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 150 ASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE-WSKIGFENARKNSLDNSPydelvdkveklfskLGTGATSEDLAQ--V 226
Cdd:cd05349   158 AALLGFTRNMAKELGPYGITVNMVSGGLLKVTdASAATPKEVFDAIAQTTP--------------LGKVTTPQDIADavL 223

                         250       260
                  ....*....|....*....|....*...
gi 1774021274 227 FYhaatdAHPKRRYY---NSVVDHRMVM 251
Cdd:cd05349   224 FF-----ASPWARAVtgqNLVVDGGLVM 246
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 5-189 1.04e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 80.18  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARRVER----LTDLREKGI--HTQKLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:PRK08085   12 ILITGSAQGIGFLLATGLAEYGAEIIINDITAERaelaVAKLRQEGIkaHAAPFNVTHKQEVEAAIEHIEKDIGPIDVLI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINV----SSIGANVYSPlggwYHATKASLNM 154
Cdd:PRK08085   92 NNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINIcsmqSELGRDTITP----YAASKGAVKM 167

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1774021274 155 WSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFEN 189
Cdd:PRK08085  168 LTRGMCVELARHNIQVNGIAPGYFKTEMTKALVED 202
PRK07577 PRK07577
SDR family oxidoreductase;
3-152 1.45e-17

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 79.39  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARrverltdlrekgiHTQ-----KLDVTDKFSIRQLVD--RTVSEQGRID 75
Cdd:PRK07577    4 RTVLVTGATKGIGLALSLRLANLGHQVIGIAR-------------SAIddfpgELFACDLADIEQTAAtlAQINEIHPVD 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIgANVYSPLGGWYHATKASL 152
Cdd:PRK07577   71 AIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSR-AIFGALDRTSYSAAKSAL 146
PRK08589 PRK08589
SDR family oxidoreductase;
3-176 2.32e-17

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 79.44  E-value: 2.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGG--ARRVERLTD-LREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK08589    7 KVAVITGASTGIGQASAIALAQEGAYVLAVdiAEAVSETVDkIKSNGgkAKAYHVDISDEQQVKDFASEIKEQFGRVDVL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGY-GEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMrRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK08589   87 FNNAGVdNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLM-MEQGGSIINTSSFSGQAADLYRSGYNAAKGAVINFT 165

                         170       180
                  ....*....|....*....|
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK08589  166 KSIAIEYGRDGIRANAIAPG 185
PRK07832 PRK07832
SDR family oxidoreductase;
5-168 5.78e-17

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 78.16  E-value: 5.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK07832    3 CFVTGAASGIGRATALRLAAQGAELFltdrdadGLAQTVADARALGGTVPEHRALDISDYDAVAAFAADIHAAHGSMDVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQ-LVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK07832   83 MNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIEtFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLRGLS 162

                         170
                  ....*....|..
gi 1774021274 157 DVLDSEVKRFGI 168
Cdd:PRK07832  163 EVLRFDLARHGI 174
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 3-181 5.95e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 78.02  E-value: 5.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRveRLTDLREkGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNAG 82
Cdd:PRK06523   10 KRALVTGGTKGIGAATVARLLEAGARVVTTARS--RPDDLPE-GVEFVAADLTTAEGCAAVARAVLERLGGVDILVHVLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  83 yGEYGPL---EEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANvySPLGG---WYHATKASLNMWS 156
Cdd:PRK06523   87 -GSSAPAggfAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRR--LPLPEsttAYAAAKAALSTYS 163

                         170       180
                  ....*....|....*....|....*
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK06523  164 KSLSKEVAPKGVRVNTVSPGWIETE 188
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-168 6.04e-17

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 77.84  E-value: 6.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEV---YGGARRVERLT--DLREKGIHTQ--KLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK08063    3 SGKVALVTGSSRGIGKAIALRLAEEGYDIavnYARSRKAAEETaeEIEALGRKALavKANVGDVEKIKEMFAQIDEEFGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:PRK08063   83 LDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKAALE 162

                         170
                  ....*....|....*
gi 1774021274 154 MWSDVLDSEVKRFGI 168
Cdd:PRK08063  163 ALTRYLAVELAPKGI 177
PRK06114 PRK06114
SDR family oxidoreductase;
3-178 6.79e-17

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 77.90  E-value: 6.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY--------GGARRVERLTDLREKGIHTQKlDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK06114    9 QVAFVTGAGSGIGQRIAIGLAQAGADVAlfdlrtddGLAETAEHIEAAGRRAIQIAA-DVTSKADLRAAVARTEAELGAL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSP--LGGWYHATKASL 152
Cdd:PRK06114   88 TLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRglLQAHYNASKAGV 167

                         170       180
                  ....*....|....*....|....*.
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPGLT 178
Cdd:PRK06114  168 IHLSKSLAMEWVGRGIRVNSISPGYT 193
PRK08251 PRK08251
SDR family oxidoreductase;
1-181 1.06e-16

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 77.28  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK------GIH--TQKLDVTDKFSIRQLVDRTVSEQG 72
Cdd:PRK08251    1 TRQKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAEllarypGIKvaVAALDVNDHDQVFEVFAEFRDELG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLfaVGQLTQL--VLPVMRRQNSGRIINVSSIGANVYSPLG-GWYHATK 149
Cdd:PRK08251   81 GLDRVIVNAGIGKGARLGTGKFWANKATAETNF--VAALAQCeaAMEIFREQGSGHLVLISSVSAVRGLPGVkAAYAASK 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1774021274 150 ASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK08251  159 AGVASLGEGLRAELAKTPIKVSTIEPGYIRSE 190
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 3-234 1.18e-16

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 76.88  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKgIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:PRK12936    7 RKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLealaAELGER-VKIFPANLSDRDEVKALGQKAEADLEGVDILV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLT-QLVLPVMRRQNsGRIINVSSIGANVYSPLGGWYHATKASLNMWSD 157
Cdd:PRK12936   86 NNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTrELTHPMMRRRY-GRIINITSVVGVTGNPGQANYCASKAGMIGFSK 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274 158 VLDSEVKRFGIRSIIDQPGLtksewskigFENARKNSLDNSPYDELVDKVEklFSKLGTGAtsEDLAQVFYHAATDA 234
Cdd:PRK12936  165 SLAQEIATRNVTVNCVAPGF---------IESAMTGKLNDKQKEAIMGAIP--MKRMGTGA--EVASAVAYLASSEA 228
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 3-169 1.50e-16

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 77.07  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV-------YGGARRVerLTDLREKGIH--TQKLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK08936    8 KVVVITGGSTGLGRAMAVRFGKEKAKVvinyrsdEEEANDV--AEEIKKAGGEaiAVKGDVTVESDVVNLIQTAVKEFGT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN-SGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:PRK08936   86 LDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDiKGNIINMSSVHEQIPWPLFVHYAASKGGV 165

                         170
                  ....*....|....*..
gi 1774021274 153 NMWSDVLDSEVKRFGIR 169
Cdd:PRK08936  166 KLMTETLAMEYAPKGIR 182
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 3-169 2.05e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 76.69  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK--GIHTQkLDVTDKFSIRQLVDRTVSEQGRIDVLINN 80
Cdd:PRK06057    8 RVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEvgGLFVP-TDVTDEDAVNALFDTAAETYGSVDIAFNN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  81 AGYG--EYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGW-YHATKASLNMWSD 157
Cdd:PRK06057   87 AGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQIsYTASKGGVLAMSR 166

                         170
                  ....*....|..
gi 1774021274 158 VLDSEVKRFGIR 169
Cdd:PRK06057  167 ELGVQFARQGIR 178
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 3-234 2.19e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 76.59  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLTDlREKGIHTqklDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK08265    7 KVAIVTGGATLIGAAVARALVAAGARVAivdidadNGAAVAASLGE-RARFIAT---DITDDAAIERAVATVVARFGRVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNA-GYGEYGpleevpIENAKKQ----FDVNLFAVGQLTQLVLPVMRRQnSGRIINVSSIGANVySPLGGW-YHATK 149
Cdd:PRK08265   83 ILVNLAcTYLDDG------LASSRADwlaaLDVNLVSAAMLAQAAHPHLARG-GGAIVNFTSISAKF-AQTGRWlYPASK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 150 ASLNMWSDVLDSEVKRFGIRSIIDQPGLTkseWSKIGFENARKNSldnspydELVDKVEKLFSKLGTGATSEDLAQVFYH 229
Cdd:PRK08265  155 AAIRQLTRSMAMDLAPDGIRVNSVSPGWT---WSRVMDELSGGDR-------AKADRVAAPFHLLGRVGDPEEVAQVVAF 224


                  ....*
gi 1774021274 230 AATDA 234
Cdd:PRK08265  225 LCSDA 229
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
3-176 2.89e-16

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 75.88  E-value: 2.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARR-VERLTDL----REKGIHTQkLDVTDKFSIRQL---VDRTVSEQGRI 74
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTeNKELTKLaeqyNSNLTFHS-LDLQDVHELETNfneILSSIQEDNVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DV-LINNAGYGE-YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMR-RQNSGRIINVSSiGANVYsPLGGW--YHATK 149
Cdd:PRK06924   81 SIhLINNAGMVApIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKdWKVDKRVINISS-GAAKN-PYFGWsaYCSSK 158

                         170       180
                  ....*....|....*....|....*....
gi 1774021274 150 ASLNMWSDVLDSE--VKRFGIRSIIDQPG 176
Cdd:PRK06924  159 AGLDMFTQTVATEqeEEEYPVKIVAFSPG 187
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 3-176 3.20e-16

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: 75.70  E-value: 3.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLT----DLREKG---IHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05369     4 KVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEaaaeEISSATggrAHPIQCDVRDPEAVEAAVDETLKEFGKID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGyGEY-GPLEEVPiENA-KKQFDVNLFAVGQLTQLVLP-VMRRQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:cd05369    84 ILINNAA-GNFlAPAESLS-PNGfKTVIDIDLNGTFNTTKAVGKrLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAGV 161

                         170       180
                  ....*....|....*....|....
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:cd05369   162 DALTRSLAVEWGPYGIRVNAIAPG 185
PRK09242 PRK09242
SDR family oxidoreductase;
3-169 6.12e-16

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 75.17  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKG----IHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK09242   10 QTALITGASKGIGLAIAREFLGLGADVLIVARDADALaqarDELAEEFpereVHGLAADVSDDEDRRAILDWVEDHWDGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYG------EYGPleevpiENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHAT 148
Cdd:PRK09242   90 HILVNNAGGNirkaaiDYTE------DEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMT 163

                         170       180
                  ....*....|....*....|.
gi 1774021274 149 KASLNMWSDVLDSEVKRFGIR 169
Cdd:PRK09242  164 KAALLQMTRNLAVEWAEDGIR 184
PRK07024 PRK07024
SDR family oxidoreductase;
1-176 6.12e-16

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 75.35  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK-----GIHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK07024    1 MPLKVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARlpkaaRVSVYAADVRDADALAAAAADFIAAHGLPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYgEYGPLEEVP--IENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:PRK07024   81 VVIANAGI-SVGTLTEERedLAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAI 159

                         170       180
                  ....*....|....*....|...
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK07024  160 KYLESLRVELRPAGVRVVTIAPG 182
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 3-193 6.29e-16

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: 74.92  E-value: 6.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL---------REKGIHTQKLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:cd05340     5 RIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVadhineeggRQPQWFILDLLTCTSENCQQLAQRIAVNYPR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGY-GEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:cd05340    85 LDGVLHNAGLlGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFAT 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGF--ENARKN 193
Cdd:cd05340   165 EGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFptEDPQKL 207
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 4-169 7.26e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 75.45  E-value: 7.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEV-------YGGA----RRVErltdlrEKGIH--TQKLDVTDKFSIRQLVDRTVSE 70
Cdd:PRK06701   48 VALITGGDSGIGRAVAVLFAKEGADIaivyldeHEDAnetkQRVE------KEGVKclLIPGDVSDEAFCKDAVEETVRE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  71 QGRIDVLINNAGYGEY-GPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSgrIINVSSIGANVYSPLGGWYHATK 149
Cdd:PRK06701  122 LGRLDILVNNAAFQYPqQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQGSA--IINTGSITGYEGNETLIDYSATK 199

                         170       180
                  ....*....|....*....|
gi 1774021274 150 ASLNMWSDVLDSEVKRFGIR 169
Cdd:PRK06701  200 GAIHAFTRSLAQSLVQKGIR 219
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 3-234 8.21e-16

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: 74.96  E-value: 8.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVER---LTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:cd05363     4 KTALITGSARGIGRAFAQAYVREGARVAIADINLEAaraTAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDILVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQ-NSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDV 158
Cdd:cd05363    84 NAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQS 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274 159 LDSEVKRFGIRSIIDQPGLTKSE-WSKIGFENARknsLDNSPYDELVDKVEKLFSkLGTGATSEDL-AQVFYHAATDA 234
Cdd:cd05363   164 AGLNLIRHGINVNAIAPGVVDGEhWDGVDAKFAR---YENRPRGEKKRLVGEAVP-FGRMGRAEDLtGMAIFLASTDA 237
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-199 1.14e-15

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 74.27  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV---YGGARRVER--LTDLREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK12935    7 KVAIVTGGAKGIGKAITVALAQEGAKVvinYNSSKEAAEnlVNELGKEGhdVYAVQADVSKVEDANRLVEEAVNHFGKVD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVysplGGW----YHATKAS 151
Cdd:PRK12935   87 ILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQA----GGFgqtnYSAAKAG 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1774021274 152 LNMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKNSLDNSP 199
Cdd:PRK12935  163 MLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIP 210
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 3-181 1.27e-15

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: 74.41  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARR--------VERLTDLREKGIHTQkLDVTDKFSIRQLVDRTVSE-QGR 73
Cdd:cd09763     4 KIALVTGASRGIGRGIALQLGEAGATVYITGRTilpqlpgtAEEIEARGGKCIPVR-CDHSDDDEVEALFERVAREqQGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAgYGEYG--------PLEEVPIENakkqFDvNLFAVGQLTQLV-----LPVMRRQNSGRIINVSSIGANVYSp 140
Cdd:cd09763    83 LDILVNNA-YAAVQlilvgvakPFWEEPPTI----WD-DINNVGLRAHYAcsvyaAPLMVKAGKGLIVIISSTGGLEYL- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1774021274 141 LGGWYHATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:cd09763   156 FNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTE 196
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 3-195 1.49e-15

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: 74.12  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARR---VER-LTDLREKGI-------HTQKLDVTDKfsirqLVDRTVSEQ 71
Cdd:cd08936    11 KVALVTASTDGIGLAIARRLAQDGAHVVVSSRKqqnVDRaVATLQGEGLsvtgtvcHVGKAEDRER-----LVATAVNLH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  72 GRIDVLINNAGYGEY-GPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGAnvYSPLGGW--YHAT 148
Cdd:cd08936    86 GGVDILVSNAAVNPFfGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAA--FHPFPGLgpYNVS 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1774021274 149 KASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFEN-ARKNSL 195
Cdd:cd08936   164 KTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDkAVEESM 211
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-152 1.68e-15

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 73.97  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEV----YGGARRVERLTD-LREKGIHTQKlDVTDKFSIRQLVDRTVSEQGR-I 74
Cdd:PRK08642    4 SEQTVLVTGGSRGLGAAIARAFAREGARVvvnyHQSEDAAEALADeLGDRAIALQA-DVTDREQVQAMFATATEHFGKpI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNA--GYGEYG----PLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINvssIGANVY-SPLGGW--Y 145
Cdd:PRK08642   83 TTVVNNAlaDFSFDGdarkKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIIN---IGTNLFqNPVVPYhdY 159


                  ....*..
gi 1774021274 146 HATKASL 152
Cdd:PRK08642  160 TTAKAAL 166
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 1-177 1.68e-15

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: 73.86  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHT--QKLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:cd05371     1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGDNCrfVPVDVTSEKDVKAALALAKAKFGRLDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAG-------YGEYGPLeEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQ------NSGRIINVSS-------IGANVY 138
Cdd:cd05371    81 NCAGiavaaktYNKKGQQ-PHSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggERGVIINTASvaafegqIGQAAY 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1774021274 139 SplggwyhATKASLNMWSDVLDSEVKRFGIRSIIDQPGL 177
Cdd:cd05371   160 S-------ASKGGIVGMTLPIARDLAPQGIRVVTIAPGL 191
PRK07985 PRK07985
SDR family oxidoreductase;
3-176 2.25e-15

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 74.26  E-value: 2.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY--------GGARRVERLtdLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQG 72
Cdd:PRK07985   50 RKALVTGGDSGIGRAAAIAYAREGADVAisylpveeEDAQDVKKI--IEECGRKAVLLpgDLSDEKFARSLVHEAHKALG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGP-LEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSgrIINVSSIGANVYSPLGGWYHATKAS 151
Cdd:PRK07985  128 GLDIMALVAGKQVAIPdIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGAS--IITTSSIQAYQPSPHLLDYAATKAA 205

                         170       180
                  ....*....|....*....|....*
gi 1774021274 152 LNMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK07985  206 ILNYSRGLAKQVAEKGIRVNIVAPG 230
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-149 2.35e-15

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 73.61  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEV------YGGARRV-ERLTDLREKGIHTqKLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK08643    1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVaivdynEETAQAAaDKLSKDGGKAIAV-KADVSDRDQVFAAVRQVVDTFGD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN-SGRIINVSSIGANVYSPLGGWYHATK 149
Cdd:PRK08643   80 LNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhGGKIINATSQAGVVGNPELAVYSSTK 156
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 3-196 2.35e-15

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 73.38  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE-KGIHTQ--KLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:cd09761     2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEaEGPNLFfvHGDVADETLVKFVVYAMLEKLGRIDVLVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRqNSGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVL 159
Cdd:cd09761    82 NAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIK-NKGRIINIASTRAFQSEPDSEAYAASKGGLVALTHAL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1774021274 160 DSEVKRFgIRSIIDQPG-LTKSEWSKigFENARKNSLD 196
Cdd:cd09761   161 AMSLGPD-IRVNCISPGwINTTEQQE--FTAAPLTQED 195
PRK06947 PRK06947
SDR family oxidoreductase;
1-181 2.43e-15

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 73.30  E-value: 2.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEV---YGGARRVERLT--DLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK06947    1 MRKVVLITGASRGIGRATAVLAAARGWSVginYARDAAAAEETadAVRAAGGRACVVagDVANEADVIAMFDAVQSAFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAG-YGEYGPLEEVPIENAKKQFDVNL---FAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGW-YHAT 148
Cdd:PRK06947   81 LDALVNNAGiVAPSMPLADMDAARLRRMFDTNVlgaYLCAREAARRLSTDRGGRGGAIVNVSSIASRLGSPNEYVdYAGS 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774021274 149 KASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK06947  161 KGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE 193
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 3-133 3.47e-15

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 73.27  E-value: 3.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVER--------LTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd09807     2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKceeaaaeiRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDRL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774021274  75 DVLINNAGYGE--YGPLEevpiENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSI 133
Cdd:cd09807    82 DVLINNAGVMRcpYSKTE----DGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSL 138
PRK05867 PRK05867
SDR family oxidoreductase;
3-181 3.54e-15

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 73.15  E-value: 3.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK------GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK05867   10 KRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEigtsggKVVPVCCDVSQHQQVTSMLDQVTAELGGIDI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN-SGRIINVSSIGANVYS-PLG-GWYHATKASLN 153
Cdd:PRK05867   90 AVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGqGGVIINTASMSGHIINvPQQvSHYCASKAAVI 169

                         170       180
                  ....*....|....*....|....*...
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK05867  170 HLTKAMAVELAPHKIRVNSVSPGYILTE 197
PRK07814 PRK07814
SDR family oxidoreductase;
3-156 1.04e-14

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 71.73  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD----LREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07814   11 QVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEvaeqIRAAGrrAHVVAADLAHPEATAGLAGQAVEAFGRLDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVM-RRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:PRK07814   91 VVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMlEHSGGGSVINISSTMGRLAGRGFAAYGTAKAALAHY 170


                  .
gi 1774021274 156 S 156
Cdd:PRK07814  171 T 171
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 3-175 2.03e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 71.54  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAA--LYFKqqgfevygGARRVerLTDLREK-------------GIHTQKLDVTDKFSIRQLVDRT 67
Cdd:PRK05872   10 KVVVVTGAARGIGAELArrLHAR--------GAKLA--LVDLEEAelaalaaelggddRVLTVVADVTDLAAMQAAAEEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  68 VSEQGRIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLP-VMRRqnSGRIINVSSIGANVYSPLGGWYH 146
Cdd:PRK05872   80 VERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPaLIER--RGYVLQVSSLAAFAAAPGMAAYC 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1774021274 147 ATKASLNMWSDVLDSEVKRFGIR------SIIDQP 175
Cdd:PRK05872  158 ASKAGVEAFANALRLEVAHHGVTvgsaylSWIDTD 192
PRK06500 PRK06500
SDR family oxidoreductase;
1-233 2.40e-14

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 70.76  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRV----AIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLR-EKGIHTQKL--DVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK06500    1 MSRLqgktALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARaELGESALVIraDAGDVAAQKALAQALAEAFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSgrIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:PRK06500   81 LDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPAS--IVLNGSINAHIGMPNSSVYAASKAALL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTKSE-WSKIGfenarknsLDNSPYDELVDKVEKLFSkLGTGATSEDLAQVFYHAAT 232
Cdd:PRK06500  159 SLAKTLSGELLPRGIRVNAVSPGPVQTPlYGKLG--------LPEATLDAVAAQIQALVP-LGRFGTPEEIAKAVLYLAS 229


                  .
gi 1774021274 233 D 233
Cdd:PRK06500  230 D 230
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 3-169 2.98e-14

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 70.70  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLT----DLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK08277   11 KVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEavvaEIKAAGGEALAVkaDVLDKESLEQARQQILEDFGPCDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAG---------YGEYGPLEEV------PIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGAnvYSPL 141
Cdd:PRK08277   91 LINGAGgnhpkattdNEFHELIEPTktffdlDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNA--FTPL 168

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1774021274 142 ----GgwYHATKASLNMWSDVLDSEVKRFGIR 169
Cdd:PRK08277  169 tkvpA--YSAAKAAISNFTQWLAVHFAKVGIR 198
PRK08177 PRK08177
SDR family oxidoreductase;
3-190 3.23e-14

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 70.06  E-value: 3.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE-KGIHTQKLDVTDKFSIRQLVDRtVSEQgRIDVLINNA 81
Cdd:PRK08177    2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQAlPGVHIEKLDMNDPASLDQLLQR-LQGQ-RFDLLFVNA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  82 GYgeYGPLEEVPIenakkqfDVNLFAVGQL--TQLVLPV--------MRRQNSGRIINVSSIGANVYSPLGG---WYHAT 148
Cdd:PRK08177   80 GI--SGPAHQSAA-------DATAAEIGQLflTNAIAPIrlarrllgQVRPGQGVLAFMSSQLGSVELPDGGempLYKAS 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1774021274 149 KASLNMWSDVLDSEVKR--FGIRSIidQPGLTKSEwskIGFENA 190
Cdd:PRK08177  151 KAALNSMTRSFVAELGEptLTVLSM--HPGWVKTD---MGGDNA 189
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
3-184 3.79e-14

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 70.04  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGA-----RRVERLTDLREKGIH--TQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK12938    4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAGCgpnspRRVKWLEDQKALGFDfiASEGNVGDWDSTKAAFDKVKAEVGEID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMW 155
Cdd:PRK12938   84 VLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIHGF 163

                         170       180
                  ....*....|....*....|....*....
gi 1774021274 156 SDVLDSEVKRFGIRSIIDQPGLTKSEWSK 184
Cdd:PRK12938  164 TMSLAQEVATKGVTVNTVSPGYIGTDMVK 192
PRK07831 PRK07831
SDR family oxidoreductase;
3-150 1.40e-13

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 68.52  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGIS-SGMGRAAALYFKQQGFEVYGGARRVERLTDLREK--------GIHTQKLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK07831   18 KVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADElaaelglgRVEAVVCDVTSEAQVDALIDAAVERLGR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMR-RQNSGRIINVSSIganvysplGGW-------- 144
Cdd:PRK07831   98 LDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRaRGHGGVIVNNASV--------LGWraqhgqah 169


                  ....*.
gi 1774021274 145 YHATKA 150
Cdd:PRK07831  170 YAAAKA 175
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 3-81 2.37e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 67.78  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK------GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK07677    2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEieqfpgQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81


                  ....*
gi 1774021274  77 LINNA 81
Cdd:PRK07677   82 LINNA 86
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 6-135 3.15e-13

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: 67.52  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQGFEVYGgarrverlTDLREKGIHTqklDVTDKFSIRQLVDR-TVSEQGRIDVLINNAGYG 84
Cdd:cd05328     3 VITGAASGIGAATAELLEDAGHTVIG--------IDLREADVIA---DLSTPEGRAAAIADvLARCSGVLDGLVNCAGVG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1774021274  85 EYGPLEEVpienakkqFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGA 135
Cdd:cd05328    72 GTTVAGLV--------LKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAG 114
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-182 6.19e-13

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 66.64  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGIS--SGMGRAAALYFKQQGFEVY------------GGARRVE--RLTDLREKG---IHTQKLDVTDKFSIR 61
Cdd:PRK12748    4 MKKIALVTGASrlNGIGAAVCRRLAAKGIDIFftywspydktmpWGMHDKEpvLLKEEIESYgvrCEHMEIDLSQPYAPN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  62 QLVDRTVSEQGRIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSiGANVySPL 141
Cdd:PRK12748   84 RVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTS-GQSL-GPM 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1774021274 142 GG--WYHATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEW 182
Cdd:PRK12748  162 PDelAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGW 204
PRK06196 PRK06196
oxidoreductase; Provisional
 3-134 8.96e-13

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 67.01  E-value: 8.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD-LRE-KGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINN 80
Cdd:PRK06196   27 KTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREaLAGiDGVEVVMLDLADLESVRAFAERFLDSGRRIDILINN 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274  81 AG-----YGEYGPLEEVpienakkQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIG 134
Cdd:PRK06196  107 AGvmacpETRVGDGWEA-------QFATNHLGHFALVNLLWPALAAGAGARVVALSSAG 158
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-181 1.32e-12

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 65.75  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEV----YGGARRVERLTDLREKGIHTQ--KLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK08217    7 VIVITGGAQGLGRAMAEYLAQKGAKLalidLNQEKLEEAVAECGALGTEVRgyAANVTDEEDVEATFAQIAEDFGQLNGL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPL---------EEVPIENAKKQFDVNLFAVGQLTQLVLPVM-RRQNSGRIINVSSI------GANVYSpl 141
Cdd:PRK08217   87 INNAGILRDGLLvkakdgkvtSKMSLEQFQSVIDVNLTGVFLCGREAAAKMiESGSKGVIINISSIaragnmGQTNYS-- 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1774021274 142 ggwyhATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK08217  165 -----ASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETE 199
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 3-152 1.49e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 65.80  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFE---VYG-----GARRVERLTDLREKGIHTQKlDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK06198    7 KVALVTGGTQGLGAAIARAFAERGAAglvICGrnaekGEAQAAELEALGAKAVFVQA-DLSDVEDCRRVVAAADEAFGRL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNS-GRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:PRK06198   86 DALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKGAL 164
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 3-168 1.69e-12

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 65.29  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGG----ARRVERlTDLREKGIHTQKLDVTDKfsiRQLVDRTVSEQGRIDVLI 78
Cdd:cd05361     2 SIALVTHARHFAGPASAEALTEDGYTVVCHdasfADAAER-QAFESENPGTKALSEQKP---EELVDAVLQAGGAIDVLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAGYG-EYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIganvySPLGGW-----YHATKASL 152
Cdd:cd05361    78 SNDYIPrPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSA-----VPKKPLaynslYGPARAAA 152

                         170
                  ....*....|....*.
gi 1774021274 153 NMWSDVLDSEVKRFGI 168
Cdd:cd05361   153 VALAESLAKELSRDNI 168
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 5-168 2.19e-12

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 66.04  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD----LREKGIHTQKLDVTDKFS--IRQLVDRTVSEQGRIDV-- 76
Cdd:PLN02780   56 ALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDvsdsIQSKYSKTQIKTVVVDFSgdIDEGVKRIKETIEGLDVgv 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAG----YGEYgpLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVY--SPLGGWYHATKA 150
Cdd:PLN02780  136 LINNVGvsypYARF--FHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIpsDPLYAVYAATKA 213

                         170
                  ....*....|....*...
gi 1774021274 151 SLNMWSDVLDSEVKRFGI 168
Cdd:PLN02780  214 YIDQFSRCLYVEYKKSGI 231
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 4-128 2.59e-12

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: 64.71  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQK-------LDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGgsakavpTDARDEDEVIALFDLIEEEIGPLEV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRII 128
Cdd:cd05373    81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTII 132
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 3-152 3.32e-12

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 64.22  E-value: 3.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVE----RLTD-LREKGIHTQ--KLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEaeaqRLKDeLNALRNSAVlvQADLSDFAACADLVAAAFRAFGRCD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274  76 VLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVssIGANVYSPLGGW--YHATKASL 152
Cdd:cd05357    81 VLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINI--IDAMTDRPLTGYfaYCMSKAAL 157
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 3-132 4.75e-12

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 64.12  E-value: 4.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLT---DLREKGIHTQKLDVT------DKFSIRQLVDRTVSEQGR 73
Cdd:PRK08945   13 RIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEavyDEIEAAGGPQPAIIPldlltaTPQNYQQLADTIEEQFGR 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAG-YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSS 132
Cdd:PRK08945   93 LDGVLHNAGlLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSS 152
PRK08278 PRK08278
SDR family oxidoreductase;
3-131 5.13e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 64.15  E-value: 5.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLrEKGIHTQ--------------KLDVTDKFSIRQLVDRTV 68
Cdd:PRK08278    7 KTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHPKL-PGTIHTAaeeieaaggqalplVGDVRDEDQVAAAVAKAV 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274  69 SEQGRIDVLINNAGYGEYGPLEEVPIenakKQFD----VNLFAVGQLTQLVLPVMRRQNSGRIINVS 131
Cdd:PRK08278   86 ERFGGIDICVNNASAINLTGTEDTPM----KRFDlmqqINVRGTFLVSQACLPHLKKSENPHILTLS 148
PRK09730 PRK09730
SDR family oxidoreductase;
2-225 5.84e-12

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 63.72  E-value: 5.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   2 TRVAIITGISSGMGRAAALYFKQQGFEV--------YGGARRVERLTDLREKGIHTQKlDVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK09730    1 MAIALVTGGSRGIGRATALLLAQEGYTVavnyqqnlHAAQEVVNLITQAGGKAFVLQA-DISDENQVVAMFTAIDQHDEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAG-YGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGR---IINVSSIGANVYSPlGGW--YHA 147
Cdd:PRK09730   80 LAALVNNAGiLFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASRLGAP-GEYvdYAA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274 148 TKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARknsldnspydelVDKVEKLFSkLGTGATSEDLAQ 225
Cdd:PRK09730  159 SKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGR------------VDRVKSNIP-MQRGGQPEEVAQ 223
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 1-132 6.60e-12

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 64.05  E-value: 6.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVaIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE---KGIHTQKLDVTDKFSIRQLVDRtVSEQGRIDVL 77
Cdd:cd08951     7 MKRI-FITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAacpGAAGVLIGDLSSLAETRKLADQ-VNAIGRFDAV 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1774021274  78 INNAGYGeYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPvmrrqnSGRIINVSS 132
Cdd:cd08951    85 IHNAGIL-SGPNRKTPDTGIPAMVAVNVLAPYVLTALIRR------PKRLIYLSS 132
PRK06101 PRK06101
SDR family oxidoreductase;
4-176 6.86e-12

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 63.73  E-value: 6.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE--KGIHTQKLDVTDKFSIRQlvdrTVSEQGRI-DVLINN 80
Cdd:PRK06101    3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHTqsANIFTLAFDVTDHPGTKA----ALSQLPFIpELWIFN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  81 AGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNsgRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLD 160
Cdd:PRK06101   79 AGDCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGH--RVVIVGSIASELALPRAEAYGASKAAVAYFARTLQ 156

                         170
                  ....*....|....*.
gi 1774021274 161 SEVKRFGIRSIIDQPG 176
Cdd:PRK06101  157 LDLRPKGIEVVTVFPG 172
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-176 7.41e-12

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 63.77  E-value: 7.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYG----GARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:PRK12481    9 KVAIITGCNTGLGQGMAIGLAKAGADIVGvgvaEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDILI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVL-PVMRRQNSGRIINVSSI-----GANVYSplggwYHATKASL 152
Cdd:PRK12481   89 NNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAkQFVKQGNGGKIINIASMlsfqgGIRVPS-----YTASKSAV 163

                         170       180
                  ....*....|....*....|....
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK12481  164 MGLTRALATELSQYNINVNAIAPG 187
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 1-149 8.30e-12

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 63.52  E-value: 8.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEV------YGGARRV--ERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQG 72
Cdd:PRK12384    1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVavadinSEKAANVaqEINAEYGEGMAYGFGADATSEQSVLALSRGVDEIFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN-SGRIINVSSIGANVYSPLGGWYHATK 149
Cdd:PRK12384   81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAK 158
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 3-149 1.18e-11

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 63.05  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE---KGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLIN 79
Cdd:PRK06200    7 QVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQrfgDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFVG 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274  80 NAGYGEYG-PLEEVPIENAKKQFDvNLFAVGQLTQL-----VLPVMRRQNSGRIINVSSIGanvYSPLGG--WYHATK 149
Cdd:PRK06200   87 NAGIWDYNtSLVDIPAETLDTAFD-EIFNVNVKGYLlgakaALPALKASGGSMIFTLSNSS---FYPGGGgpLYTASK 160
PRK06194 PRK06194
hypothetical protein; Provisional
 3-150 1.75e-11

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 63.11  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGF-----EVYGGArrVERLTD-LREKGI--HTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK06194    7 KVAVITGAASGFGLAFARIGAALGMklvlaDVQQDA--LDRAVAeLRAQGAevLGVRTDVSDAAQVEALADAALERFGAV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQN------SGRIINVSSIGANVYSPLGGWYHAT 148
Cdd:PRK06194   85 HLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAekdpayEGHIVNTASMAGLLAPPAMGIYNVS 164


                  ..
gi 1774021274 149 KA 150
Cdd:PRK06194  165 KH 166
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 3-134 1.80e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 63.12  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLTDLREKG-IHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK06197   17 RVAVVTGANTGLGYETAAALAAKGAHVVlavrnldKGKAAAARITAATPGAdVTLQELDLTSLASVRAAADALRAAYPRI 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774021274  75 DVLINNAG--YGEYGpleeVPIENAKKQFDVN---LFAV-GQLTQLVLPVmrrqNSGRIINVSSIG 134
Cdd:PRK06197   97 DLLINNAGvmYTPKQ----TTADGFELQFGTNhlgHFALtGLLLDRLLPV----PGSRVVTVSSGG 154
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 3-134 4.19e-11

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 61.46  E-value: 4.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLR--------EKGIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd09808     2 RSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARkeietesgNQNIFLHIVDMSDPKQVWEFVEEFKEEGKKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYgeYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIG 134
Cdd:cd09808    82 HVLINNAGC--MVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGG 139
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
6-263 4.56e-11

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 61.92  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE-KGIHTQKLDVTDKFSIRQLVDrtvseqgRIDVLINNAGYG 84
Cdd:COG0451     3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAAlPGVEFVRGDLRDPEALAAALA-------GVDAVVHLAAPA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  85 eygpleEVPIENAKKQFDVNLfavgQLTQLVLPVMRRQNSGRIINVSSIGanVYSPLGGW------------YHATKASL 152
Cdd:COG0451    76 ------GVGEEDPDETLEVNV----EGTLNLLEAARAAGVKRFVYASSSS--VYGDGEGPidedtplrpvspYGASKLAA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 153 NMWsdvLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARKNSLDNSPYDELVDkveklfsklGTGATS----EDLAQVFY 228
Cdd:COG0451   144 ELL---ARAYARRYGLPVTILRPGNVYGPGDRGVLPRLIRRALAGEPVPVFGD---------GDQRRDfihvDDVARAIV 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1774021274 229 HAATDAHPKRRYYNsVVDHRMV-------MIARTMPNTYRIV 263
Cdd:COG0451   212 LALEAPAAPGGVYN-VGGGEPVtlrelaeAIAEALGRPPEIV 252
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 4-149 9.53e-11

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


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 60.44  E-value: 9.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLRE------KGIHTqklDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:cd05348     6 VALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRAdfgdavVGVEG---DVRSLADNERAVARCVERFGKLDCF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYG-PLEEVPIENAKKQFDvNLFAVGQLTQLV-----LPVMRRQNSGRIINVSSIGanvYSPLGG--WYHATK 149
Cdd:cd05348    83 IGNAGIWDYStSLVDIPEEKLDEAFD-ELFHINVKGYILgakaaLPALYATEGSVIFTVSNAG---FYPGGGgpLYTASK 158
PRK09135 PRK09135
pteridine reductase; Provisional
 1-154 1.03e-10

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 60.33  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARR--------VERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQG 72
Cdd:PRK09135    5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsaaeadalAAELNALRPGSAAALQADLLDPDALPELVAACVAAFG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMrRQNSGRIINVSSIgaNVYSPLGGW--YHATKA 150
Cdd:PRK09135   85 RLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQL-RKQRGAIVNITDI--HAERPLKGYpvYCAAKA 161


                  ....
gi 1774021274 151 SLNM 154
Cdd:PRK09135  162 ALEM 165
PRK06953 PRK06953
SDR family oxidoreductase;
3-154 1.09e-10

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 60.09  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEqgRIDVLINNAG 82
Cdd:PRK06953    2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGAEALALDVADPASVAGLAWKLDGE--ALDAAVYVAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  83 YgeYGPLEEVPIENAKKQFD----VNLFAVGQLTQLVLPVMrrQNSGRIINV-----SSIGANVYSplGGW-YHATKASL 152
Cdd:PRK06953   80 V--YGPRTEGVEPITREDFDavmhTNVLGPMQLLPILLPLV--EAAGGVLAVlssrmGSIGDATGT--TGWlYRASKAAL 153


                  ..
gi 1774021274 153 NM 154
Cdd:PRK06953  154 ND 155
PRK06123 PRK06123
SDR family oxidoreductase;
1-233 1.15e-10

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 60.18  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYGGARR--------VERLTDLREKGIHTQKlDVTDKFSIRQLVDRTVSEQG 72
Cdd:PRK06123    1 MRKVMIITGASRGIGAATALLAAERGYAVCLNYLRnrdaaeavVQAIRRQGGEALAVAA-DVADEADVLRLFEAVDRELG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGE-YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGR---IINVSSIGANVYSPlGGW--YH 146
Cdd:PRK06123   80 RLDALVNNAGILEaQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSP-GEYidYA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 147 ATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKIGFENARknsldnspydelVDKVeKLFSKLGTGATSEDLAQV 226
Cdd:PRK06123  159 ASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGR------------VDRV-KAGIPMGRGGTAEEVARA 225


                  ....*..
gi 1774021274 227 FYHAATD 233
Cdd:PRK06123  226 ILWLLSD 232
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 3-169 1.54e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 60.07  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV----YGG-----------ARRV--ERLTDLREKGIHTQklDVTDKFSIRQLVD 65
Cdd:PRK07791    7 RVVIVTGAGGGIGRAHALAFAAEGARVvvndIGVgldgsasggsaAQAVvdEIVAAGGEAVANGD--DIADWDGAANLVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  66 RTVSEQGRIDVLINNAGYgeygpLEEVPIEN-AKKQFD----VNL---FAvgqltqlvlpVMR-------------RQNS 124
Cdd:PRK07791   85 AAVETFGGLDVLVNNAGI-----LRDRMIANmSEEEWDaviaVHLkghFA----------TLRhaaaywraeskagRAVD 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1774021274 125 GRIINVSSiGANVYSPLG-GWYHATKASLNMWSDVLDSEVKRFGIR 169
Cdd:PRK07791  150 ARIINTSS-GAGLQGSVGqGNYSAAKAGIAALTLVAAAELGRYGVT 194
PRK08703 PRK08703
SDR family oxidoreductase;
3-186 1.73e-10

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 59.56  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK----------GIHTQKLDVTDKfSIRQLVDRTVSE-Q 71
Cdd:PRK08703    7 KTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAiveaghpepfAIRFDLMSAEEK-EFEQFAATIAEAtQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  72 GRIDVLINNAGY-GEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKA 150
Cdd:PRK08703   86 GKLDGIVHCAGYfYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFGASKA 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1774021274 151 SLNMWSDVLDSEVKRFG-----------IRS---IIDQPGLTKSEWSKIG 186
Cdd:PRK08703  166 ALNYLCKVAADEWERFGnlranvlvpgpINSpqrIKSHPGEAKSERKSYG 215
PRK12746 PRK12746
SDR family oxidoreductase;
3-181 2.07e-10

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 59.66  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV---YGGARRV--ERLTDLREKG--IHTQKLDVTDKFSIRQLVDRTVSE----- 70
Cdd:PRK12746    7 KVALVTGASRGIGRAIAMRLANDGALVaihYGRNKQAadETIREIESNGgkAFLIEADLNSIDGVKKLVEQLKNElqirv 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  71 -QGRIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQnsGRIINVSSIGANVYSPLGGWYHATK 149
Cdd:PRK12746   87 gTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRLGFTGSIAYGLSK 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1774021274 150 ASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK12746  165 GALNTMTLPLAKHLGERGITVNTIMPGYTKTD 196
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 3-181 2.08e-10

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 59.70  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQG--FEVYGGARRverltDLREKGIHTQKLDVTDKFSI------------------RQ 62
Cdd:PRK12747    5 KVALVTGASRGIGRAIAKRLANDGalVAIHYGNRK-----EEAEETVYEIQSNGGSAFSIganleslhgvealyssldNE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  63 LVDRTVSEQgrIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRrqNSGRIINVSSIGANVYSPLG 142
Cdd:PRK12747   80 LQNRTGSTK--FDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLR--DNSRIINISSAATRISLPDF 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1774021274 143 GWYHATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK12747  156 IAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTD 194
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 3-207 2.68e-10

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 59.19  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGfevyggARRV---------ERLTDLREKGIHTQKL--DVTDKFSIRQLVDRTVSEQ 71
Cdd:PRK12823    9 KVVVVTGAAQGIGRGVALRAAAEG------ARVVlvdrselvhEVAAELRAAGGEALALtaDLETYAGAQAAMAAAVEAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  72 GRIDVLINNAG-------YGEYgplEEVPIEnakKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSI---GAN--VYS 139
Cdd:PRK12823   83 GRIDVLINNVGgtiwakpFEEY---EEEQIE---AEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIatrGINrvPYS 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274 140 PLGGWYHATKASLNMwsdvldsEVKRFGIRSIIDQPGLTKSEWSKIGFENARKNSLDNSPYDELVDKV 207
Cdd:PRK12823  157 AAKGGVNALTASLAF-------EYAEHGIRVNAVAPGGTEAPPRRVPRNAAPQSEQEKAWYQQIVDQT 217
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-176 3.85e-10

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 58.73  E-value: 3.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYG-----GARRVERLTDLREKGIHTQKlDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK08993   11 KVAVVTGCDTGLGQGMALGLAEAGCDIVGinivePTETIEQVTALGRRFLSLTA-DLRKIDGIPALLERAVAEFGHIDIL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEygplEEVPIENAKKQFD----VNLFAVGQLTQLVLPVMRRQ-NSGRIINVSSI-----GANVYSplggwYHA 147
Cdd:PRK08993   90 VNNAGLIR----REDAIEFSEKDWDdvmnLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMlsfqgGIRVPS-----YTA 160

                         170       180
                  ....*....|....*....|....*....
gi 1774021274 148 TKASLNMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK08993  161 SKSGVMGVTRLMANEWAKHNINVNAIAPG 189
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 5-132 5.47e-10

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 58.08  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDrtvseQGRIDVLINNAGYG 84
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLRFVEGDLTDRDALEKLLA-----DVRPDAVIHLAAVG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1774021274  85 EYGpleeVPIENAKKQFDVNLfavgQLTQLVLPVMRRQNSGRIINVSS 132
Cdd:pfam01370  76 GVG----ASIEDPEDFIEANV----LGTLNLLEAARKAGVKRFLFASS 115
PLN02253 PLN02253
xanthoxin dehydrogenase
 3-169 8.25e-10

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 57.91  E-value: 8.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLTDlrEKGIHTQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PLN02253   19 KVALVTGGATGIGESIVRLFHKHGAKVCivdlqddLGQNVCDSLGG--EPNVCFFHCDVTVEDDVSRAVDFTVDKFGTLD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGeyGP----LEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGanvySPLGGW----YHA 147
Cdd:PLN02253   97 IMVNNAGLT--GPpcpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVA----SAIGGLgphaYTG 170

                         170       180
                  ....*....|....*....|..
gi 1774021274 148 TKASLNMWSDVLDSEVKRFGIR 169
Cdd:PLN02253  171 SKHAVLGLTRSVAAELGKHGIR 192
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-182 1.33e-09

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 57.10  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGIS--SGMGRAAALYFKQQGFEVY------------GGARRVERL---TDLREKGI--HTQKLDVTDKFSIRQL 63
Cdd:PRK12859    7 KVAVVTGVSrlDGIGAAICKELAEAGADIFftywtaydkempWGVDQDEQIqlqEELLKNGVkvSSMELDLTQNDAPKEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  64 VDRTVSEQGRIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSigANVYSPLGG 143
Cdd:PRK12859   87 LNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTS--GQFQGPMVG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1774021274 144 --WYHATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEW 182
Cdd:PRK12859  165 elAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGW 205
PRK09134 PRK09134
SDR family oxidoreductase;
1-140 2.19e-09

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 56.47  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEV---YGGARR-----VERLTDLREKGIHTQKlDVTDKFSIRQLVDRTVSEQG 72
Cdd:PRK09134    8 APRAALVTGAARRIGRAIALDLAAHGFDVavhYNRSRDeaealAAEIRALGRRAVALQA-DLADEAEVRALVARASAALG 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQ---LVLPVMRRqnsGRIINVssIGANVYSP 140
Cdd:PRK09134   87 PITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQafaRALPADAR---GLVVNM--IDQRVWNL 152
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 3-181 2.28e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 56.93  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRV-----------------ERLTDLREKGIHTQkLDVTDKFSIRQLVD 65
Cdd:PRK08303    9 KVALVAGATRGAGRGIAVELGAAGATVYVTGRSTrarrseydrpetieetaELVTAAGGRGIAVQ-VDHLVPEQVRALVE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  66 RTVSEQGRIDVLINNAGYGE-----YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSiGANVYSP 140
Cdd:PRK08303   88 RIDREQGRLDILVNDIWGGEklfewGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEITD-GTAEYNA 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774021274 141 ----LGGWYHATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK08303  167 thyrLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSE 211
PRK08628 PRK08628
SDR family oxidoreductase;
3-132 2.66e-09

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 56.51  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQG-FEVYGG--ARRVERLTDLREKGI--HTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK08628    8 KVVIVTGGASGIGAAISLRLAEEGaIPVIFGrsAPDDEFAEELRALQPraEFVQVDLTDDAQCRDAVEQTVAKFGRIDGL 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274  78 INNAGYGeygplEEVPIENAKKQF----DVNLFAVGQLTQLVLPVMrRQNSGRIINVSS 132
Cdd:PRK08628   88 VNNAGVN-----DGVGLEAGREAFvaslERNLIHYYVMAHYCLPHL-KASRGAIVNISS 140
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 3-235 3.88e-09

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 56.85  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLR--EKGIHT------QKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:COG3347   426 RVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAaeLGGGYGadavdaTDVDVTAEAAVAAAFGFAGLDIGGS 505

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQ-NSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:COG3347   506 DIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQgLGGSSVFAVSKNAAAAAYGAAAAATAKAAAQ 585

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 154 MWSDVLDSEVKRFGIRSIIDQPGLTkSEWSKIGFENARknsldnspydELVDKVEKLFSKLGTGATSEDLAQVFYHAATD 233
Cdd:COG3347   586 HLLRALAAEGGANGINANRVNPDAV-LDGSAIWASAAR----------AERAAAYGIGNLLLEEVYRKRVALAVLVLAED 654


                  ..
gi 1774021274 234 AH 235
Cdd:COG3347   655 IA 656
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 3-181 6.47e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 55.19  E-value: 6.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK--------GIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK05875    8 RTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEiealkgagAVRYEPADVTDEDQVARAVDAATAWHGRL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGE-YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLN 153
Cdd:PRK05875   88 HGVVHCAGGSEtIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKSAVD 167

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774021274 154 ----MWSDVL-DSEVKRFGIRsiidqPGLTKSE 181
Cdd:PRK05875  168 hlmkLAADELgPSWVRVNSIR-----PGLIRTD 195
PRK07023 PRK07023
SDR family oxidoreductase;
5-176 6.49e-09

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 55.02  E-value: 6.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARRV---------ERLTDLRekgihtqkLDVTDKFSIRQ-----LVDRTVSE 70
Cdd:PRK07023    4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARSRhpslaaaagERLAEVE--------LDLSDAAAAAAwlagdLLAAFVDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  71 QGRIdVLINNAGYGE-YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSiGA--NVYSplgGW--Y 145
Cdd:PRK07023   76 ASRV-LLINNAGTVEpIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISS-GAarNAYA---GWsvY 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1774021274 146 HATKASLNMWSDVLDSEVKRfGIRSIIDQPG 176
Cdd:PRK07023  151 CATKAALDHHARAVALDANR-ALRIVSLAPG 180
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 73-180 1.87e-08

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 52.90  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  73 RIDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:cd02266    31 RRDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAAL 110

                          90       100
                  ....*....|....*....|....*...
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPGLTKS 180
Cdd:cd02266   111 DGLAQQWASEGWGNGLPATAVACGTWAG 138
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 5-229 3.70e-08

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 52.97  E-value: 3.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISS----GMGRAAALYfkQQGFEV-YGGA-----RRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd05372     4 ILITGIANdrsiAWGIAKALH--EAGAELaFTYQpealrKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEY----GPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSgrIINVSSIGANVYSPLGGWYHATKA 150
Cdd:cd05372    82 DGLVHSIAFAPKvqlkGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNPGGS--IVTLSYLGSERVVPGYNVMGVAKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 151 SLNmwSDV--LDSEVKRFGIRS--IIDQPGLTKSEWSKIGFENARKNSLDNSPYDELVDKVE------KLFSKLGTGATs 220
Cdd:cd05372   160 ALE--SSVryLAYELGRKGIRVnaISAGPIKTLAASGITGFDKMLEYSEQRAPLGRNVTAEEvgntaaFLLSDLSSGIT- 236


                  ....*....
gi 1774021274 221 edlAQVFYH 229
Cdd:cd05372   237 ---GEIIYV 242
PRK07806 PRK07806
SDR family oxidoreductase;
3-132 3.82e-08

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 52.80  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV---Y-GGARRVERLT-DLREKGIH--TQKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK07806    7 KTALVTGSSRGIGADTAKILAGAGAHVvvnYrQKAPRANKVVaEIEAAGGRasAVGADLTDEESVAALMDTAREEFGGLD 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274  76 VLINNAGYG-EYGPLEEVPIEnakkqfdVNLFAVGQLTQLVLPVMrrQNSGRIINVSS 132
Cdd:PRK07806   87 ALVLNASGGmESGMDEDYAMR-------LNRDAQRNLARAALPLM--PAGSRVVFVTS 135
PRK09009 PRK09009
SDR family oxidoreductase;
6-184 4.37e-08

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 52.37  E-value: 4.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAAlyfkQQGFEVYGGAR-----RVERlTDLREKGIHTQKLDVTDKFSIRQLvdrtvSEQ-GRIDVLIN 79
Cdd:PRK09009    4 LIVGGSGGIGKAMV----KQLLERYPDATvhatyRHHK-PDFQHDNVQWHALDVTDEAEIKQL-----SEQfTQLDWLIN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGY---GEYGPleevpiENAKKQFDVNLF----AVGQLTQLVL-----PVMRRQNSGRIINVS----SIGANvysPLGG 143
Cdd:PRK09009   74 CVGMlhtQDKGP------EKSLQALDADFFlqniTLNTLPSLLLakhftPKLKQSESAKFAVISakvgSISDN---RLGG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1774021274 144 WY--HATKASLNMWSDVLDSE----VKRFGIRSIidQPGLTKSEWSK 184
Cdd:PRK09009  145 WYsyRASKAALNMFLKTLSIEwqrsLKHGVVLAL--HPGTTDTALSK 189
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 3-168 6.27e-08

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 52.27  E-value: 6.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLtdlREKG--IHTQKLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:PRK05876    7 RGAVITGGASGIGLATGTEFARRGARVVlgdvdkpGLRQAVNHL---RAEGfdVHGVMCDVRHREEVTHLADEAFRLLGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLG-GWYHATKASL 152
Cdd:PRK05876   84 VDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGlGAYGVAKYGV 163

                         170
                  ....*....|....*.
gi 1774021274 153 NMWSDVLDSEVKRFGI 168
Cdd:PRK05876  164 VGLAETLAREVTADGI 179
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 3-151 1.36e-07

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 50.79  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGgarrverlTDLRE-----KGIhTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:cd05334     2 RVVLVYGGRGALGSAVVQAFKSRGWWVAS--------IDLAEneeadASI-IVLDSDSFTEQAKQVVASVARLSGKVDAL 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774021274  78 INNAGYGEYGPL-EEVPIENAKKQFDVNLFAVGQLTQLVLPVMRrqNSGRIINVSSIGANVYSPLGGWYHATKAS 151
Cdd:cd05334    73 ICVAGGWAGGSAkSKSFVKNWDLMWKQNLWTSFIASHLATKHLL--SGGLLVLTGAKAALEPTPGMIGYGAAKAA 145
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 4-180 1.48e-07

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: 51.23  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMG-----RAAALYFKQQGFEVYGGARRVERLTDLRE--KGIHTQK--------LDVTDKFSIRQLVDRTV 68
Cdd:cd08941     3 VVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQRAEAACRalLASHPDArvvfdyvlVDLSNMVSVFAAAKELK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  69 SEQGRIDVLINNAGYGEYG--------------PLEEVPIENAKKQ-------------------FDVNLFAVGQLTQLV 115
Cdd:cd08941    83 KRYPRLDYLYLNAGIMPNPgidwigaikevltnPLFAVTNPTYKIQaegllsqgdkatedglgevFQTNVFGHYYLIREL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774021274 116 LPVMRRQNS-GRIINVSSIGANV-YSPLGGW--------YHATKASLNMWSDVLDSEVKRFGIRSIIDQPGLTKS 180
Cdd:cd08941   163 EPLLCRSDGgSQIIWTSSLNASPkYFSLEDIqhlkgpapYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTT 237
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-169 2.20e-07

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 50.53  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIItGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREK-----GIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK05786    7 KVAII-GVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTlskygNIHYVVGDVSSTESARNVIEKAAKVLNAIDGL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNAGYGEYGPLEEVP--IENAKKQFDVNLFAVGQLtqlvLPVMRRQNSgrIINVSSI-GANVYSPLGGWYHATKASLNM 154
Cdd:PRK05786   86 VVTVGGYVEDTVEEFSglEEMLTNHIKIPLYAVNAS----LRFLKEGSS--IVLVSSMsGIYKASPDQLSYAVAKAGLAK 159

                         170
                  ....*....|....*
gi 1774021274 155 WSDVLDSEVKRFGIR 169
Cdd:PRK05786  160 AVEILASELLGRGIR 174
PRK07041 PRK07041
SDR family oxidoreductase;
6-152 2.42e-07

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 50.42  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQGFEVYGGARRVERL-TDLREKGIH----TQKLDVTDKfsirQLVDRTVSEQGRIDVLINN 80
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLaAAARALGGGapvrTAALDITDE----AAVDAFFAEAGPFDHVVIT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774021274  81 AGYGEYGPLEEVPIENAKKQFDVNLFavGQLtqLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:PRK07041   77 AADTPGGPVRALPLAAAQAAMDSKFW--GAY--RVARAARIAPGGSLTFVSGFAAVRPSASGVLQGAINAAL 144
PRK09186 PRK09186
flagellin modification protein A; Provisional
 40-169 2.45e-07

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 50.37  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  40 TDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINNA-----GYGEYgpLEEVPIENAKKQFDVNLFAVGQLTQL 114
Cdd:PRK09186   50 KEFKSKKLSLVELDITDQESLEEFLSKSAEKYGKIDGAVNCAyprnkDYGKK--FFDVSLDDFNENLSLHLGSSFLFSQQ 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274 115 VLPVMRRQNSGRIINVSSI------------GANVYSPLGgwYHATKASLNMWSDVLDSEVKRFGIR 169
Cdd:PRK09186  128 FAKYFKKQGGGNLVNISSIygvvapkfeiyeGTSMTSPVE--YAAIKAGIIHLTKYLAKYFKDSNIR 192
PRK12742 PRK12742
SDR family oxidoreductase;
3-181 3.56e-07

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 49.76  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV---YGGAR-RVERLTdlREKGIHTQKLDVTDkfsiRQLVDRTVSEQGRIDVLI 78
Cdd:PRK12742    7 KKVLVLGGSRGIGAAIVRRFVTDGANVrftYAGSKdAAERLA--QETGATAVQTDSAD----RDAVIDVVRKSGALDILV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  79 NNAGYGEYG-PLEEVPiENAKKQFDVNLFAVGQLTqlVLPVMRRQNSGRIINVSSIGAN-VYSPLGGWYHATKASLNMWS 156
Cdd:PRK12742   81 VNAGIAVFGdALELDA-DDIDRLFKINIHAPYHAS--VEAARQMPEGGRIIIIGSVNGDrMPVAGMAAYAASKSALQGMA 157

                         170       180
                  ....*....|....*....|....*...
gi 1774021274 157 DVLdseVKRFGIRSI---IDQPGLTKSE 181
Cdd:PRK12742  158 RGL---ARDFGPRGItinVVQPGPIDTD 182
PRK05717 PRK05717
SDR family oxidoreductase;
3-152 3.60e-07

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 49.89  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYggarrverLTDL-REKGIHTQK----------LDVTDKFSIRQLVDRTVSEQ 71
Cdd:PRK05717   11 RVALVTGAARGIGLGIAAWLIAEGWQVV--------LADLdRERGSKVAKalgenawfiaMDVADEAQVAAGVAEVLGQF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  72 GRIDVLINNAGYGE--YGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNsGRIINVSSIGANVYSPLGGWYHATK 149
Cdd:PRK05717   83 GRLDALVCNAAIADphNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPDTEAYAASK 161


                  ...
gi 1774021274 150 ASL 152
Cdd:PRK05717  162 GGL 164
PRK07102 PRK07102
SDR family oxidoreductase;
1-176 8.01e-07

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 48.77  E-value: 8.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIItGISSGMGRAAALYFKQQGFEVYGGARRVERLT----DLREKG---IHTQKLDVTDKFSIRQLVDRTvseQGR 73
Cdd:PRK07102    1 MKKILII-GATSDIARACARRYAAAGARLYLAARDVERLErladDLRARGavaVSTHELDILDTASHAAFLDSL---PAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGY-GEYGPLEEVPiENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:PRK07102   77 PDIVLIAVGTlGDQAACEADP-ALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAAL 155

                         170       180
                  ....*....|....*....|....
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK07102  156 TAFLSGLRNRLFKSGVHVLTVKPG 179
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 5-110 1.25e-06

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 47.96  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARrverltdlrEKGIHTqkLDVTDKFSIRQLVDRTvseqGRIDVLINNAGYG 84
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVITAGR---------SSGDYQ--VDITDEASIKALFEKV----GHFDAIVSTAGDA 65

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1774021274  85 EYGPLEEVPIENAKKQFD------VNLFAVGQ 110
Cdd:cd11731    66 EFAPLAELTDADFQRGLNskllgqINLVRHGL 97
PRK08416 PRK08416
enoyl-ACP reductase;
6-234 1.63e-06

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 48.23  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQGFEV---YGGARRV--ERLTDLREK-GIHTQ--KLDVTDKFSIRQLVDRTVSEQGRIDVL 77
Cdd:PRK08416   12 VISGGTRGIGKAIVYEFAQSGVNIaftYNSNVEEanKIAEDLEQKyGIKAKayPLNILEPETYKELFKKIDEDFDRVDFF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  78 INNA---------GYGEYGPLEEVPIENAKKQfDVNLFAVGqlTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHAT 148
Cdd:PRK08416   92 ISNAiisgravvgGYTKFMRLKPKGLNNIYTA-TVNAFVVG--AQEAAKRMEKVGGGSIISLSSTGNLVYIENYAGHGTS 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274 149 KASLNMWSDVLDSEVKRFGIRSIIDQPGLTKSEWSKiGFENarknsldnspYDELVDKVEKLfSKLGTGATSEDLAQVFY 228
Cdd:PRK08416  169 KAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALK-AFTN----------YEEVKAKTEEL-SPLNRMGQPEDLAGACL 236


                  ....*.
gi 1774021274 229 HAATDA 234
Cdd:PRK08416  237 FLCSEK 242
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 7-131 1.98e-06

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 47.83  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   7 ITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLreKG-IHTQ--------------KLDVTDKFSIRQLVDRTVSEQ 71
Cdd:cd09762     8 ITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKL--PGtIYTAaeeieaaggkalpcIVDIRDEDQVRAAVEKAVEKF 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774021274  72 GRIDVLINNAGYGEYGPLEEVPIenakKQFD----VNLFAVGQLTQLVLPVMRRQNSGRIINVS 131
Cdd:cd09762    86 GGIDILVNNASAISLTGTLDTPM----KRYDlmmgVNTRGTYLCSKACLPYLKKSKNPHILNLS 145
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 5-207 2.91e-06

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 46.75  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDL-REKGIHTQKLDVTDKFSIRQLVDrtvsEQGRIDVLINNAGY 83
Cdd:cd11730     1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLaAEVGALARPADVAAELEVWALAQ----ELGPLDLLVYAAGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  84 GEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQnsGRIINVSSIGANVYSPLGGWYHATKASLNMWSDVLDSEV 163
Cdd:cd11730    77 ILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAG--ARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARKEV 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774021274 164 KrfGIRSIIDQPGLTKSE-WSKIGfeNARKNSLdnSPyDELVDKV 207
Cdd:cd11730   155 R--GLRLTLVRPPAVDTGlWAPPG--RLPKGAL--SP-EDVAAAI 192
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
24-135 4.48e-06

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 46.53  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  24 QQGFEVYGgarrverlTDLREKGIHTQ---KLDVTDKFSIRQLVDRTvseQGRIDVLINNAGYGEYGPLEEVpienakkq 100
Cdd:PRK12428    7 FLGARVIG--------VDRREPGMTLDgfiQADLGDPASIDAAVAAL---PGRIDALFNIAGVPGTAPVELV-------- 67

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1774021274 101 FDVNLFAVGQLTQLVLPVMRrqNSGRIINVSSIGA 135
Cdd:PRK12428   68 ARVNFLGLRHLTEALLPRMA--PGGAIVNVASLAG 100
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 3-176 8.24e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 46.10  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD----LREKGihTQKL----DVTDKFSIRQLVDRTVSEQGRI 74
Cdd:PRK07576   10 KNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAavaqLQQAG--PEGLgvsaDVRDYAAVEAAFAQIADEFGPI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  75 DVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNsGRIINVSSIGANVYSPLGGWYHATKASLNM 154
Cdd:PRK07576   88 DVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG-ASIIQISAPQAFVPMPMQAHVCAAKAGVDM 166

                         170       180
                  ....*....|....*....|....
gi 1774021274 155 WSDVLDSEVKRFGIR--SIIdqPG 176
Cdd:PRK07576  167 LTRTLALEWGPEGIRvnSIV--PG 188
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 5-103 8.36e-06

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 45.09  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDrtvseqgRIDVLINNAGYG 84
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRLSKEDQEPVAVVEGDLRDLDSLSDAVQ-------GVDVVIHLAGAP 73

                          90       100
                  ....*....|....*....|
gi 1774021274  85 EYGPL-EEVPIENAKKQFDV 103
Cdd:cd05226    74 RDTRDfCEVDVEGTRNVLEA 93
PRK05854 PRK05854
SDR family oxidoreductase;
3-180 8.75e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 46.21  E-value: 8.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVER----LTDLREKG----IHTQKLDVTDKFSIRQLVDrTVSEQGR- 73
Cdd:PRK05854   15 KRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKgeaaVAAIRTAVpdakLSLRALDLSSLASVAALGE-QLRAEGRp 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  74 IDVLINNAGYGEyGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMrRQNSGRIINVSSIGAN-------------VYSP 140
Cdd:PRK05854   94 IHLLINNAGVMT-PPERQTTADGFELQFGTNHLGHFALTAHLLPLL-RAGRARVTSQSSIAARrgainwddlnwerSYAG 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1774021274 141 LGGwYHATKASLNMWSDVLD--SEVKRFGIRSIIDQPGLTKS 180
Cdd:PRK05854  172 MRA-YSQSKIAVGLFALELDrrSRAAGWGITSNLAHPGVAPT 212
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 4-176 9.91e-06

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 45.67  E-value: 9.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYF----KQQGFEVYGGARRVERLTDLRE--------KGIHTQKLDVTDKFSIRQLVdRTVSEQ 71
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELakclKSPGSVLVLSARNDEALRQLKAeigaersgLRVVRVSLDLGAEAGLEQLL-KALREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  72 GRID-----VLINNAG-YGEYGPLEEV--PIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGR--IINVSSIGAnvYSPL 141
Cdd:TIGR01500  81 PRPKglqrlLLINNAGtLGDVSKGFVDlsDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGLNrtVVNISSLCA--IQPF 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1774021274 142 GGW--YHATKASLNMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:TIGR01500 159 KGWalYCAGKAARDMLFQVLALEEKNPNVRVLNYAPG 195
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 2-142 1.28e-05

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 45.59  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   2 TRVAIITGISSGMGRAAALYFKQQG-FEVYGGARRVERLTDLREK-GIHTQK-----LDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd09810     1 KGTVVITGASSGLGLAAAKALARRGeWHVVMACRDFLKAEQAAQEvGMPKDSysvlhCDLASLDSVRQFVDNFRRTGRPL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774021274  75 DVLINNAGYgeYGPLEEVPIENA---KKQFDVNLFAVGQLTQLVLPVMRRQ--NSGRIINVSSIGANVYSPLG 142
Cdd:cd09810    81 DALVCNAAV--YLPTAKEPRFTAdgfELTVGVNHLGHFLLTNLLLEDLQRSenASPRIVIVGSITHNPNTLAG 151
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 7-150 1.29e-05

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 44.84  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   7 ITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVdrtvseQGrIDVLINNAGYGEY 86
Cdd:COG0702     4 VTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAGVEVVQGDLDDPESLAAAL------AG-VDAVFLLVPSGPG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774021274  87 GPLEevpienakkqFDVnlfavgQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGgwYHATKA 150
Cdd:COG0702    77 GDFA----------VDV------EGARNLADAAKAAGVKRIVYLSALGADRDSPSP--YLRAKA 122
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 7-83 1.54e-05

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 45.31  E-value: 1.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274   7 ITGiSSGM-GRAAALYFKQQGFEVYGGARRVERLTdlrekgihtqKLDVTDKFSIRQLVDRTvseqgRIDVLINNAGY 83
Cdd:cd05254     4 ITG-ATGMlGRALVRLLKERGYEVIGTGRSRASLF----------KLDLTDPDAVEEAIRDY-----KPDVIINCAAY 65
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 3-132 1.68e-05

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 45.28  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD-----LRE---KGIHTQKLDVTDKFSIRQLVDRTVSEQGRI 74
Cdd:cd09809     2 KVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEwhkARVEAMTLDLASLRSVQRFAEAFKAKNSPL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774021274  75 DVLINNAG-YGEYGPLEEVPIENAkkqFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSS 132
Cdd:cd09809    82 HVLVCNAAvFALPWTLTEDGLETT---FQVNHLGHFYLVQLLEDVLRRSAPARVIVVSS 137
PRK08340 PRK08340
SDR family oxidoreductase;
6-141 1.75e-05

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 45.18  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQGFEVYGGARRVERL----TDLREKG-IHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLINN 80
Cdd:PRK08340    4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLekalKELKEYGeVYAVKADLSDKDDLKNLVKEAWELLGGIDALVWN 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774021274  81 AGYGEYGP--LEEVPIENAKKQFDVNLFAVGQLTQLVLPV-MRRQNSGRIINVSSigANVYSPL 141
Cdd:PRK08340   84 AGNVRCEPcmLHEAGYSDWLEAALLHLVAPGYLTTLLIQAwLEKKMKGVLVYLSS--VSVKEPM 145
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
7-83 1.94e-05

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 45.12  E-value: 1.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274   7 ITGiSSGM-GRAAALYFKQQGFEVYGGARrverltdlrekgihtQKLDVTDKFSIRQLVDRTvseqgRIDVLINNAGY 83
Cdd:COG1091     4 VTG-ANGQlGRALVRLLAERGYEVVALDR---------------SELDITDPEAVAALLEEV-----RPDVVINAAAY 60
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-82 2.03e-05

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 45.16  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEV----YGGARRVERLTD-LREKGIHTQKL--DVTDKFSIRQLVdRTVSEQGRID 75
Cdd:PRK07792   13 KVAVVTGAAAGLGRAEALGLARLGATVvvndVASALDASDVLDeIRAAGAKAVAVagDISQRATADELV-ATAVGLGGLD 91


                  ....*..
gi 1774021274  76 VLINNAG 82
Cdd:PRK07792   92 IVVNNAG 98
PRK05599 PRK05599
SDR family oxidoreductase;
4-176 2.04e-05

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 44.88  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYfkQQGFEVYGGARRVERL----TDLREKG---IHTQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK05599    3 ILILGGTSDIAGEIATLL--CHGEDVVLAARRPEAAqglaSDLRQRGatsVHVLSFDAQDLDTHRELVKQTQELAGEISL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LInnAGYGEYGPLEEVPIENAKKqFDVNLF----AVGQLTQLVlPVMRRQNS-GRIINVSSIganvysplGGW------- 144
Cdd:PRK05599   81 AV--VAFGILGDQERAETDEAHA-VEIATVdytaQVSMLTVLA-DELRAQTApAAIVAFSSI--------AGWrarrany 148

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774021274 145 -YHATKASLNMWSDVLDSEVKRFGIRSIIDQPG 176
Cdd:PRK05599  149 vYGSTKAGLDAFCQGLADSLHGSHVRLIIARPG 181
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
3-135 3.15e-05

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 43.69  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIItGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREkGIHTQKLDVTDKFSIRQLVdrtvseQGrIDVLINNAG 82
Cdd:COG2910     1 KIAVI-GATGRVGSLIVREALARGHEVTALVRNPEKLPDEHP-GLTVVVGDVLDPAAVAEAL------AG-ADAVVSALG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1774021274  83 ygeygpleevpienAKKQFDVNLFAVGqlTQLVLPVMRRQNSGRIINVSSIGA 135
Cdd:COG2910    72 --------------AGGGNPTTVLSDG--ARALIDAMKAAGVKRLIVVGGAGS 108
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 1-81 5.78e-05

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 43.38  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVYgGARRVER--LTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:PRK06483    1 MPAPILITGAGQRIGLALAWHLLAQGQPVI-VSYRTHYpaIDGLRQAGAQCIQADFSTNAGIMAFIDELKQHTDGLRAII 79


                  ...
gi 1774021274  79 NNA 81
Cdd:PRK06483   80 HNA 82
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 7-184 8.09e-05

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 42.61  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   7 ITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVdrtvseQGrIDVLINNAGYGEY 86
Cdd:cd05243     4 VVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAAGAEVVVGDLTDAESLAAAL------EG-IDAVISAAGSGGK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  87 GPleevpienaKKQFDVNLFAVGQLTQLvlpvMRRQNSGRIINVSSIGANVYSP----LGGWYHATKASlnmwsdvlDSE 162
Cdd:cd05243    77 GG---------PRTEAVDYDGNINLIDA----AKKAGVKRFVLVSSIGADKPSHpleaLGPYLDAKRKA--------EDY 135

                         170       180
                  ....*....|....*....|...
gi 1774021274 163 VKRFGIRSIIDQPG-LTKSEWSK 184
Cdd:cd05243   136 LRASGLDYTIVRPGgLTDDPAGT 158
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 1-149 1.38e-04

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: 42.45  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLTDLREKGIHTQKLDVTDKFSIRQLVDRTVSEQGR 73
Cdd:cd05322     1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAvadinseNAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274  74 IDVLINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNS-GRIINVSSIGANVYSPLGGWYHATK 149
Cdd:cd05322    81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAK 157
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
3-143 2.11e-04

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 41.90  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTD-LREKGI-----HTQKLDVTDKFSIRQLVDrTVSEQGR-ID 75
Cdd:COG5748     7 STVIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAaAQELGIppdsyTIIHIDLASLESVRRFVA-DFRALGRpLD 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774021274  76 VLINNAGYgeYGPLEEVPIENAKK---QFDVNLFAVGQLTQLVLPVMRRQNSG--RIINVSSIGANvYSPLGG 143
Cdd:COG5748    86 ALVCNAAV--YYPLLKEPLRSPDGyelSVATNHLGHFLLCNLLLEDLKKSPASdpRLVILGTVTAN-PKELGG 155
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-133 3.27e-04

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 41.75  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYG----GARrvERLTDL--REKGIHTQkLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK08261  211 KVALVTGAARGIGAAIAEVLARDGAHVVCldvpAAG--EALAAVanRVGGTALA-LDITAPDAPARIAEHLAERHGGLDI 287

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774021274  77 LINNAGygeygpleevpIENAK-------KQFD----VNLFAVGQLTQLVLPVMRRQNSGRIINVSSI 133
Cdd:PRK08261  288 VVHNAG-----------ITRDKtlanmdeARWDsvlaVNLLAPLRITEALLAAGALGDGGRIVGVSSI 344
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 3-181 3.97e-04

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 40.99  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLREKGIHTQKLDVT---DKFSIRQLVDRTVSEQGRI---DV 76
Cdd:PRK08339    9 KLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSyivADLTKREDLERTVKELKNIgepDI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQNSGRIINVSSIGANVYSPLGGWYHATKASLNMWS 156
Cdd:PRK08339   89 FFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRISMAGLV 168

                         170       180
                  ....*....|....*....|....*
gi 1774021274 157 DVLDSEVKRFGIRSIIDQPGLTKSE 181
Cdd:PRK08339  169 RTLAKELGPKGITVNGIMPGIIRTD 193
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
6-221 9.46e-04

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 39.61  E-value: 9.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMG--RAAALYFKQQGFEVYGG------ARRVERLTDlrEKGIH-TQKLDVTDKFSIRQLVDRTVSEQGRIDV 76
Cdd:PRK06603   12 LITGIANNMSisWAIAQLAKKHGAELWFTyqsevlEKRVKPLAE--EIGCNfVSELDVTNPKSISNLFDDIKEKWGSFDF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  77 LINNAGYGEYGPLE----EVPIENAKKQFDVNLFAVGQLTQLVLPVMrrQNSGRIINVSSIGANVYSPLGGWYHATKASL 152
Cdd:PRK06603   90 LLHGMAFADKNELKgryvDTSLENFHNSLHISCYSLLELSRSAEALM--HDGGSIVTLTYYGAEKVIPNYNVMGVAKAAL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774021274 153 NMWSDVLDSEVKRFGIRSIIDQPGLTKS-EWSKIG-FENARKNSLDNSPY------DELVDKVEKLFSKLGTGATSE 221
Cdd:PRK06603  168 EASVKYLANDMGENNIRVNAISAGPIKTlASSAIGdFSTMLKSHAATAPLkrnttqEDVGGAAVYLFSELSKGVTGE 244
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 5-152 1.03e-03

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 39.62  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   5 AIITGI--SSGMGRAAALYFKQQGFEV---YGGAR---RVERLTD-LREKGIHtqKLDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:COG0623     8 GLITGVanDRSIAWGIAKALHEEGAELaftYQGEAlkkRVEPLAEeLGSALVL--PCDVTDDEQIDALFDEIKEKWGKLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  76 VLINNAGYGEY----GPLEEVPIENAKKQFDVNLFAVGQLTQLVLPVMRRQnsGRIINVSSIGANVYSPLGGWYHATKAS 151
Cdd:COG0623    86 FLVHSIAFAPKeelgGRFLDTSREGFLLAMDISAYSLVALAKAAEPLMNEG--GSIVTLTYLGAERVVPNYNVMGVAKAA 163


                  .
gi 1774021274 152 L 152
Cdd:COG0623   164 L 164
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
 4-67 1.21e-03

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 39.50  E-value: 1.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEVYGGARRVERLTDLR-------EKGIHTQKLDVTDKFSIRQLVDRT 67
Cdd:cd05260     1 RALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTDRidhlyinKDRITLHYGDLTDSSSLRRAIEKV 71
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-91 1.73e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 38.23  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274    6 IITGISSGMGRAAALYFKQQgfevygGARRV--------------ERLTDLREKG--IHTQKLDVTDKFSIRQLVDRTVS 69
Cdd:smart00822   4 LITGGLGGLGRALARWLAER------GARRLvllsrsgpdapgaaALLAELEAAGarVTVVACDVADRDALAAVLAAIPA 77

                           90       100
                   ....*....|....*....|..
gi 1774021274   70 EQGRIDVLINNAGYGEYGPLEE 91
Cdd:smart00822  78 VEGPLTGVIHAAGVLDDGVLAS 99
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
52-169 1.94e-03

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 38.96  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  52 LDVTDKFSIRQLVDRTVSEQGRIDVLINNAGYGEYGPLEEVPIENAKKQFDV----NLFAVGQLTQLVLPVMrrQNSGRI 127
Cdd:PRK08415   62 LDVSKPEHFKSLAESLKKDLGKIDFIVHSVAFAPKEALEGSFLETSKEAFNIameiSVYSLIELTRALLPLL--NDGASV 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1774021274 128 INVSSIGANVYSPLGGWYHATKASLNMWSDVLDSEVKRFGIR 169
Cdd:PRK08415  140 LTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIR 181
PRK06720 PRK06720
hypothetical protein; Provisional
 3-82 1.94e-03

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 38.03  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   3 RVAIITGISSGMGRAAALYFKQQGFEVY-------GGARRVERLTDLREKGIHTQKlDVTDKFSIRQLVDRTVSEQGRID 75
Cdd:PRK06720   17 KVAIVTGGGIGIGRNTALLLAKQGAKVIvtdidqeSGQATVEEITNLGGEALFVSY-DMEKQGDWQRVISITLNAFSRID 95


                  ....*..
gi 1774021274  76 VLINNAG 82
Cdd:PRK06720   96 MLFQNAG 102
PRK05884 PRK05884
SDR family oxidoreductase;
6-171 2.25e-03

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 38.25  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQGFEV-YGGARRVERLTDLREKGIHTQKLDVTDKFSI---RQLVDRtvseqgRIDVLIN-- 79
Cdd:PRK05884    4 LVTGGDTDLGRTIAEGFRNDGHKVtLVGARRDDLEVAAKELDVDAIVCDNTDPASLeeaRGLFPH------HLDTIVNvp 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274  80 NAGYGEYGPLEEVPIENA---KKQFDVNLFAVGQLTQLVLPVMRrqNSGRIINVSSIGAnvysPLGGWYHATKASLNMWS 156
Cdd:PRK05884   78 APSWDAGDPRTYSLADTAnawRNALDATVLSAVLTVQSVGDHLR--SGGSIISVVPENP----PAGSAEAAIKAALSNWT 151

                         170
                  ....*....|....*
gi 1774021274 157 dvlDSEVKRFGIRSI 171
Cdd:PRK05884  152 ---AGQAAVFGTRGI 163
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 1-128 3.39e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 38.08  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   1 MTRVAIITGiSSGMGRAAAlyfKQQGF--EVYGGARRVERLTD----LREKG--IHTQKLDVTDKFSIRQLVDrTVSEQG 72
Cdd:PRK06940    1 MKEVVVVIG-AGGIGQAIA---RRVGAgkKVLLADYNEENLEAaaktLREAGfdVSTQEVDVSSRESVKALAA-TAQTLG 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1774021274  73 RIDVLINNAGygeYGPlEEVPIENAKKqfdVNLFAVGQLTQLVLPVMRRQNSGRII 128
Cdd:PRK06940   76 PVTGLVHTAG---VSP-SQASPEAILK---VDLYGTALVLEEFGKVIAPGGAGVVI 124
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 4-81 5.10e-03

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


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 37.60  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGFEVY-------GGARR-VERLTDLREKGIHTQKLDVTDKFSI----RQLVDRTVSEQ 71
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVlhyhrsaAAASTlAAELNARRPNSAVTCQADLSNSATLfsrcEAIIDACFRAF 82

                          90
                  ....*....|
gi 1774021274  72 GRIDVLINNA 81
Cdd:TIGR02685  83 GRCDVLVNNA 92
PLN00015 PLN00015
protochlorophyllide reductase
 6-136 5.48e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 37.76  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   6 IITGISSGMGRAAALYFKQQG-FEVYGGARRVERL-TDLREKGIHTQ-----KLDVTDKFSIRQLVDRTVSEQGRIDVLI 78
Cdd:PLN00015    1 IITGASSGLGLATAKALAETGkWHVVMACRDFLKAeRAAKSAGMPKDsytvmHLDLASLDSVRQFVDNFRRSGRPLDVLV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774021274  79 NNAGYgeYGPLEEVPIENA---KKQFDVNLFAVGQLTQLVLPVMRRQ--NSGRIINVSSIGAN 136
Cdd:PLN00015   81 CNAAV--YLPTAKEPTFTAdgfELSVGTNHLGHFLLSRLLLDDLKKSdyPSKRLIIVGSITGN 141
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 4-82 9.62e-03

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 36.96  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774021274   4 VAIITGISSGMGRAAALYFKQQGfevygGARRV---------------ERLTDLREKG--IHTQKLDVTDKFSIRQLVDR 66
Cdd:cd08953   207 VYLVTGGAGGIGRALARALARRY-----GARLVllgrsplppeeewkaQTLAALEALGarVLYISADVTDAAAVRRLLEK 281

                          90
                  ....*....|....*.
gi 1774021274  67 TVSEQGRIDVLINNAG 82
Cdd:cd08953   282 VRERYGAIDGVIHAAG 297
 
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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