|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
8-267 |
2.82e-137 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 387.76 E-value: 2.82e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRG-EEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAAS----GVRREDVFITSKLAPNEQGYSKAMS 82
Cdd:cd19136 1 MPILGLGTFRLRGeEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 83 ALTSSLQRLNTSYLDLYLIHWPGAAKTPLESPANKRLRLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCV 162
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSDPRNAELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 163 NQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGVqsLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQ 242
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLR--LLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPE 238
|
250 260
....*....|....*....|....*
gi 428171326 243 RLAENLETTqVFEHDESTDTQGNRL 267
Cdd:cd19136 239 RIAENIKVF-DFELSEEDMAELNAL 262
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
8-249 |
5.96e-106 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 307.87 E-value: 5.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTSS 87
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWPGaaktPLESPANKRLRLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVEL 167
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPV----PGKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQIEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 168 HPACFQEELLRFCEAHKVQVQAYSPLGSPAGvqSLLSNADVLRASKEEGVSAAQVLIRWAMQTcGSAV-ARSSNEQRLAE 246
Cdd:cd19071 157 HPYLQQKELVEFCKEHGIVVQAYSPLGRGRR--PLLDDPVLKEIAKKYGKTPAQVLLRWALQR-GVVViPKSSNPERIKE 233
|
...
gi 428171326 247 NLE 249
Cdd:cd19071 234 NLD 236
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
7-249 |
4.32e-101 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 295.81 E-value: 4.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTS 86
Cdd:COG0656 4 EIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAAFEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGaaKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVE 166
Cdd:COG0656 84 SLERLGLDYLDLYLIHWPG--PGPYV---------ETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPAVNQVE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLGSPagvqSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLAE 246
Cdd:COG0656 153 LHPYLQQRELLAFCREHGIVVEAYSPLGRG----KLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRE 228
|
...
gi 428171326 247 NLE 249
Cdd:COG0656 229 NLD 231
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-249 |
2.52e-80 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 243.45 E-value: 2.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLR-GEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTS 86
Cdd:cd19157 10 MPWLGLGVFKVEeGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYDSTLKAFEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGAAKtplespaNKrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVE 166
Cdd:cd19157 90 SLERLGLDYLDLYLIHWPVKGK-------YK----ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLgspagVQSLLSNADVLRA-SKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLA 245
Cdd:cd19157 159 FHPRLTQKELRDYCKKQGIQLEAWSPL-----MQGQLLDNPVLKEiAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRII 233
|
....
gi 428171326 246 ENLE 249
Cdd:cd19157 234 ENAD 237
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-261 |
1.38e-77 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 235.79 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLR-GEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTS 86
Cdd:cd19126 9 MPWLGLGVFQTPdGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARRTEDAFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGAAKTplespankrlrLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVE 166
Cdd:cd19126 89 SLDRLGLDYVDLYLIHWPGKDKF-----------IDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLGSpagvQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLAE 246
Cdd:cd19126 158 FHPYLTQKELRGYCKSKGIVVEAWSPLGQ----GGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKE 233
|
250
....*....|....*
gi 428171326 247 NLEttqVFEHDESTD 261
Cdd:cd19126 234 NAD---IFDFELSED 245
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
3-249 |
1.66e-77 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 235.63 E-value: 1.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 3 EAAGSLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMS 82
Cdd:cd19132 2 NDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 83 ALTSSLQRLNTSYLDLYLIHWPgaaktpleSPaNKRLRLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCV 162
Cdd:cd19132 82 TIEESLYRLGLDYVDLYLIHWP--------NP-SRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 163 NQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGvqsLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQ 242
Cdd:cd19132 153 NQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---LLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPE 229
|
....*..
gi 428171326 243 RLAENLE 249
Cdd:cd19132 230 RQRENLA 236
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-248 |
1.17e-76 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 233.42 E-value: 1.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTS 86
Cdd:cd19131 9 TIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDSTLRAFDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPgaaktpleSPANKRLrLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVE 166
Cdd:cd19131 89 SLRKLGLDYVDLYLIHWP--------VPAQDKY-VETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLGSpagvQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLAE 246
Cdd:cd19131 160 LHPRFQQRELRAFHAKHGIQTESWSPLGQ----GGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAE 235
|
..
gi 428171326 247 NL 248
Cdd:cd19131 236 NF 237
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-247 |
6.94e-76 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 232.02 E-value: 6.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLR-GEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTS 86
Cdd:cd19156 9 MPRLGLGVWRVQdGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYESTLAAFEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGAAKTplespankrlrLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVE 166
Cdd:cd19156 89 SLEKLGLDYVDLYLIHWPVKGKF-----------KDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLGSpagvQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLAE 246
Cdd:cd19156 158 LHPLLTQEPLRKFCKEKNIAVEAWSPLGQ----GKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQE 233
|
.
gi 428171326 247 N 247
Cdd:cd19156 234 N 234
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
8-249 |
3.04e-74 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 227.15 E-value: 3.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTSS 87
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWPGAAKtPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVEL 167
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNPTV-PLE---------ETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQVEF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 168 HPACFQEELLRFCEAHKVQVQAYSPLGspagvQSLLSNADVLRA-SKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLAE 246
Cdd:cd19073 151 HPFLYQAELLEYCRENDIVITAYSPLA-----RGEVLRDPVIQEiAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKE 225
|
...
gi 428171326 247 NLE 249
Cdd:cd19073 226 NLA 228
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-254 |
6.14e-74 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 226.82 E-value: 6.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASrATQQAM-ELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTS 86
Cdd:cd19135 13 MPILGLGTSHSGGYSHE-AVVYALkECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYESTKQAFEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGAaktPLESPANKRLRLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVE 166
Cdd:cd19135 92 SLKRLGVDYLDLYLLHWPDC---PSSGKNVKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVPHVNQVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLGSpagvQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLAE 246
Cdd:cd19135 169 FHPFQNPVELIEYCRDNNIVFEGYCPLAK----GKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKE 244
|
....*...
gi 428171326 247 NletTQVF 254
Cdd:cd19135 245 N---CQVF 249
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
6-254 |
3.29e-72 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 223.38 E-value: 3.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 6 GSLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASG----VRREDVFITSKLAPNEQGYSKAM 81
Cdd:cd19125 9 AKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDHAPEDVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 82 SALTSSLQRLNTSYLDLYLIHWPGAAK--TPLESPANK-RLRLES-WQALEDALKLGMIRRAGVSNFCVRHLQELLACSE 157
Cdd:cd19125 89 PALEKTLKDLQLDYLDLYLIHWPVRLKkgAHMPEPEEVlPPDIPStWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 158 LVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAG---VQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSA 234
Cdd:cd19125 169 VPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTtwvKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQRGTSV 248
|
250 260
....*....|....*....|
gi 428171326 235 VARSSNEQRLAENLettQVF 254
Cdd:cd19125 249 LPKSTNEERIKENI---DVF 265
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-259 |
2.32e-71 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 221.52 E-value: 2.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAA----SGVRREDVFITSKLAPNEQGYSKAMSA 83
Cdd:cd19123 12 IPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEvfkeGKVKREDLWITSKLWNNSHAPEDVLPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 84 LTSSLQRLNTSYLDLYLIHWPGAAKTPLESPANKRLRL--------ESWQALEDALKLGMIRRAGVSNFCVRHLQELLAC 155
Cdd:cd19123 92 LEKTLADLQLDYLDLYLMHWPVALKKGVGFPESGEDLLslspipleDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLAT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 156 SELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSP--------AGVQSLLSNADVLRASKEEGVSAAQVLIRWA 227
Cdd:cd19123 172 ARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGdrpaamkaEGEPVLLEDPVINKIAEKHGASPAQVLIAWA 251
|
250 260 270
....*....|....*....|....*....|..
gi 428171326 228 MQTCGSAVARSSNEQRLAENLETTQVfEHDES 259
Cdd:cd19123 252 IQRGTVVIPKSVNPERIQQNLEAAEV-ELDAS 282
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
9-249 |
1.61e-70 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 217.83 E-value: 1.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGTFQLRG-EEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTSS 87
Cdd:cd19133 10 PILGFGVFQIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEKAKKAFERS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWP-----GAaktplespankrlrlesWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCV 162
Cdd:cd19133 90 LKRLGLDYLDLYLIHQPfgdvyGA-----------------WRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKPAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 163 NQVELHPACFQEELLRFCEAHKVQVQAYSPLGspAGVQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQ 242
Cdd:cd19133 153 NQIETHPFNQQIEAVEFLKKYGVQIEAWGPFA--EGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPE 230
|
....*..
gi 428171326 243 RLAENLE 249
Cdd:cd19133 231 RIAENFD 237
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-249 |
1.10e-69 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 217.15 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEE-ASRATQQAMELGYRAIDTASIYRNEEDIAMGLA---ASG-VRREDVFITSKLAPNEQGYSKAMS 82
Cdd:cd19116 11 IPAIALGTWKLKDDEgVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIRekiAEGvVKREDLFITTKLWNSYHEREQVEP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 83 ALTSSLQRLNTSYLDLYLIHWPGAAKTPLESPANKRLR------LESWQALEDALKLGMIRRAGVSNFCVRHLQELLACS 156
Cdd:cd19116 91 ALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGSlsdidyLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 157 ELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPA-----GVQSLLSNADVLRASKEEGVSAAQVLIRWAMQTC 231
Cdd:cd19116 171 NIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVprgqtNPPPRLDDPTLVAIAKKYGKTTAQIVLRYLIDRG 250
|
250
....*....|....*...
gi 428171326 232 GSAVARSSNEQRLAENLE 249
Cdd:cd19116 251 VVPIPKSSNKKRIKENID 268
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-249 |
5.10e-68 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 211.88 E-value: 5.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTSS 87
Cdd:cd19127 9 MPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDKALRGFDAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWPgaaktpleSPANKRLRLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVEL 167
Cdd:cd19127 89 LRRLGLDYVDLYLLHWP--------VPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAVNQVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 168 HPACFQEELLRFCEAHKVQVQAYSPLGS--------PAGVQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSS 239
Cdd:cd19127 161 HPYFSQKDLRAFHRRLGIVTQAWSPIGGvmrygasgPTGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSV 240
|
250
....*....|
gi 428171326 240 NEQRLAENLE 249
Cdd:cd19127 241 HPERIAENID 250
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
7-264 |
1.81e-67 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 210.48 E-value: 1.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTS 86
Cdd:cd19134 10 TMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTASQAACRA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGAAKTPLespankrlrLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVE 166
Cdd:cd19134 90 SLERLGLDYVDLYLIHWPAGREGKY---------VDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLgspaGVQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLAE 246
Cdd:cd19134 161 LHPLLNQAELRKVNAQHGIVTQAYSPL----GVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIAS 236
|
250
....*....|....*...
gi 428171326 247 NLettQVFEHDESTDTQG 264
Cdd:cd19134 237 NL---DVFDFELTADHMD 251
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
7-250 |
2.08e-66 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 207.86 E-value: 2.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGT----FQLRGEEASR----ATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYS 78
Cdd:cd19120 3 KIPAIAFGTgtawYKSGDDDIQRdlvdSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGIKDPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 79 KamsALTSSLQRLNTSYLDLYLIHWPGAAKTPLESPAnkrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSEL 158
Cdd:cd19120 83 E---ALRKSLAKLGVDYVDLYLIHSPFFAKEGGPTLA------EAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 159 VPCVNQVELHPAC--FQEELLRFCEAHKVQVQAYSPLgspagvQSLLSNAD------VLRASKEEGVSAAQVLIRWAMQT 230
Cdd:cd19120 154 KPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSPL------SPLTRDAGgpldpvLEKIAEKYGVTPAQVLLRWALQK 227
|
250 260
....*....|....*....|
gi 428171326 231 CGSAVARSSNEQRLAENLET 250
Cdd:cd19120 228 GIVVVTTSSKEERMKEYLEA 247
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
8-249 |
3.76e-65 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 205.19 E-value: 3.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGT--FQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLA---ASGV--RREDVFITSKLAPNEQGYSKA 80
Cdd:cd19124 5 MPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGLvkSRDELFVTSKLWCSDAHPDLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 81 MSALTSSLQRLNTSYLDLYLIHWP-----GAAKTPLESPANKRLRLES-WQALEDALKLGMIRRAGVSNFCVRHLQELLA 154
Cdd:cd19124 85 LPALKKSLRNLQLEYVDLYLIHWPvslkpGKFSFPIEEEDFLPFDIKGvWEAMEECQRLGLTKAIGVSNFSCKKLQELLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 155 CSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPA---GVQSLLSNADVLRASKEEGVSAAQVLIRWAMQTC 231
Cdd:cd19124 165 FATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGtkwGSNAVMESDVLKEIAAAKGKTVAQVSLRWVYEQG 244
|
250
....*....|....*...
gi 428171326 232 GSAVARSSNEQRLAENLE 249
Cdd:cd19124 245 VSLVVKSFNKERMKQNLD 262
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
8-250 |
1.81e-64 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 202.49 E-value: 1.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTSS 87
Cdd:cd19140 8 IPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLASVEES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVEL 167
Cdd:cd19140 88 LRKLRTDYVDLLLLHWPN-KDVPLA---------ETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTNQVEY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 168 HPACFQEELLRFCEAHKVQVQAYSPLGSPAgvqsLLSNADVLRASKEEGVSAAQVLIRWAMQTCG-SAVARSSNEQRLAE 246
Cdd:cd19140 158 HPYLDQRKLLDAAREHGIALTAYSPLARGE----VLKDPVLQEIGRKHGKTPAQVALRWLLQQEGvAAIPKATNPERLEE 233
|
....
gi 428171326 247 NLET 250
Cdd:cd19140 234 NLDI 237
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
7-257 |
3.61e-63 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 200.06 E-value: 3.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLA---ASGVRREDVFITSKLAPNEqgYSKAMSA 83
Cdd:cd19121 11 SIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKeaiAGGVKREDLFVTTKLWSTY--HRRVELC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 84 LTSSLQRLNTSYLDLYLIHWPgaakTPLESPANKRL----------------RLESWQALEDALKLGMIRRAGVSNFCVR 147
Cdd:cd19121 89 LDRSLKSLGLDYVDLYLVHWP----VLLNPNGNHDLfptlpdgsrdldwdwnHVDTWKQMEKVLKTGKTKAIGVSNYSIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 148 HLQELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGvqSLLSNADVLRASKEEGVSAAQVLIRWA 227
Cdd:cd19121 165 YLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGS--PLISDEPVVEIAKKHNVGPGTVLISYQ 242
|
250 260 270
....*....|....*....|....*....|
gi 428171326 228 MQTCGSAVARSSNEQRLAENLETTQVFEHD 257
Cdd:cd19121 243 VARGAVVLPKSVTPDRIKSNLEIIDLDDED 272
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-249 |
7.59e-63 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 199.26 E-value: 7.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQgySKAMSALTS 86
Cdd:cd19117 13 EIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWH--RRVEEALDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPgaakTPLESPANKRLRLE---------------SWQALEDALKLGMIRRAGVSNFCVRHLQE 151
Cdd:cd19117 91 SLKKLGLDYVDLYLMHWP----VPLDPDGNDFLFKKddgtkdhepdwdfikTWELMQKLPATGKVKAIGVSNFSIKNLEK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 152 LLA--CSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGvqSLLSNADVLRASKEEGVSAAQVLIRWAMQ 229
Cdd:cd19117 167 LLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNA--PLLKEPVIIKIAKKHGKTPAQVIISWGLQ 244
|
250 260
....*....|....*....|
gi 428171326 230 TCGSAVARSSNEQRLAENLE 249
Cdd:cd19117 245 RGYSVLPKSVTPSRIESNFK 264
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
6-250 |
1.11e-62 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 199.56 E-value: 1.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 6 GSLPPLF-FGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLA---ASGV-RREDVFITSKLAPNEQGYSKA 80
Cdd:cd19154 9 GVKMPLIgLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAellEEGVvKREDLFITTKLWTHEHAPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 81 MSALTSSLQRLNTSYLDLYLIHWPGAAKtPLESPANKRLR----------LESWQALEDALKLGMIRRAGVSNFCVRHLQ 150
Cdd:cd19154 89 EEALRESLKKLQLEYVDLYLIHAPAAFK-DDEGESGTMENgmsihdavdvEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 151 ELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSP-----------AGVQSLLSNADVLRASKEEGVSA 219
Cdd:cd19154 168 RILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPgranftkstgvSPAPNLLQDPIVKAIAEKHGKTP 247
|
250 260 270
....*....|....*....|....*....|.
gi 428171326 220 AQVLIRWAMQTCGSAVARSSNEQRLAENLET 250
Cdd:cd19154 248 AQVLLRYLLQRGIAVIPKSATPSRIKENFNI 278
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-249 |
4.52e-62 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 197.25 E-value: 4.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLA-----ASGVRREDVFITSKLAPNEQGYSKAM 81
Cdd:cd19118 6 KIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKellkeEPGVKREDLFITSKLWNNSHRPEYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 82 SALTSSLQRLNTSYLDLYLIHWPGAAK--TPLES----PANKRLRL--------ESWQALEDALKLGMIRRAGVSNFCVR 147
Cdd:cd19118 86 PALDDTLKELGLDYLDLYLIHWPVAFKptGDLNPltavPTNGGEVDldlsvslvDTWKAMVELKKTGKVKSIGVSNFSID 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 148 HLQELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLG-SPAGVQSLLSNADVLRASKEEGVSAAQVLIRW 226
Cdd:cd19118 166 HLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGnNLAGLPLLVQHPEVKAIAAKLGKTPAQVLIAW 245
|
250 260
....*....|....*....|...
gi 428171326 227 AMQTCGSAVARSSNEQRLAENLE 249
Cdd:cd19118 246 GIQRGHSVIPKSVTPSRIRSNFE 268
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
7-261 |
1.10e-61 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 195.51 E-value: 1.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTS 86
Cdd:cd19130 9 SIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEPAAAFAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGAAKTplespankrLRLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVE 166
Cdd:cd19130 89 SLAKLGLDQVDLYLVHWPTPAAG---------NYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLGSpagvQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLAE 246
Cdd:cd19130 160 LHPAYQQRTIRDWAQAHDVKIEAWSPLGQ----GKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMED 235
|
250
....*....|....*
gi 428171326 247 NLEttqVFEHDESTD 261
Cdd:cd19130 236 NLD---VFDFDLTDT 247
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-267 |
1.76e-57 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 185.28 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQgySKAMSALTSS 87
Cdd:PRK11565 15 MPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDH--KRPREALEES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWPgaaktpleSPANKRLrLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVEL 167
Cdd:PRK11565 93 LKKLQLDYVDLYLMHWP--------VPAIDHY-VEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 168 HPACFQEELLRFCEAHKVQVQAYSPLGSpaGVQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLAEN 247
Cdd:PRK11565 164 HPLMQQRQLHAWNATHKIQTESWSPLAQ--GGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAEN 241
|
250 260
....*....|....*....|....*...
gi 428171326 248 LEttqVF----EHDESTDT----QGNRL 267
Cdd:PRK11565 242 FD---VFdfrlDKDELGEIakldQGKRL 266
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-255 |
6.96e-57 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 184.51 E-value: 6.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAAS-----GVRREDVFITSKLAPNEQGYSKAMS 82
Cdd:cd19106 7 MPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKHHPEDVEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 83 ALTSSLQRLNTSYLDLYLIHWPGAAK---TPLESPANKRLR------LESWQALEDALKLGMIRRAGVSNFCVRHLQELL 153
Cdd:cd19106 87 ALRKTLKDLQLDYLDLYLIHWPYAFErgdNPFPKNPDGTIRydsthyKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 154 ACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSP------AGVQSLLSNADVLRASKEEGVSAAQVLIRWA 227
Cdd:cd19106 167 SVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPdrpwakPDEPVLLEEPKVKALAKKYNKSPAQILLRWQ 246
|
250 260
....*....|....*....|....*...
gi 428171326 228 MQTCGSAVARSSNEQRLAENLettQVFE 255
Cdd:cd19106 247 VQRGVVVIPKSVTPSRIKQNI---QVFD 271
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
6-257 |
1.56e-55 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 180.93 E-value: 1.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 6 GSLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAAS----GVRREDVFITSKLAPNEQGYSKAM 81
Cdd:cd19110 2 EDIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKikegVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 82 SALTSSLQRLNTSYLDLYLIHWP-----GAAKTPLES-----PANKRLrLESWQALEDALKLGMIRRAGVSNFCVRHLQE 151
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPmgfkpGEPDLPLDRsgmviPSDTDF-LDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 152 LLACSEL--VPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGVQSLLSNADVLRASKEEGVSAAQVLIRWAMQ 229
Cdd:cd19110 161 LLNKPGLrvKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVDLIDDPVIQRIAKKHGKSPAQILIRFQIQ 240
|
250 260 270
....*....|....*....|....*....|...
gi 428171326 230 TCGSAVARSSNEQRLAENLettQVF-----EHD 257
Cdd:cd19110 241 RNVIVIPKSVTPSRIKENI---QVFdfeltEHD 270
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
8-253 |
2.83e-54 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 176.00 E-value: 2.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTSS 87
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWPgaaktpleSPANKRLRLESWQALEDALKLGMIRRAGVSNFCVRHLQELLAC-SELVPCVNQVE 166
Cdd:cd19139 81 LEKLRTDYVDLTLIHWP--------SPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVvGAGAIATNQIE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLGspagvQSLLSNADVLRA-SKEEGVSAAQVLIRWAMQTCGSAVARSSNEQRLA 245
Cdd:cd19139 153 LSPYLQNRKLVAHCKQHGIHVTSYMTLA-----YGKVLDDPVLAAiAERHGATPAQIALAWAMARGYAVIPSSTKREHLR 227
|
....*...
gi 428171326 246 ENLETTQV 253
Cdd:cd19139 228 SNLLALDL 235
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
8-249 |
6.67e-54 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 176.53 E-value: 6.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLA---ASG-VRREDVFITSKLAPNEQGYSKAMSA 83
Cdd:cd19111 4 MPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDTEKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 84 LTSSLQRLNTSYLDLYLIHWPGA---AKTPLESPANKRLRLESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVP 160
Cdd:cd19111 84 LEKSLENLKLPYVDLYLIHHPCGfvnKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAKVKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 161 CVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGVQ--------SLLSNADVLRASKEEGVSAAQVLIRWAMQTCG 232
Cdd:cd19111 164 SNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANqslwpdqpDLLEDPTVLAIAKELDKTPAQVLLRFVLQRGT 243
|
250
....*....|....*..
gi 428171326 233 SAVARSSNEQRLAENLE 249
Cdd:cd19111 244 GVLPKSTNKERIEENFE 260
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
7-248 |
4.04e-53 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 173.67 E-value: 4.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSKAMSALTS 86
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPgaaktpleSPANKRLRLESWQALEDALKLGMIRRAGVSNFCVRHLQELLAC--SELVpCVNQ 164
Cdd:PRK11172 82 SLQKLRTDYVDLTLIHWP--------SPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAvgAENI-ATNQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 165 VELHPACFQEELLRFCEAHKVQVQAYSPLgspaGVQSLLSNADVLRASKEEGVSAAQVLIRWAMQTcGSAVARSSNE-QR 243
Cdd:PRK11172 153 IELSPYLQNRKVVAFAKEHGIHVTSYMTL----AYGKVLKDPVIARIAAKHNATPAQVILAWAMQL-GYSVIPSSTKrEN 227
|
....*
gi 428171326 244 LAENL 248
Cdd:PRK11172 228 LASNL 232
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
8-255 |
2.17e-51 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 170.40 E-value: 2.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGL----AASGVRREDVFITSKLAPNEQGYSKAMSA 83
Cdd:cd19155 12 MPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLkkwiDSGKVKREELFIVTKLPPGGNRREKVEKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 84 LTSSLQRLNTSYLDLYLIHWP-----------GAAKTPLESPANKRLRLESWQALEDALKLGMIRRAGVSNFCVRHLQEL 152
Cdd:cd19155 92 LLKSLEKLQLDYVDLYLIHFPvgslskeddsgKLDPTGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 153 LACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPA-------------GVQSLLSNADVLRASKEEGVSA 219
Cdd:cd19155 172 LKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGaahfspgtgspsgSSPDLLQDPVVKAIAERHGKSP 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 428171326 220 AQVLIRWAMQTCGSAVARSSNEQRLAENLettQVFE 255
Cdd:cd19155 252 AQVLLRWLMQRGVVVIPKSTNAARIKENF---QVFD 284
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
7-255 |
6.09e-51 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 169.59 E-value: 6.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAASG----VRREDVFITSKLAPNEQGYSKamS 82
Cdd:cd19112 10 KMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLWNSDHGHVI--E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 83 ALTSSLQRLNTSYLDLYLIHWPGAAK-TPLESPA-----------NKRLRLES-WQALEDALKLGMIRRAGVSNFCVRHL 149
Cdd:cd19112 88 ACKDSLKKLQLDYLDLYLVHFPVATKhTGVGTTGsalgedgvldiDVTISLETtWHAMEKLVSAGLVRSIGISNYDIFLT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 150 QELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPA------GVQSLLSNADVLRASKEEGVSAAQVL 223
Cdd:cd19112 168 RDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAanaewfGSVSPLDDPVLKDLAKKYGKSAAQIV 247
|
250 260 270
....*....|....*....|....*....|..
gi 428171326 224 IRWAMQTCGSAVARSSNEQRLAENLEttqVFE 255
Cdd:cd19112 248 LRWGIQRNTAVIPKSSKPERLKENID---VFD 276
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
7-252 |
1.01e-48 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 162.40 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRG---------EEASRATQQAMELGYRAIDTASIY---RNEEDIAMglAASGVRREDVFITSKLAPNE 74
Cdd:cd19072 3 EVPVLGLGTWGIGGgmskdysddKKAIEALRYAIELGINLIDTAEMYgggHAEELVGK--AIKGFDREDLFITTKVSPDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 75 QGYSKAMSALTSSLQRLNTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLA 154
Cdd:cd19072 81 LKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPS-IPIE---------ETLRAMEELVEEGKIRYIGVSNFSLEELEEAQS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 155 CSELVPCV-NQVELHPAcFQEE---LLRFCEAHKVQVQAYSPLGspagvQSLLSNADVLRA----SKEEGVSAAQVLIRW 226
Cdd:cd19072 151 YLKKGPIVaNQVEYNLF-DREEesgLLPYCQKNGIAIIAYSPLE-----KGKLSNAKGSPLldeiAKKYGKTPAQIALNW 224
|
250 260
....*....|....*....|....*..
gi 428171326 227 AMQTCGS-AVARSSNEQRLAENLETTQ 252
Cdd:cd19072 225 LISKPNViAIPKASNIEHLEENAGALG 251
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-253 |
2.56e-48 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 161.26 E-value: 2.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLrGEEASRATQQ------AMELGYRAIDTASIYRN--EEDIAmGLAASGvRREDVFITSKLAPNEQGYSK 79
Cdd:cd19138 11 VPALGQGTWYM-GEDPAKRAQEiealraGIDLGMTLIDTAEMYGDggSEELV-GEAIRG-RRDKVFLVSKVLPSNASRQG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 80 AMSALTSSLQRLNTSYLDLYLIHWPGAakTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELV 159
Cdd:cd19138 88 TVRACERSLRRLGTDYLDLYLLHWRGG--VPLA---------ETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 160 PCV-NQVELHPAC--FQEELLRFCEAHKVQVQAYSPLGS-PAGVQSLLSNADVLRASKEEGVSAAQVLIRWAMqTCGSAV 235
Cdd:cd19138 157 NCAaNQVLYNLGSrgIEYDLLPWCREHGVPVMAYSPLAQgGLLRRGLLENPTLKEIAARHGATPAQVALAWVL-RDGNVI 235
|
250 260
....*....|....*....|
gi 428171326 236 A--RSSNEQRLAENLETTQV 253
Cdd:cd19138 236 AipKSGSPEHARENAAAADL 255
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
9-261 |
2.89e-48 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 161.54 E-value: 2.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAA----SGVRREDVFITSKLAPNEQGYSKAMSAL 84
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 85 TSSLQRLNTSYLDLYLIHWPGA------------------AKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCV 146
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAfdmdtdgdprddnqiqslSKKPLE---------DTWRAMEQCVDEKLTKNIGVSNYST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 147 RHLQELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGVQSL-LSNADVLRA-SKEEGVSAAQVLI 224
Cdd:cd19128 153 KLLTDLLNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNLtFLNDSELKAlATKYNTTPPQVII 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 428171326 225 RWAMQTCG---SAVARSSNEQRLAENLETTQVFEHDESTD 261
Cdd:cd19128 233 AWHLQKWPknySVIPKSANKSRCQQNFDINDLALTKEDMD 272
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
8-255 |
1.81e-47 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 160.28 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAA----SGVRREDVFITSKLAPNEQGYSKAMSA 83
Cdd:cd19107 4 MPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEkikeQVVKREDLFIVSKLWCTFHEKGLVKGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 84 LTSSLQRLNTSYLDLYLIHWP-----GAAKTPLES-----PANKRLrLESWQALEDALKLGMIRRAGVSNFCVRHLQELL 153
Cdd:cd19107 84 CQKTLSDLKLDYLDLYLIHWPtgfkpGKELFPLDEsgnviPSDTTF-LDTWEAMEELVDEGLVKAIGVSNFNHLQIERIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 154 ACSELV--PCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSP------AGVQSLLSNADVLRASKEEGVSAAQVLIR 225
Cdd:cd19107 163 NKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakPEDPSLLEDPKIKEIAAKHNKTTAQVLIR 242
|
250 260 270
....*....|....*....|....*....|
gi 428171326 226 WAMQTCGSAVARSSNEQRLAENLettQVFE 255
Cdd:cd19107 243 FPIQRNLVVIPKSVTPERIAENF---KVFD 269
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-257 |
3.09e-46 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 156.63 E-value: 3.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGE--EASRATQQAMELGYRAIDTASIYRNEEDIAMGL-----AASGVRREDVFITSKLAPNEQGYSKA 80
Cdd:cd19122 9 IPAVGFGTFANEGAkgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVrdflkENPSVKREDLFICTKVWNHLHEPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 81 MSALTSSLQRLNTSYLDLYLIHWPGAAK-----TPLESPANKRLRLE--------SWQALEDALKLGMIRRAGVSNFCVR 147
Cdd:cd19122 89 KWSIDNSLKNLKLDYIDLFLVHWPIAAEkndqrSPKLGPDGKYVILKdltenpepTWRAMEEIYESGKAKAIGVSNWTIP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 148 HLQELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGS----PAGVQSLLSNADVLRASKEEGVSAAQVL 223
Cdd:cd19122 169 GLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqnqvPSTGERVSENPTLNEVAEKGGYSLAQVL 248
|
250 260 270
....*....|....*....|....*....|....
gi 428171326 224 IRWAMQTCGSAVARSSNEQRLAENLETTQVFEHD 257
Cdd:cd19122 249 IAWGLRRGYVVLPKSSTPSRIESNFKSIELSDED 282
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
13-249 |
5.14e-46 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 155.93 E-value: 5.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 13 FGTFQLRG-------EEASRATQQAMELGYRAIDTASIYR---NEEDIAMGLAASGVRREDVFITSKL----APNEQGYS 78
Cdd:pfam00248 3 LGTWQLGGgwgpiskEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVpdgdGPWPSGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 79 KA--MSALTSSLQRLNTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACS 156
Cdd:pfam00248 83 KEniRKSLEESLKRLGTDYIDLYYLHWPDPD-TPIE---------ETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 157 ELVPCVNQVELHPAC--FQEELLRFCEAHKVQVQAYSPLGSPAGVQSLLSNADVLRAS---------------------- 212
Cdd:pfam00248 153 KIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGErrrllkkgtplnlealealeei 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 428171326 213 -KEEGVSAAQVLIRWAMQ--TCGSAVARSSNEQRLAENLE 249
Cdd:pfam00248 233 aKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLG 272
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
7-255 |
1.45e-44 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 152.77 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTF---QLRGEEASRATQQAMELGYRAIDTASIYRNEEDIamGLA-----ASG-VRREDVFITSKLAPNEQGY 77
Cdd:cd19108 10 FIPVLGFGTYapeEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEV--GQAirskiADGtVKREDIFYTSKLWCTFHRP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 78 SKAMSALTSSLQRLNTSYLDLYLIHWPGAAK---TPLESPANKRLRLES------WQALEDALKLGMIRRAGVSNFCVRH 148
Cdd:cd19108 88 ELVRPALEKSLKKLQLDYVDLYLIHFPVALKpgeELFPKDENGKLIFDTvdlcatWEAMEKCKDAGLAKSIGVSNFNRRQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 149 LQELLACSEL--VPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGS---PAGV-QSL--LSNADVLRA-SKEEGVSA 219
Cdd:cd19108 168 LEMILNKPGLkyKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSqrdKEWVdQNSpvLLEDPVLCAlAKKHKRTP 247
|
250 260 270
....*....|....*....|....*....|....*.
gi 428171326 220 AQVLIRWAMQTCGSAVARSSNEQRLAENLettQVFE 255
Cdd:cd19108 248 ALIALRYQLQRGVVVLAKSFNEKRIKENL---QVFE 280
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
6-251 |
1.90e-44 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 152.23 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 6 GSLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDI--AM--GLAASGVRREDVFITSKLAPNEQGYSKAM 81
Cdd:cd19129 4 GAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVgeAMqeVFKAGKIRREDLFVTTKLWNTNHRPERVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 82 SALTSSLQRLNTSYLDLYLIHWPGAAKTPLES-PANKRLR---------LESWQALEDALKLGMIRRAGVSNFCVRHLQE 151
Cdd:cd19129 84 PAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQdPRDANGNviyddgvtlLDTWRAMERLVDEGRCKAIGLSDVSLEKLRE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 152 LLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSpAGVQSLLSNADVLRASKEEGVSAAQVLIRWAMQTC 231
Cdd:cd19129 164 IFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGH-GMEPKLLEDPVITAIARRVNKTPAQVLLAWAIQRG 242
|
250 260
....*....|....*....|
gi 428171326 232 GSAVARSSNEQRLAENLETT 251
Cdd:cd19129 243 TALLTTSKTPSRIRENFDIS 262
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
7-249 |
4.22e-44 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 151.11 E-value: 4.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTF--QLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMG----LAASGVRREDVFITSKLAPNEqgYSKA 80
Cdd:cd19119 11 SIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAikraIDDGSIKREELFITTKVWPTF--YDEV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 81 MSALTSSLQRLNTSYLDLYLIHWP----------GAAKTPlESPANKRLR------LESWQALEDALKLGMIRRAGVSNF 144
Cdd:cd19119 89 ERSLDESLKALGLDYVDLLLVHWPvcfekdsddsGKPFTP-VNDDGKTRYaasgdhITTYKQLEKIYLDGRAKAIGVSNY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 145 CVRHLQELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGvqSLLSNADVLRASKEEGVSAAQVLI 224
Cdd:cd19119 168 SIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGA--PNLKNPLVKKIAEKYNVSTGDILI 245
|
250 260
....*....|....*....|....*
gi 428171326 225 RWAMQTCGSAVARSSNEQRLAENLE 249
Cdd:cd19119 246 SYHVRQGVIVLPKSLKPVRIVSNGK 270
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
8-262 |
1.11e-42 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 147.70 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAAS----GVRREDVFITSKLAPNEQGYSKAMSA 83
Cdd:cd19114 4 MPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAiqegLVKREDLFIVTKLWNNFHGKDHVREA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 84 LTSSLQRLNTSYLDLYLIHWPGAAK--------TPL-ESPANKRLRLES------WQALEDALKLGMIRRAGVSNFCVRH 148
Cdd:cd19114 84 FDRQLKDYGLDYIDLYLIHFPIPAAyvdpaenyPFLwKDKELKKFPLEQspmqecWREMEKLVDAGLVRNIGIANFNVQL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 149 LQELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGVQ---------SLLSNADVLRASKEEGVSA 219
Cdd:cd19114 164 ILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKvtkhlkhftNLLEHPVVKKLADKHKRDT 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 428171326 220 AQVLIRWAMQTCGSAVARSSNEQRLAENLETTQVFEHDESTDT 262
Cdd:cd19114 244 GQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEA 286
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-249 |
7.56e-42 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 146.05 E-value: 7.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMG----LAASGVRREDVFITSKLAPNEQGYSKAMSA 83
Cdd:cd19113 11 MPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGvnraIDEGLVKREELFLTSKLWNNFHDPKNVETA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 84 LTSSLQRLNTSYLDLYLIHWPGAAK-TPLE---------------SPANKRLrLESWQALEDALKLGMIRRAGVSNFCVR 147
Cdd:cd19113 91 LNKTLSDLKLDYVDLFLIHFPIAFKfVPIEekyppgfycgdgdnfVYEDVPI-LDTWKALEKLVDAGKIKSIGVSNFPGA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 148 HLQELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSPAGV----------QSLLSNADVLRASKEEGV 217
Cdd:cd19113 170 LILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVelnqgralntPTLFEHDTIKSIAAKHNK 249
|
250 260 270
....*....|....*....|....*....|..
gi 428171326 218 SAAQVLIRWAMQTCGSAVARSSNEQRLAENLE 249
Cdd:cd19113 250 TPAQVLLRWATQRGIAVIPKSNLPERLLQNLS 281
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
8-253 |
5.79e-40 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 139.63 E-value: 5.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRG---------EEASRATQQAMELGYRAIDTASIY-RNEEDIAMGLAASGVRREDVFITSKLAPNEQGY 77
Cdd:cd19137 4 IPALGLGTWGIGGfltpdysrdEEMVELLKTAIELGYTHIDTAEMYgGGHTEELVGKAIKDFPREDLFIVTKVWPTNLRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 78 SKAMSALTSSLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSE 157
Cdd:cd19137 84 DDLLRSLQNSLRRLDTDYIDLYLIHWPN-PNIPLE---------ETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 158 LVPCVNQVELH---PACFQEELLRFCEAHKVQVQAYSPLGSPAgvqsLLSNADVLRASKEEGVSAAQVLIRWAMQTCG-S 233
Cdd:cd19137 154 TPIVCNQVKYNledRDPERDGLLEYCQKNGITVVAYSPLRRGL----EKTNRTLEEIAKNYGKTIAQIALAWLIQKPNvV 229
|
250 260
....*....|....*....|
gi 428171326 234 AVARSSNEQRLAENLETTQV 253
Cdd:cd19137 230 AIPKAGRVEHLKENLKATEI 249
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
4-251 |
8.94e-40 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 140.63 E-value: 8.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 4 AAGSLPPLFFGTFQLRGEEASRATQQAMELGYRAIDTASIYRNEEDIAMGLAAS---G-VRREDVFITSKLAPNEQGYSK 79
Cdd:cd19115 9 SGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAikeGiVKREDLFIVSKLWNTFHDGER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 80 AMSALTSSLQRLNTSYLDLYLIHWPGAAK--------TPLESPANKRLRL------ESWQALEDALKLGMIRRAGVSNFC 145
Cdd:cd19115 89 VEPICRKQLADWGIDYFDLFLIHFPIALKyvdpavryPPGWFYDGKKVEFsnapiqETWTAMEKLVDKGLARSIGVSNFS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 146 VRHLQELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGsPAG-----------VQSLLSNADVLRASKE 214
Cdd:cd19115 169 AQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PQSfleldlpgakdTPPLFEHDVIKSIAEK 247
|
250 260 270
....*....|....*....|....*....|....*..
gi 428171326 215 EGVSAAQVLIRWAMQTCGSAVARSSNEQRLAENLETT 251
Cdd:cd19115 248 HGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVT 284
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
7-253 |
2.75e-38 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 136.46 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQL------RGEEASRAT-QQAMELGYRAIDTASIY---RNEEdiAMGLAASGVRREDVFITSKLA----- 71
Cdd:COG0667 12 KVSRLGLGTMTFggpwggVDEAEAIAIlDAALDAGINFFDTADVYgpgRSEE--LLGEALKGRPRDDVVIATKVGrrmgp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 72 -PNEQGYSKA--MSALTSSLQRLNTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRH 148
Cdd:COG0667 90 gPNGRGLSREhiRRAVEASLRRLGTDYIDLYQLHRPDPD-TPIE---------ETLGALDELVREGKIRYIGVSNYSAEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 149 LQELLACSE-LVPCV-NQVELHPAC--FQEELLRFCEAHKVQVQAYSPLGS-------------PAG------------V 199
Cdd:COG0667 160 LRRALAIAEgLPPIVaVQNEYSLLDrsAEEELLPAARELGVGVLAYSPLAGglltgkyrrgatfPEGdraatnfvqgylT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 428171326 200 QSLLSNADVLRA-SKEEGVSAAQVLIRWAMQ--TCGSAVARSSNEQRLAENLETTQV 253
Cdd:COG0667 240 ERNLALVDALRAiAAEHGVTPAQLALAWLLAqpGVTSVIPGARSPEQLEENLAAADL 296
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
7-255 |
5.19e-38 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 135.70 E-value: 5.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQ-----LRGEeASRATQQAMELGYRAIDTASIYRNEEDIAMG----LAASGVRREDVFITSKLAPNEQGY 77
Cdd:cd19109 3 SIPIIGLGTYSepkttPKGA-CAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAirekIAEGKVKREDIFYCGKLWNTCHPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 78 SKAMSALTSSLQRLNTSYLDLYLIHWPGAAKtPLES--PANKRLR--------LESWQALEDALKLGMIRRAGVSNFCVR 147
Cdd:cd19109 82 ELVRPTLERTLKVLQLDYVDLYIIEMPMAFK-PGDEiyPRDENGKwlyhktnlCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 148 HLQELLACSELV--PCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLGSP-----AGVQS--LLSNADVLRASKEEGVS 218
Cdd:cd19109 161 QLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrdpiwVNVSSppLLEDPLLNSIGKKYNKT 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 428171326 219 AAQVLIRWAMQTCGSAVARSSNEQRLAENLettQVFE 255
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENF---QIFD 274
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
8-253 |
1.29e-37 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 134.25 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRG---------EEASRATQQAMELGYRAIDTASIY---RNEEDIAMGLAAsgvRREDVFITSKLAPNEQ 75
Cdd:cd19085 1 VSRLGLGCWQFGGgywwgdqddEESIATIHAALDAGINFFDTAEAYgdgHSEEVLGKALKG---RRDDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 76 GYSKAMSALTSSLQRLNTSYLDLYLIHWPgAAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLAC 155
Cdd:cd19085 78 TPEDVRKSCERSLKRLGTDYIDLYQIHWP-SSDVPLE---------ETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 156 SELVpcVNQVELHPacFQ----EELLRFCEAHKVQVQAYSPLGspagvQSLL-----SNADV------------------ 208
Cdd:cd19085 148 GRID--SNQLPYNL--LWraieYEILPFCREHGIGVLAYSPLA-----QGLLtgkfsSAEDFppgdartrlfrhfepgae 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 428171326 209 ---------LRA-SKEEGVSAAQVLIRWAMQT--CGSAVARSSNEQRLAENLETTQV 253
Cdd:cd19085 219 eetfealekLKEiADELGVTMAQLALAWVLQQpgVTSVIVGARNPEQLEENAAAVDL 275
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
9-249 |
5.56e-36 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 128.41 E-value: 5.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGTFQLRG----EEASRATQQAMELGYRAIDTASIY---RNEEDIAMGLAASGVRrEDVFITSKLA------PNEQ 75
Cdd:cd06660 1 SRLGLGTMTFGGdgdeEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGNR-DDVVIATKGGhppggdPSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 76 GYSKA--MSALTSSLQRLNTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELL 153
Cdd:cd06660 80 RLSPEhiRRDLEESLRRLGTDYIDLYYLHRDDPS-TPVE---------ETLEALNELVREGKIRYIGVSNWSAERLAEAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 154 ACSELV----PCVNQVE---LHPACFQEELLRFCEAHKVQVQAYSPLGSpaGVqsllsnadvlraskeegvsaAQVLIRW 226
Cdd:cd06660 150 AYAKAHglpgFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR--GP--------------------AQLALAW 207
|
250 260
....*....|....*....|....*
gi 428171326 227 AMQTCG--SAVARSSNEQRLAENLE 249
Cdd:cd06660 208 LLSQPFvtVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-251 |
1.13e-35 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 129.18 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 13 FGTFQLRG--------EEASRATQQAMELGYRAIDTASIY---RNEEDIAMGLaasGVRREDVFITSK--LAPNEQGYSK 79
Cdd:cd19084 9 LGTWAIGGtwwgevddQESIEAIKAAIDLGINFFDTAPVYgfgHSEEILGKAL---KGRRDDVVIATKcgLRWDGGKGVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 80 A-------MSALTSSLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQEL 152
Cdd:cd19084 86 KdlspesiRKEVEQSLRRLQTDYIDLYQIHWPD-PNTPIE---------ETAEALEKLKKEGKIRYIGVSNFSVEQLEEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 153 LACSELVpcVNQVELHPAC--FQEELLRFCEAHKVQVQAYSPLGspagvQSLLSN------------------------- 205
Cdd:cd19084 156 RKYGPIV--SLQPPYSMLEreIEEELLPYCRENGIGVLPYGPLA-----QGLLTGkykkeptfppddrrsrfpffrgenf 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 428171326 206 ------ADVLRA-SKEEGVSAAQVLIRWAMQTCG--SAVARSSNEQRLAENLETT 251
Cdd:cd19084 229 eknleiVDKLKEiAEKYGKSLAQLAIAWTLAQPGvtSAIVGAKNPEQLEENAGAL 283
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
21-253 |
1.37e-29 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 113.86 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 21 EEASRATQQAMELGYRAIDTASIYRN-EEDIAMGLAASGvRREDVFITSKL------APNEQGYSKA--MSALTSSLQRL 91
Cdd:cd19091 39 EEADRLVDIALDAGINFFDTADVYSEgESEEILGKALKG-RRDDVLIATKVrgrmgeGPNDVGLSRHhiIRAVEASLKRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 92 NTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELV----PCVNQVEL 167
Cdd:cd19091 118 GTDYIDLYQLHGFDAL-TPLE---------ETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRglarFVALQAYY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 168 HPAC--FQEELLRFCEAHKVQVQAYSPL-----------GSPAGVQSLLSNA----------------DVLRA-SKEEGV 217
Cdd:cd19091 188 SLLGrdLEHELMPLALDQGVGLLVWSPLaggllsgkyrrGQPAPEGSRLRRTgfdfppvdrergydvvDALREiAKETGA 267
|
250 260 270
....*....|....*....|....*....|....*...
gi 428171326 218 SAAQVLIRWAMQ--TCGSAVARSSNEQRLAENLETTQV 253
Cdd:cd19091 268 TPAQVALAWLLSrpTVSSVIIGARNEEQLEDNLGAAGL 305
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
8-229 |
4.12e-29 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 111.94 E-value: 4.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQ-----------LRGEEASRATQQAMELGYRAIDTASIY---RNEEdiAMGLAASGV-RREDVFITSKLA- 71
Cdd:cd19093 2 VSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSER--LLGRFLKELgDRDEVVIATKFAp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 72 -PNEQGYSKAMSALTSSLQRLNTSYLDLYLIHWPGAAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQ 150
Cdd:cd19093 80 lPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIE---------ALMDGLADAVEEGLVRAVGVSNYSADQLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 151 ELLAC---SELVPCVNQVE---LHPACFQEELLRFCEAHKVQVQAYSPLG-----------SPAG--------------V 199
Cdd:cd19093 151 RAHKAlkeRGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspeNPPPggrrrlfgrknlekV 230
|
250 260 270
....*....|....*....|....*....|.
gi 428171326 200 QSLLsnaDVLRA-SKEEGVSAAQVLIRWAMQ 229
Cdd:cd19093 231 QPLL---DALEEiAEKYGKTPAQVALNWLIA 258
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
10-253 |
6.22e-29 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 111.54 E-value: 6.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 10 PLFFGTFQLrGEEASRATQQAM-----ELGYRAIDTASIY----------RNEEDIAMGLAASGvRREDVFITSKLA--- 71
Cdd:cd19081 11 PLCLGTMVF-GWTADEETSFALldafvDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATKVGfpm 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 72 -PNEQGYSKA--MSALTSSLQRLNTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRH 148
Cdd:cd19081 89 gPNGPGLSRKhiRRAVEASLRRLQTDYIDLYQAHWDDPA-TPLE---------ETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 149 LQELLACSE---------LVPCVNQVelHPACFQEELLRFCEAHKVQVQAYSPLGS-------------------PAGVQ 200
Cdd:cd19081 159 LQEALELSRqhglpryvsLQPEYNLV--DRESFEGELLPLCREEGIGVIPYSPLAGgfltgkyrseadlpgstrrGEAAK 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 428171326 201 SLLS--NADVLRA----SKEEGVSAAQVLIRWAMQTCG--SAVARSSNEQRLAENLETTQV 253
Cdd:cd19081 237 RYLNerGLRILDAldevAAEHGATPAQVALAWLLARPGvtAPIAGARTVEQLEDLLAAAGL 297
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
21-246 |
1.26e-27 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 107.93 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 21 EEASRATQQAMELGYRAIDTASIYRN---EEDIAMGLAASGVRREDVFITSK---LAPNEQG--------YSKA--MSAL 84
Cdd:COG4989 31 AEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLSPSLREKIELQTKcgiRLPSEARdnrvkhydTSKEhiIASV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 85 TSSLQRLNTSYLDLYLIHWPgaakTPLESPAnkrlrlESWQALEDALKLGMIRRAGVSNFCVRHLqELLA---CSELVpc 161
Cdd:COG4989 111 EGSLRRLGTDYLDLLLLHRP----DPLMDPE------EVAEAFDELKASGKVRHFGVSNFTPSQF-ELLQsalDQPLV-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 162 VNQVE---LHPACFQEELLRFCEAHKVQVQAYSPLG-----SPAGVQSLLSNADVLRASKEEGVSAAQVLIRW------A 227
Cdd:COG4989 178 TNQIElslLHTDAFDDGTLDYCQLNGITPMAWSPLAggrlfGGFDEQFPRLRAALDELAEKYGVSPEAIALAWllrhpaG 257
|
250
....*....|....*....
gi 428171326 228 MQtcgsAVARSSNEQRLAE 246
Cdd:COG4989 258 IQ----PVIGTTNPERIKA 272
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
21-253 |
6.41e-26 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 103.02 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 21 EEASRATQQAMELGYRAIDTASIY-RNEEDIAMG--LAASGVRREDVFITSK--------LAPNEQGY---SKA--MSAL 84
Cdd:cd19092 24 EELLSLIEAALELGITTFDHADIYgGGKCEELFGeaLALNPGLREKIEIQTKcgirlgddPRPGRIKHydtSKEhiLASV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 85 TSSLQRLNTSYLDLYLIHWPgaakTPLESPAnkrlrlESWQALEDALKLGMIRRAGVSNFCVRHLqELL--ACS-ELVpc 161
Cdd:cd19092 104 EGSLKRLGTDYLDLLLLHRP----DPLMDPE------EVAEAFDELVKSGKVRYFGVSNFTPSQI-ELLqsYLDqPLV-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 162 VNQVELHPACFQ---EELLRFCEAHKVQVQAYSPLG-----SPAGVQSLLSNADVLRASKEEGVSAAQVLIRWAMQ--TC 231
Cdd:cd19092 171 TNQIELSLLHTEaidDGTLDYCQLLDITPMAWSPLGggrlfGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRhpAR 250
|
250 260
....*....|....*....|..
gi 428171326 232 GSAVARSSNEQRLAENLETTQV 253
Cdd:cd19092 251 IQPILGTTNPERIRSAVKALDI 272
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-228 |
2.23e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 101.98 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 22 EASRATQQAMELGYRAIDTASIY---RNEEdiAMGLAASGvRREDVFITSK--LAPNEQG-----YSKA--MSALTSSLQ 89
Cdd:cd19102 27 DSIAAIRAALDLGINWIDTAAVYglgHSEE--VVGRALKG-LRDRPIVATKcgLLWDEEGrirrsLKPAsiRAECEASLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 90 RLNTSYLDLYLIHWPgAAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQellACSELVPcVNQVE--- 166
Cdd:cd19102 104 RLGVDVIDLYQIHWP-DPDEPIE---------EAWGALAELKEEGKVRAIGVSNFSVDQMK---RCQAIHP-IASLQppy 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 --LHPAcFQEELLRFCEAHKVQVQAYSPLGS--------PAGVQSLLSN--------------------ADVLRA-SKEE 215
Cdd:cd19102 170 slLRRG-IEAEILPFCAEHGIGVIVYSPMQSglltgkmtPERVASLPADdwrrrspffqepnlarnlalVDALRPiAERH 248
|
250
....*....|...
gi 428171326 216 GVSAAQVLIRWAM 228
Cdd:cd19102 249 GRTVAQLAIAWVL 261
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
20-226 |
1.20e-24 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 100.35 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 20 GEEASRA-TQQAMELGYRAIDTASIYRN--EEDIaMGLAASG-VRREDVFITSKL------APNEQGYSKA--MSALTSS 87
Cdd:cd19079 33 DEEESRPiIKRALDLGINFFDTANVYSGgaSEEI-LGRALKEfAPRDEVVIATKVyfpmgdGPNGRGLSRKhiMAEVDAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSE---LVPCVNQ 164
Cdd:cd19079 112 LKRLGTDYIDLYQIHRWDYE-TPIE---------ETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEkngWTKFVSM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 165 VELHPACFQE---ELLRFCEAHKVQVQAYSPL------GSPAGVQSLLSNAD--------------------VLRASKEE 215
Cdd:cd19079 182 QNHYNLLYREeerEMIPLCEEEGIGVIPWSPLargrlaRPWGDTTERRRSTTdtaklkydyfteadkeivdrVEEVAKER 261
|
250
....*....|.
gi 428171326 216 GVSAAQVLIRW 226
Cdd:cd19079 262 GVSMAQVALAW 272
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
10-194 |
1.24e-23 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 97.64 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 10 PLFFGT--FqlrGEEASRATQQAM-----ELGYRAIDTASIY---RNEEDIAMGLAAsgvRREDVFITSKL------APN 73
Cdd:cd19087 15 RLCLGTmnF---GGRTDEETSFAImdralDAGINFFDTADVYgggRSEEIIGRWIAG---RRDDIVLATKVfgpmgdDPN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 74 EQGYS--KAMSALTSSLQRLNTSYLDLYLIHWPGAaKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQE 151
Cdd:cd19087 89 DRGLSrrHIRRAVEASLRRLQTDYIDLYQMHHFDR-DTPLE---------ETLRALDDLVRQGKIRYIGVSNFAAWQIAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 428171326 152 LLACSE------LV---PCVN----QVELhpacfqeELLRFCEAHKVQVQAYSPLG 194
Cdd:cd19087 159 AQGIAArrgllrFVseqPMYNllkrQAEL-------EILPAARAYGLGVIPYSPLA 207
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
9-193 |
1.36e-23 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 97.34 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGTFQLRG---------EEASRATQQAMELGYRAIDTASIYR--NEEDIaMGLAASGvRREDVFITSKLAPN---- 73
Cdd:cd19149 12 SVIGLGTWAIGGgpwwggsddNESIRTIHAALDLGINLIDTAPAYGfgHSEEI-VGKAIKG-RRDKVVLATKCGLRwdre 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 74 EQGYSKAMSALT---------------SSLQRLNTSYLDLYLIHWPgAAKTPLEspankrlrlESWQALEDALKLGMIRR 138
Cdd:cd19149 90 GGSFFFVRDGVTvyknlspesireeveQSLKRLGTDYIDLYQTHWQ-DVETPIE---------ETMEALEELKRQGKIRA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 428171326 139 AGVSNFCVRHLQELLACSELvpCVNQVE---LHPAcFQEELLRFCEAHKVQVQAYSPL 193
Cdd:cd19149 160 IGASNVSVEQIKEYVKAGQL--DIIQEKysmLDRG-IEKELLPYCKKNNIAFQAYSPL 214
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
13-195 |
2.09e-21 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 89.84 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 13 FGTFQLRG--------EEASRATQQAMELGYRAIDTASIY---RNEEDIAMGLAAsgvRREDVFITSKLAPN-------E 74
Cdd:cd19086 8 FGTWGLGGdwwgdvddAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKG---RRDKVVIATKFGNRfdggperP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 75 QGYSKA--MSALTSSLQRLNTSYLDLYLIHWPgaaktPLESPANKrlrlESWQALEDALKLGMIRRAGVSnfcVRHLQEL 152
Cdd:cd19086 85 QDFSPEyiREAVEASLKRLGTDYIDLYQLHNP-----PDEVLDND----ELFEALEKLKQEGKIRAYGVS---VGDPEEA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 428171326 153 LACSE--LVPCV----NQVELHPAcfqEELLRFCEAHKVQVQAYSPLGS 195
Cdd:cd19086 153 LAALRrgGIDVVqviyNLLDQRPE---EELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
21-193 |
2.22e-21 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 91.21 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 21 EEASRAT-QQAMELGYRAIDTASIY---RNEEDIAMGLAASGVRrEDVFITSKLA---PNEQGY----SKA--MSALTSS 87
Cdd:cd19148 24 EKEAIETiHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYGKR-DRVVIATKVGlewDEGGEVvrnsSPAriRKEVEDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVEL 167
Cdd:cd19148 103 LRRLQTDYIDLYQVHWPD-PLVPIE---------ETAEALKELLDEGKIRAIGVSNFSPEQMETFRKVAPLHTVQPPYNL 172
|
170 180
....*....|....*....|....*.
gi 428171326 168 HPACFQEELLRFCEAHKVQVQAYSPL 193
Cdd:cd19148 173 FEREIEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-249 |
1.72e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 87.54 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 13 FGTFQLRG---EEASRATQQAMELGYRAIDTASIYRNEEdIAMGLAASGvRREDVFITSKLapNEQGYSKAMSALTSSLQ 89
Cdd:cd19100 16 FGGGPLGRlsqEEAAAIIRRALDLGINYFDTAPSYGDSE-EKIGKALKG-RRDKVFLATKT--GARDYEGAKRDLERSLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 90 RLNTSYLDLYLIHwpgAAKTPLESPANKRLRlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSE----LVPcVNQV 165
Cdd:cd19100 92 RLGTDYIDLYQLH---AVDTEEDLDQVFGPG-GALEALLEAKEEGKIRFIGISGHSPEVLLRALETGEfdvvLFP-INPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 166 ELHPACFQEELLRFCEAHKVQVQAYSPLGspAGvqsllsnadvlRASKEEGVSAAQvLIRWAMQTCG--SAVARSSNEQR 243
Cdd:cd19100 167 GDHIDSFREELLPLAREKGVGVIAMKVLA--GG-----------RLLSGDPLDPEQ-ALRYALSLPPvdVVIVGMDSPEE 232
|
....*.
gi 428171326 244 LAENLE 249
Cdd:cd19100 233 LDENLA 238
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
8-248 |
1.87e-20 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 87.66 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRG---------EEASRAT-QQAMELGYRAIDTASIY---RNEEDIAMGLAAsgvRREDVFITSK--LAP 72
Cdd:cd19088 1 VSRLGYGAMRLTGpgiwgppadREEAIAVlRRALELGVNFIDTADSYgpdVNERLIAEALHP---YPDDVVIATKggLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 73 NEQGY-----SKA--MSALTSSLQRLNTSYLDLYLIHWPGAaKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFC 145
Cdd:cd19088 78 TGPGWwgpdgSPEylRQAVEASLRRLGLDRIDLYQLHRIDP-KVPFE---------EQLGALAELQDEGLIRHIGLSNVT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 146 VRHLQELLACSELVpCVnQVELHPACFQ-EELLRFCEAHKVQVQAYSPLGSPAGVQSLLSNADVlraSKEEGVSAAQVLI 224
Cdd:cd19088 148 VAQIEEARAIVRIV-SV-QNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGGGDLAQPGGLLAEV---AARLGATPAQVAL 222
|
250 260
....*....|....*....|....*.
gi 428171326 225 RWAMQT--CGSAVARSSNEQRLAENL 248
Cdd:cd19088 223 AWLLARspVMLPIPGTSSVEHLEENL 248
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
18-195 |
4.00e-20 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 87.86 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 18 LRGEEASRATQQAMELGYRAIDTASIY---RNEEDIamGLAASGVRREDVFITSKLAPNEQGYSKAM--------SALTS 86
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELV--GEVLKEYNRNEVVIATKGAHKFGGDGSVLnnspeflrSAVEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSelvpcvnQVE 166
Cdd:cd19083 108 SLKRLNTDYIDLYYIHFPD-GETPKA---------EAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDG-------YVD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 428171326 167 LHPACF-------QEELLRFCEAHKVQVQAYSPLGS 195
Cdd:cd19083 171 VLQGEYnllqreaEEDILPYCVENNISFIPYFPLAS 206
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
9-249 |
6.04e-20 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 86.84 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGTFQL------RGEEASRAT-QQAMELGYRAIDTASIYRNEEDIaMGLAASGVRREDVFITSKLAPNEQG---YS 78
Cdd:cd19090 1 SALGLGTAGLggvfggVDDDEAVATiRAALDLGINYIDTAPAYGDSEER-LGLALAELPREPLVLSTKVGRLPEDtadYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 79 KA--MSALTSSLQRLNTSYLDLYLIH---WPGAAKTPLESPAnkrlrLEswqALEDALKLGMIRRAGVSnfcVRHLQELL 153
Cdd:cd19090 80 ADrvRRSVEESLERLGRDRIDLLMIHdpeRVPWVDILAPGGA-----LE---ALLELKEEGLIKHIGLG---GGPPDLLR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 154 ACSE-----LVPCVNQVELhpaCFQE---ELLRFCEAHKVQVQAYSPLGspagvQSLLSNAD------------------ 207
Cdd:cd19090 149 RAIEtgdfdVVLTANRYTL---LDQSaadELLPAAARHGVGVINASPLG-----MGLLAGRPpervrytyrwlspelldr 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 428171326 208 ---VLRASKEEGVSAAQVLIRWAMQ--TCGSAVARSSNEQRLAENLE 249
Cdd:cd19090 221 akrLYELCDEHGVPLPALALRFLLRdpRISTVLVGASSPEELEQNVA 267
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
9-250 |
6.92e-20 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 86.13 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGTFQLRG-------EEASRATQQAMELGYRAIDTASIY-RNEEDIamGLAASGVRREDVFITSKLAPNEQGY--S 78
Cdd:cd19095 1 SVLGLGTSGIGRvwgvpseAEAARLLNTALDLGINLIDTAPAYgRSEERL--GRALAGLRRDDLFIATKVGTHGEGGrdR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 79 KAMSA------LTSSLQRLNTSYLDLYLIHwpgaaktpleSPANKRLRLESWQALEDALKLGMIRRAGVSNFcVRHLQEL 152
Cdd:cd19095 79 KDFSPaairasIERSLRRLGTDYIDLLQLH----------GPSDDELTGEVLETLEDLKAAGKVRYIGVSGD-GEELEAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 153 LAcSELVPCVnQVELHPA-CFQEELLRFCEAHKVQVQAYSPLGS---PAGVQSLLSNADVLRASKE----EGVSAAQVLI 224
Cdd:cd19095 148 IA-SGVFDVV-QLPYNVLdREEEELLPLAAEAGLGVIVNRPLANgrlRRRVRRRPLYADYARRPEFaaeiGGATWAQAAL 225
|
250 260
....*....|....*....|....*...
gi 428171326 225 RWAMQT--CGSAVARSSNEQRLAENLET 250
Cdd:cd19095 226 RFVLSHpgVSSAIVGTTNPEHLEENLAA 253
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
8-250 |
1.98e-19 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 86.80 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGT--FQLRGEEASRAT-QQAMELGYRAIDTASIYRNEEdIAMGLAASGvRREDVFITSKLAPNEQGYSKAMSAL 84
Cdd:COG1453 13 VSVLGFGGmrLPRKDEEEAEALiRRAIDNGINYIDTARGYGDSE-EFLGKALKG-PRDKVILATKLPPWVRDPEDMRKDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 85 TSSLQRLNTSYLDLYLIHWPGAAKTpLESPANKrlrLESWQALEDALKLGMIRRAGVSNfcvrH-----LQELLAcSELV 159
Cdd:COG1453 91 EESLKRLQTDYIDLYLIHGLNTEED-LEKVLKP---GGALEALEKAKAEGKIRHIGFST----HgslevIKEAID-TGDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 160 PCVN-QV----ELHPAcfQEELLRFCEAHKVQVQAYSPLgspAGvQSLLSNADVLRASKEEGVSAAQVLIRWAMQTCGSA 234
Cdd:COG1453 162 DFVQlQYnyldQDNQA--GEEALEAAAEKGIGVIIMKPL---KG-GRLANPPEKLVELLCPPLSPAEWALRFLLSHPEVT 235
|
250
....*....|....*...
gi 428171326 235 VARS--SNEQRLAENLET 250
Cdd:COG1453 236 TVLSgmSTPEQLDENLKT 253
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
13-248 |
3.94e-19 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 84.95 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 13 FGTfQLRGEEASRATQQAMELGYRAIDTASIY-RNEEDIAMGLAASGVRREDVFITSKL------APNEQGYSKA--MSA 83
Cdd:cd19074 15 FGG-QVDDEDAKACVRKAYDLGINFFDTADVYaAGQAEEVLGKALKGWPRESYVISTKVfwptgpGPNDRGLSRKhiFES 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 84 LTSSLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLA-CSELV--- 159
Cdd:cd19074 94 IHASLKRLQLDYVDIYYCHRYD-PETPLE---------ETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDlARQFGlip 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 160 PCVNQVELHPACFQ--EELLRFCEAHKVQVQAYSPL-----------GSPAGVQS------------------LLSNADV 208
Cdd:cd19074 164 PVVEQPQYNMLWREieEEVIPLCEKNGIGLVVWSPLaqglltgkyrdGIPPPSRSratdednrdkkrrlltdeNLEKVKK 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 428171326 209 LRA-SKEEGVSAAQVLIRWAMQTCG--SAVARSSNEQRLAENL 248
Cdd:cd19074 244 LKPiADELGLTLAQLALAWCLRNPAvsSAIIGASRPEQLEENV 286
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
7-250 |
2.95e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 82.64 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQL--------RGEEASRATQQAMELGYRAIDTASIYRNEEDI----AMGLAASGVRREDVFITSKLAP-- 72
Cdd:cd19101 1 TISRVINGMWQLsgghggirDEDAAVRAMAAYVDAGLTTFDCADIYGPAEELigefRKRLRRERDAADDVQIHTKWVPdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 73 NEQGYSKAM--SALTSSLQRLNTSYLDLYLIHWpgaaktplESPANKRLrLESWQALEDALKLGMIRRAGVSNFCVRHLQ 150
Cdd:cd19101 81 GELTMTRAYveAAIDRSLKRLGVDRLDLVQFHW--------WDYSDPGY-LDAAKHLAELQEEGKIRHLGLTNFDTERLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 151 ELlaCSELVPCV-NQVEL-----HPacfQEELLRFCEAHKVQVQAYSPL------------------------------- 193
Cdd:cd19101 152 EI--LDAGVPIVsNQVQYslldrRP---ENGMAALCEDHGIKLLAYGTLaggllsekylgvpeptgpaletrslqkyklm 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 428171326 194 ----GSPAGVQSLLSnadVLRA-SKEEGVSAAQVLIRWAM-QTCGSAV---ARssNEQRLAENLET 250
Cdd:cd19101 227 idewGGWDLFQELLR---TLKAiADKHGVSIANVAVRWVLdQPGVAGVivgAR--NSEHIDDNVRA 287
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-249 |
1.32e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 80.82 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 13 FGTFQL-----RGEEASRATQQAMELGYRAIDTASIYRN---EEDIAMGL----AASGVRREDVFITSK----------- 69
Cdd:cd19099 8 LGTYRGdsddeTDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALreliEKGGIKRDEVVIVTKagyipgdgdep 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 70 LAPNEQGYSKAMS----------------------ALTSSLQRLNTSYLDLYLIHWPGAAKTPL-ESPANKRLRlESWQA 126
Cdd:cd19099 88 LRPLKYLEEKLGRglidvadsaglrhcispayledQIERSLKRLGLDTIDLYLLHNPEEQLLELgEEEFYDRLE-EAFEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 127 LEDALKLGMIRRAGVS-NFCVR---------HLQELLACSELVPCVN------QVEL---HPACFQEE---------LLR 178
Cdd:cd19099 167 LEEAVAEGKIRYYGIStWDGFRappalpghlSLEKLVAAAEEVGGDNhhfkviQLPLnllEPEALTEKntvkgealsLLE 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428171326 179 FCEAHKVQVQAYSPLGspaGVQSLLSNADVLRASKEEGVSAAQVLIRWAMQT--CGSAVARSSNEQRLAENLE 249
Cdd:cd19099 247 AAKELGLGVIASRPLN---QGQLLGELRLADLLALPGGATLAQRALQFARSTpgVDSALVGMRRPEHVDENLA 316
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-229 |
1.56e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 79.55 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASrATQQAMELGYRAIDTASIY---RNEEdiAMGLAASGVRREDVFITSKLAPNEQGYSKA--MS 82
Cdd:cd19105 13 VSRLGFGGGGLPRESPE-LLRRALDLGINYFDTAEGYgngNSEE--IIGEALKGLRRDKVFLATKASPRLDKKDKAelLK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 83 ALTSSLQRLNTSYLDLYLIHWPGAAKTPLESPankrlrlESWQALEDALKLGMIRRAGVSnfCVRHLQELLAcsELVPC- 161
Cdd:cd19105 90 SVEESLKRLQTDYIDIYQLHGVDTPEERLLNE-------ELLEALEKLKKEGKVRFIGFS--THDNMAEVLQ--AAIESg 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 428171326 162 ---VNQVE---LHPACFQEELLRFCEAHKVQVQAYSPLGspagvqSLLSNADVLRASKEEGVSAAQVLIRWAMQ 229
Cdd:cd19105 159 wfdVIMVAynfLNQPAELEEALAAAAEKGIGVVAMKTLA------GGYLQPALLSVLKAKGFSLPQAALKWVLS 226
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
30-194 |
4.63e-17 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 79.53 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 30 AMELGYRAIDTASIY----------RNEEDIAMGLAASGvRREDVFITSKLAPNEQGYSKA------------MSALTSS 87
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVAGPGEGITWPrgggtrldreniREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 88 LQRLNTSYLDLYLIHWPgAAKTPL----ESPANKRLR-----LESWQALEDALKLGMIRRAGVSN--------FCvrHLQ 150
Cdd:cd19094 106 LKRLGTDYIDLYQLHWP-DRYTPLfgggYYTEPSEEEdsvsfEEQLEALGELVKAGKIRHIGLSNetpwgvmkFL--ELA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 428171326 151 ELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLG 194
Cdd:cd19094 183 EQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLA 226
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
9-249 |
1.52e-16 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 77.60 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGT--FQLRGEEASRATQQAM-----ELGYRAIDTASIY---RNEEDI-AMGLAASGVRredvfITSKLAPNEQGY 77
Cdd:cd19075 1 PKIILGTmtFGSQGRFTTAEAAAELldaflERGHTEIDTARVYpdgTSEELLgELGLGERGFK-----IDTKANPGVGGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 78 SKA---MSALTSSLQRLNTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLA 154
Cdd:cd19075 76 LSPenvRKQLETSLKRLKVDKVDVFYLHAPDRS-TPLE---------ETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 155 -CSE---LVPCVNQ---------VElhpacfqEELLRFCEAHKVQVQAYSPLG--------------------SPAGVQ- 200
Cdd:cd19075 146 iCKEngwVLPTVYQgmynaitrqVE-------TELFPCLRKLGIRFYAYSPLAggfltgkykysedkagggrfDPNNALg 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 428171326 201 ----------SLLSNADVLR-ASKEEGVSAAQVLIRWAMQ------TCGSAV---ArsSNEQRLAENLE 249
Cdd:cd19075 219 klyrdrywkpSYFEALEKVEeAAEKEGISLAEAALRWLYHhsaldgEKGDGVilgA--SSLEQLEENLA 285
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
10-249 |
1.51e-15 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 74.95 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 10 PLFFGTFQL---RGEEASRATQQAM-----ELGYRAIDTASIYRNE--EDIAMGLAASgvRREDVFITSKL-------AP 72
Cdd:cd19080 12 PLALGTMTFgteWGWGADREEARAMfdayvEAGGNFIDTANNYTNGtsERLLGEFIAG--NRDRIVLATKYtmnrrpgDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 73 NEQGYSKA--MSALTSSLQRLNTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNF---CVR 147
Cdd:cd19080 90 NAGGNHRKnlRRSVEASLRRLQTDYIDLLYVHAWDFT-TPVE---------EVMRALDDLVRAGKVLYVGISDTpawVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 148 HLQELLACSELVPCVN-QVELHPA--CFQEELLRFCEAHKVQVQAYSPLGS------------PAGVQSLLSN------- 205
Cdd:cd19080 160 RANTLAELRGWSPFVAlQIEYSLLerTPERELLPMARALGLGVTPWSPLGGglltgkyqrgeeGRAGEAKGVTvgfgklt 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 428171326 206 ------ADVLRA-SKEEGVSAAQVLIRWAMQTCGSAV----ARSSnEQrLAENLE 249
Cdd:cd19080 240 ernwaiVDVVAAvAEELGRSAAQVALAWVRQKPGVVIpiigARTL-EQ-LKDNLG 292
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
12-229 |
2.22e-15 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 74.56 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 12 FFGTfqlRGEEASRAT-QQAMELGYRAIDTASIY---RNEEDIAMGLAAsgvRREDVFITSKLAPNEQGYSKAM------ 81
Cdd:cd19076 25 FYGP---ADEEESIATlHRALELGVTFLDTADMYgpgTNEELLGKALKD---RRDEVVIATKFGIVRDPGSGFRgvdgrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 82 ----SALTSSLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLAC-- 155
Cdd:cd19076 99 eyvrAACEASLKRLGTDVIDLYYQHRVD-PNVPIE---------ETVGAMAELVEEGKVRYIGLSEASADTIRRAHAVhp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 156 -----SELVPCVNQVElhpacfqEELLRFCEAHKVQVQAYSPLG---------SPagvqSLLSNADVLRAS--------- 212
Cdd:cd19076 169 itavqSEYSLWTRDIE-------DEVLPTCRELGIGFVAYSPLGrgfltgaikSP----EDLPEDDFRRNNprfqgenfd 237
|
250 260 270
....*....|....*....|....*....|
gi 428171326 213 -------------KEEGVSAAQVLIRWAMQ 229
Cdd:cd19076 238 knlklvekleaiaAEKGCTPAQLALAWVLA 267
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
30-250 |
6.14e-15 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 72.59 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 30 AMELGYRAIDTASIYRNEE-DIAMGLAASGVRREDVFITSKLAPNE-QGYSKAMSALTSSLQRLNTSYLDLYLIHWPGAA 107
Cdd:cd19096 30 AIDAGINYFDTAYGYGGGKsEEILGEALKEGPREKFYLATKLPPWSvKSAEDFRRILEESLKRLGVDYIDFYLLHGLNSP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 108 KTPlespaNKRLRLESWQALEDALKLGMIRRAGVSnFcvrH-----LQELLACSELVPCvnQVELH----PACFQEELLR 178
Cdd:cd19096 110 EWL-----EKARKGGLLEFLEKAKKEGLIRHIGFS-F---HdspelLKEILDSYDFDFV--QLQYNyldqENQAGRPGIE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 428171326 179 FCEAHKVQVQAYSPLGspAGVqsLLSNA-DVLRASKEEGVSAAQVLIRWAMQTCGSAVARS--SNEQRLAENLET 250
Cdd:cd19096 179 YAAKKGMGVIIMEPLK--GGG--LANNPpEALAILCGAPLSPAEWALRFLLSHPEVTTVLSgmSTPEQLDENIAA 249
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
13-256 |
3.30e-14 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 71.47 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 13 FGTfQLRGEEASRATQQAMELGYRAIDTASIYRN-EEDIAMG--LAASGVRREDVFITSKL-------APNEQGYSKA-- 80
Cdd:cd19143 24 FGN-QVDVDEAKECMKAAYDAGVNFFDNAEVYANgQSEEIMGqaIKELGWPRSDYVVSTKIfwggggpPPNDRGLSRKhi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 81 MSALTSSLQRLNTSYLDLYLIHWPGAAkTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSE--- 157
Cdd:cd19143 103 VEGTKASLKRLQLDYVDLVFCHRPDPA-TPIE---------ETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADrlg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 158 LV-PCVNQVE---LHPACFQEELLRFCEAHKVQVQAYSPLGS-----------PAGVQSLLSNADVLRASKEE------- 215
Cdd:cd19143 173 LIpPVMEQPQynlFHRERVEVEYAPLYEKYGLGTTTWSPLASglltgkynngiPEGSRLALPGYEWLKDRKEElgqekie 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 428171326 216 ------------GVSAAQVLIRWAMQT--CGSAVARSSNEQRLAENLETTQVFEH 256
Cdd:cd19143 253 kvrklkpiaeelGCSLAQLAIAWCLKNpnVSTVITGATKVEQLEENLKALEVLPK 307
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-229 |
3.67e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 70.63 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 21 EEASRATQQAMELGYRAIDTASIYRNEEDIamgLAASGVRREDVFITSKLAPNEQGYSKA----MSALTSSLQRLNTSYL 96
Cdd:cd19097 26 KEAKKILEYALKAGINTLDTAPAYGDSEKV---LGKFLKRLDKFKIITKLPPLKEDKKEDeaaiEASVEASLKRLKVDSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 97 DLYLIHwpgaaktpleSPANKRLRLES-WQALEDALKLGMIRRAGVSnfcVRHLQELLACSELVPC-VNQVELHP---AC 171
Cdd:cd19097 103 DGLLLH----------NPDDLLKHGGKlVEALLELKKEGLIRKIGVS---VYSPEELEKALESFKIdIIQLPFNIldqRF 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 428171326 172 FQEELLRFCEAHKVQVQAYSP------LGSPAGVQSLLSNADVLRA-----SKEEGVSAAQVLIRWAMQ 229
Cdd:cd19097 170 LKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLPAKFAPAKPLLKklhelAKKLGLSPLELALGFVLS 238
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
9-249 |
1.10e-13 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 69.50 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGT----FQLRGEEASRATQQAMELGYRAIDTASIY-------RNEEDIAMGLAASGVRrEDVFITSKLA-PNEQG 76
Cdd:cd19082 1 SRIVLGTadfgTRIDEEEAFALLDAFVELGGNFIDTARVYgdwvergASERVIGEWLKSRGNR-DKVVIATKGGhPDLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 77 YSKA-MSA------LTSSLQRLNTSYLDLYLIHW--PgaaKTPLEspankrlrlESWQALEDALKLGMIRRAGVSN---- 143
Cdd:cd19082 80 MSRSrLSPediradLEESLERLGTDYIDLYFLHRddP---SVPVG---------EIVDTLNELVRAGKIRAFGASNwste 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 144 -------FCVRHLQELLACSE----LVPCVNQVELHP--ACFQEELLRFCEAHKVQVQAYSPLGS--------------P 196
Cdd:cd19082 148 riaeanaYAKAHGLPGFAASSpqwsLARPNEPPWPGPtlVAMDEEMRAWHEENQLPVFAYSSQARgffskraaggaeddS 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428171326 197 AGVQSLLSNADVLRA------SKEEGVSAAQVLIRW----AMQTCgsAVARSSNEQRLAENLE 249
Cdd:cd19082 228 ELRRVYYSEENFERLerakelAEEKGVSPTQIALAYvlnqPFPTV--PIIGPRTPEQLRDSLA 288
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-227 |
3.22e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 68.13 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 12 FFGTFQLRGEEASRAT-----QQAMELGYRAIDTASIY---RNEEdiAMGLAASGVRREDVFITSKLAPNEQG-YSKAMS 82
Cdd:cd19103 18 GAGGDQVFGNHLDEDTlkavfDKAMAAGLNLWDTAAVYgmgASEK--ILGEFLKRYPREDYIISTKFTPQIAGqSADPVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 83 A-LTSSLQRLNTSYLDLYLIHWPgaaktplespankrLRLESW-QALEDALKLGMIRRAGVSNF----CVRhLQELLACS 156
Cdd:cd19103 96 DmLEGSLARLGTDYIDIYWIHNP--------------ADVERWtPELIPLLKSGKVKHVGVSNHnlaeIKR-ANEILAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 157 ELVpcVNQVE-----LHPACFQEELLRFCEAHKVQVQAYSPL--GS-----------PAGVQSLLSNADVLRASKE---- 214
Cdd:cd19103 161 GVS--LSAVQnhyslLYRSSEEAGILDYCKENGITFFAYMVLeqGAlsgkydtkhplPEGSGRAETYNPLLPQLEEltav 238
|
250 260
....*....|....*....|
gi 428171326 215 -------EGVSAAQVLIRWA 227
Cdd:cd19103 239 maeigakHGASIAQVAIAWA 258
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
7-250 |
8.58e-13 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 66.92 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFG--TF------QLRGEEASRATQQAMELGYRAIDTASIYRNEEDIaMGLAASGVR----REDVFITSK---LA 71
Cdd:cd19164 12 GLPPLIFGaaTFsyqyttDPESIPPVDIVRRALELGIRAFDTSPYYGPSEII-LGRALKALRdefpRDTYFIITKvgrYG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 72 PNEQGYSKA---MSaLTSSLQRLNTSYLDLYLIHwpgaaktPLESPAnkrlRLESWQALEDALKL---GMIRRAGVSNFC 145
Cdd:cd19164 91 PDDFDYSPEwirAS-VERSLRRLHTDYLDLVYLH-------DVEFVA----DEEVLEALKELFKLkdeGKIRNVGISGYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 146 VRHLQEL--LACSELVPCVNQV------ELHPACFQEELLRFCEAHKV-QVQAYSPLG------------SPAGVQSLLS 204
Cdd:cd19164 159 LPVLLRLaeLARTTAGRPLDAVlsychyTLQNTTLLAYIPKFLAAAGVkVVLNASPLSmgllrsqgppewHPASPELRAA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 428171326 205 NADVLRASKEEGVSAAQVLIRWAMQTC---GSAVARSSNEQRLAENLET 250
Cdd:cd19164 239 AAKAAEYCQAKGTDLADVALRYALREWggeGPTVVGCSNVDELEEAVEA 287
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
21-253 |
1.04e-12 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 66.87 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 21 EEASRATQQAMELGYRAIDTASIY---RNEEDIAMGLAAsgvRREDVFITSKLAPNEQGYSKAMSALTS----------- 86
Cdd:cd19078 25 EEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKFGFKIDGGKPGPLGLDSrpehirkaveg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGaAKTPLESPAnkrlrleswQALEDALKLGMIRRAGVSNFCVRHLQELLACSELVPCVNQVE 166
Cdd:cd19078 102 SLKRLQTDYIDLYYQHRVD-PNVPIEEVA---------GTMKELIKEGKIRHWGLSEAGVETIRRAHAVCPVTAVQSEYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 167 LHPACFQEELLRFCEAHKVQVQAYSPLG--------------------------SPAGVQSLLSNADVLRA-SKEEGVSA 219
Cdd:cd19078 172 MMWREPEKEVLPTLEELGIGFVPFSPLGkgfltgkidentkfdegddraslprfTPEALEANQALVDLLKEfAEEKGATP 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 428171326 220 AQVLIRW--AMQTCGSAVARSSNEQRLAENLETTQV 253
Cdd:cd19078 252 AQIALAWllAKKPWIVPIPGTTKLSRLEENIGAADI 287
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
7-249 |
1.56e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 66.20 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTfqLRGEEASRAT-QQAMELGYRAIDTASIY----------RNEEDIAMGLAASGVRrEDVFITSKLA---- 71
Cdd:cd19752 4 CLGTMYFGT--RTDEETSFAIlDRYVAAGGNFLDTANNYafwteggvggESERLIGRWLKDRGNR-DDVVIATKVGagpr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 72 ------PNEQGYSKA--MSALTSSLQRLNTSYLDLYLIHWPGAAkTPLESpankrlRLESWQALEDAlklGMIRRAGVSN 143
Cdd:cd19752 81 dpdggpESPEGLSAEtiEQEIDKSLRRLGTDYIDLYYAHVDDRD-TPLEE------TLEAFNELVKA---GKVRAIGASN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 144 FCVRHLQEL--LACSELVP---CVNQ--VELHP---ACF------QEELLRFCEAHK-VQVQAYSPL--------GSPAG 198
Cdd:cd19752 151 FAAWRLERArqIARQQGWAefsAIQQrhSYLRPrpgADFgvqrivTDELLDYASSRPdLTLLAYSPLlsgaytrpDRPLP 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 428171326 199 VQSLLSNADVLRASKEE-----GVSAAQVLIRWAMQTCG---SAVARSSNEQrLAENLE 249
Cdd:cd19752 231 EQYDGPDSDARLAVLEEvagelGATPNQVVLAWLLHRTPaiiPLLGASTVEQ-LEENLA 288
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
7-194 |
1.64e-12 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 66.31 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 7 SLPPLFFGTFQLRG--------EEASRATQQAMELGYRAIDTASIYR-NEEDIAMGLAASGVRREDVFITSKLAPNEQGY 77
Cdd:cd19144 12 SVPALGFGAMGLSAfygppkpdEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKFGIEKNVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 78 SKAMS----------ALTSSLQRLNTSYLDLYLIHWPgAAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVR 147
Cdd:cd19144 92 TGEYSvdgspeyvkkACETSLKRLGVDYIDLYYQHRV-DGKTPIE---------KTVAAMAELVQEGKIKHIGLSECSAE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 428171326 148 HLQEllACS-ELVPCVnQVELHPACF-----QEELLRFCEAHKVQVQAYSPLG 194
Cdd:cd19144 162 TLRR--AHAvHPIAAV-QIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLG 211
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
21-250 |
4.40e-12 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 64.88 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 21 EEASRATQQAMELGYRAIDTASIY---RNEEdiAMGLAASGVRREDVFITSKLAPNEQG--------YSKAMSALTSSLQ 89
Cdd:cd19163 33 EEAIRTVHEALDSGINYIDTAPWYgqgRSET--VLGKALKGIPRDSYYLATKVGRYGLDpdkmfdfsAERITKSVEESLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 90 RLNTSYLDLYLIHWPGAAKTpLESPANkrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSE------LVPC-- 161
Cdd:cd19163 111 RLGLDYIDIIQVHDIEFAPS-LDQILN-----ETLPALQKLKEEGKVRFIGITGYPLDVLKEVLERSPvkidtvLSYChy 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 162 -VNQVELhpacfqEELLRFCEAHKVQVQAYSPLGSpagvqSLLSNA----------DVLRAS-------KEEGVSAAQVL 223
Cdd:cd19163 185 tLNDTSL------LELLPFFKEKGVGVINASPLSM-----GLLTERgppdwhpaspEIKEACakaaaycKSRGVDISKLA 253
|
250 260
....*....|....*....|....*....
gi 428171326 224 IRWAMQT--CGSAVARSSNEQRLAENLET 250
Cdd:cd19163 254 LQFALSNpdIATTLVGTASPENLRKNLEA 282
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-227 |
1.86e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 63.44 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 21 EEASRATQQAMELGYRAIDTASIY-RNEEDIAMGLAASGVRrEDVFITSK----LAPNEQGYSKAMSALTSSLQRLNTSY 95
Cdd:cd19104 32 EEQIAAVRRALDLGINFFDTAPSYgDGKSEENLGRALKGLP-AGPYITTKvrldPDDLGDIGGQIERSVEKSLKRLKRDS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 96 LDLYLIH---WPGAAKTPLES-PANKRLRLES-WQALEDALKLGMIRRAGVSnfCVRH---LQELLAcSELVPCVNQV-- 165
Cdd:cd19104 111 VDLLQLHnriGDERDKPVGGTlSTTDVLGLGGvADAFERLRSEGKIRFIGIT--GLGNppaIRELLD-SGKFDAVQVYyn 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 166 -------ELHPACF--QE--ELLRFCEAHKVQVQAYSPL-------------GSPAGVQSLLSnADVLRASK------EE 215
Cdd:cd19104 188 llnpsaaEARPRGWsaQDygGIIDAAAEHGVGVMGIRVLaagalttsldrgrEAPPTSDSDVA-IDFRRAAAfralarEW 266
|
250
....*....|..
gi 428171326 216 GVSAAQVLIRWA 227
Cdd:cd19104 267 GETLAQLAHRFA 278
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
15-194 |
3.16e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 62.95 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 15 TFQLRGEEASRATQ--QAMELGYRAIDTASIYR----------NEEDIAMGLAASGvRREDVFITSKLAPNEQGYSKAM- 81
Cdd:PRK10625 22 TFGEQNSEADAHAQldYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVSGPSRNNDKGIr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 82 -----------SALTSSLQRLNTSYLDLYLIHWP-------GAAKTPLESPANKRLRLESWQALEDALKLGMIRRAGVSN 143
Cdd:PRK10625 101 pnqaldrknirEALHDSLKRLQTDYLDLYQVHWPqrptncfGKLGYSWTDSAPAVSLLETLDALAEQQRAGKIRYIGVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 428171326 144 ---FCVR---HLQELLACSELVPCVNQVELHPACFQEELLRFCEAHKVQVQAYSPLG 194
Cdd:PRK10625 181 etaFGVMrylHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLA 237
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
8-250 |
2.10e-10 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 59.96 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 8 LPPLFFGTFQLRGEEASRATQQAM-----ELGYRAIDTASIYRNEE---DIAMGLAAS---GVRREDVFITSKLA----- 71
Cdd:cd19089 11 LPAISLGLWHNFGDYTSPEEARELlrtafDLGITHFDLANNYGPPPgsaEENFGRILKrdlRPYRDELVISTKAGygmwp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 72 -PNEQGYSKA--MSALTSSLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRH 148
Cdd:cd19089 91 gPYGDGGSRKylLASLDQSLKRMGLDYVDIFYHHRYD-PDTPLE---------ETMTALADAVRSGKALYVGISNYPGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 149 LQELLA-CSEL-VPCV-NQVE---LHPACFqEELLRFCEAHKVQVQAYSPL-----------GSPAG------------V 199
Cdd:cd19089 161 ARRAIAlLRELgVPLIiHQPRyslLDRWAE-DGLLEVLEEAGIGFIAFSPLaqglltdkylnGIPPDsrraaeskflteE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 428171326 200 QSLLSNADVLRA----SKEEGVSAAQVLIRWAMQ---TCGSAVARSSNEQrLAENLET 250
Cdd:cd19089 240 ALTPEKLEQLRKlnkiAAKRGQSLAQLALSWVLRdprVTSVLIGASSPSQ-LEDNVAA 296
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
17-254 |
2.04e-09 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 57.36 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 17 QLRGEEASRATQQAMELGYRAIDTASIYR-NEEDIAMG--LAASGVRREDVFITSKL-----APNEQGYSKA--MSALTS 86
Cdd:cd19159 27 QISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVILGsiIKKKGWRRSSLVITTKLywggkAETERGLSRKhiIEGLKG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSE----LVPCV 162
Cdd:cd19159 107 SLQRLQLEYVDVVFANRPD-SNTPME---------EIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 163 NQVELHpaCFQEELL--RFCEA-HKVQVQA--YSPL-----------GSPAGVQSLLSN--------------------A 206
Cdd:cd19159 177 EQAEYH--LFQREKVevQLPELyHKIGVGAmtWSPLacgiisgkygnGVPESSRASLKCyqwlkerivseegrkqqnklK 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 428171326 207 DVLRASKEEGVSAAQVLIRWAMQTCG--SAVARSSNEQRLAENLETTQVF 254
Cdd:cd19159 255 DLSPIAERLGCTLPQLAVAWCLRNEGvsSVLLGSSTPEQLIENLGAIQVL 304
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
13-256 |
3.47e-08 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 53.45 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 13 FGTfQLRGEEASRATQQAMELGYRAIDTASIY---RNEEDIAMGLAASGVRREDVFITSKL-----APNEQGYSKA--MS 82
Cdd:cd19160 26 FGS-QISDETAEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVVTTKIywggqAETERGLSRKhiIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 83 ALTSSLQRLNTSYLDLYLihwpgAAKTPLESPANKRLRleswqALEDALKLGMIRRAGVSNFCVRHLQELLACSE---LV 159
Cdd:cd19160 105 GLRGSLDRLQLEYVDIVF-----ANRSDPNSPMEEIVR-----AMTYVINQGMAMYWGTSRWSAMEIMEAYSVARqfnLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 160 PCV-NQVELHpaCFQEELLRFCEA---HKVQVQA--YSPL-------------------------------GSPAGVQSL 202
Cdd:cd19160 175 PPVcEQAEYH--LFQREKVEMQLPelyHKIGVGSvtWSPLacglitgkydgrvpdtcraavkgyqwlkekvQSEEGKKQQ 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 428171326 203 LSNADVLRASKEEGVSAAQVLIRWAMQTCG--SAVARSSNEQRLAENLETTQVFEH 256
Cdd:cd19160 253 AKVKELHPIADRLGCTVAQLAIAWCLRSEGvsSVLLGVSSAEQLIENLGSIQVLSQ 308
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
9-195 |
2.64e-07 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 50.69 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGTFQL----RGEEASRATQQ---AMELGYRAIDTASIY---RNEEDIamGLAASGVRREDVFITSKL-------- 70
Cdd:cd19152 1 PKLGFGTAPLgnlyEAVSDEEAKATlvaAWDLGIRYFDTAPWYgagLSEERL--GAALRELGREDYVISTKVgrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 71 ---APNEQG------------YSKA--MSALTSSLQRLNTSYLDLYLIHWPGAAKTPLESPA-NKRLRLESWQALEDALK 132
Cdd:cd19152 79 evePTFEPGfwnplpfdavfdYSYDgiLRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEhFAQAIKGAFRALEELRE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428171326 133 LGMIRRAGV-SN---FCVRHLQE------LLACselvpCVNQVElHPACFqeELLRFCEAHKVQVQAYSPLGS 195
Cdd:cd19152 159 EGVIKAIGLgVNdweVILRILEEadldwvMLAG-----RYTLLD-HSAAR--ELLPECEKRGVKVVNAGPFNS 223
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
1-144 |
9.42e-07 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 49.07 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 1 MEEAAGSLPPLFFGTFQLRG--------EEASRATQQAMELGYRAIDTASIYRNEEDIAM---GLAASGVRREDVFITSK 69
Cdd:cd19153 5 LEIALGNVSPVGLGTAALGGvygdgleqDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVlgkALAALQVPRSSYTVATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 70 LA---PNEQGYSKAM--SALTSSLQRLNTSYLDLYLIHwpgaaktPLESPANKRLRLESWQALEDALKLGMIRRAGVSNF 144
Cdd:cd19153 85 VGryrDSEFDYSAERvrASVATSLERLHTTYLDVVYLH-------DIEFVDYDTLVDEALPALRTLKDEGVIKRIGIAGY 157
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
11-253 |
2.77e-06 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 47.83 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 11 LFFGTF-----QLRGEEASRATQQAMELGYRAIDTASIYRNEE-DIAMG--LAASGVRREDVFITSKL-----APNEQGY 77
Cdd:cd19141 15 LGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYAAGKaEIVLGkiLKKKGWRRSSYVITTKIfwggkAETERGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 78 SKA--MSALTSSLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLAC 155
Cdd:cd19141 95 SRKhiIEGLKASLERLQLEYVDIVFANRPD-PNTPME---------EIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 156 SE----LVPCVNQVELHpaCFQEELLrfcEA------HKVQVQA--YSPL-----------GSPAGVQSLLSNADVLRAS 212
Cdd:cd19141 165 ARqfnlIPPIVEQAEYH--LFQREKV---EMqlpelfHKIGVGAmtWSPLacgilsgkyddGVPEYSRASLKGYQWLKEK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428171326 213 --KEEG------------------VSAAQVLIRWAMQTCG--SAVARSSNEQRLAENLETTQV 253
Cdd:cd19141 240 ilSEEGrrqqaklkelqiiadrlgCTLPQLAIAWCLKNEGvsSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
17-254 |
6.06e-06 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 47.00 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 17 QLRGEEASRATQQAMELGYRAIDTASIYR-NEEDIAMG--LAASGVRREDVFITSKL-----APNEQGYSKA--MSALTS 86
Cdd:cd19158 27 QITDEMAEHLMTLAYDNGINLFDTAEVYAaGKAEVVLGniIKKKGWRRSSLVITTKIfwggkAETERGLSRKhiIEGLKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 87 SLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLACSE----LVPCV 162
Cdd:cd19158 107 SLERLQLEYVDVVFANRPD-PNTPME---------ETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPIC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 163 NQVELHpaCFQEELLRFCEA---HKVQVQA--YSPLGspAGVQSLLSNADV---LRAS------------KEEG------ 216
Cdd:cd19158 177 EQAEYH--MFQREKVEVQLPelfHKIGVGAmtWSPLA--CGIVSGKYDSGIppySRASlkgyqwlkdkilSEEGrrqqak 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 428171326 217 ------------VSAAQVLIRWAMQTCG--SAVARSSNEQRLAENLETTQVF 254
Cdd:cd19158 253 lkelqaiaerlgCTLPQLAIAWCLRNEGvsSVLLGASNAEQLMENIGAIQVL 304
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
9-225 |
1.04e-04 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 42.73 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGTFQL-----RGEEASRAT-QQAMELGYRAIDTASIY-RNEEDIAMGLAASGVRREDVFITSKL----------- 70
Cdd:cd19162 1 PRLGLGAASLgnlarAGEDEAAATlDAAWDAGIRYFDTAPLYgLGLSERRLGAALARHPRAEYVVSTKVgrllepgaagr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 71 ---APNEQGYSKA--MSALTSSLQRLNTSYLDLYLIHWPG-AAKTPLES--PANKRLRLE-----------SWQALEDAl 131
Cdd:cd19162 81 pagADRRFDFSADgiRRSIEASLERLGLDRLDLVFLHDPDrHLLQALTDafPALEELRAEgvvgaigvgvtDWAALLRA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 132 klgmIRRAGVSNFCVRHLQELLAcselvpcvnqvelHPAcfQEELLRFCEAHKVQVQAYSPLGSpagvqSLLSNADVLRA 211
Cdd:cd19162 160 ----ARRADVDVVMVAGRYTLLD-------------RRA--ATELLPLCAAKGVAVVAAGVFNS-----GILATDDPAGD 215
|
250
....*....|....
gi 428171326 212 SKEEGVSAAQVLIR 225
Cdd:cd19162 216 RYDYRPATPEVLAR 229
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
38-103 |
2.23e-04 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 42.03 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 38 IDTASIYRNEED---IAMGLAASGVRREDVFITS-----------KLAPNEQG-YSKAMS-ALTSSLQRLNTSYLDLYLI 101
Cdd:cd19146 52 IDTANNYQGEESerwVGEWMASRGNRDEMVLATKyttgyrrggpiKIKSNYQGnHAKSLRlSVEASLKKLQTSYIDILYV 131
|
..
gi 428171326 102 HW 103
Cdd:cd19146 132 HW 133
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
30-193 |
2.95e-04 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 41.68 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 30 AMELGYRAIDTASIY---RNEEDIAMGLAASGVRREDVFITSKL----APNEQGYSKAM--SALTSSLQRLNTSYLDLYL 100
Cdd:cd19142 40 AYENGINYFDTSDAFtsgQAETELGRILKKKGWKRSSYIVSTKIywsyGSEERGLSRKHiiESVRASLRRLQLDYIDIVI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 101 IHwPGAAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQE-LLACSEL---VPCVNQVELHPACFQEEL 176
Cdd:cd19142 120 IH-KADPMCPME---------EVVRAMSYLIDNGLIMYWGTSRWSPVEIMEaFSIARQFncpTPICEQSEYHMFCREKME 189
|
170 180
....*....|....*....|
gi 428171326 177 LRFCEA-HKVQV--QAYSPL 193
Cdd:cd19142 190 LYMPELyNKVGVglITWSPL 209
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
21-211 |
3.35e-04 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 41.26 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 21 EEASRATQQAMELGYRAIDTASIY-RNEEDIAMGLAASGVRREDVFITSKLAPNEQGYSK---------AMSALTSSLQR 90
Cdd:cd19145 33 EEGIALIHHAFNSGVTFLDTSDIYgPNTNEVLLGKALKDGPREKVQLATKFGIHEIGGSGvevrgdpayVRAACEASLKR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 91 LNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLAcselVPCVNQVELHPA 170
Cdd:cd19145 113 LDVDYIDLYYQHRID-TTVPIE---------ITMGELKKLVEEGKIKYIGLSEASADTIRRAHA----VHPITAVQLEWS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 428171326 171 CF----QEELLRFCEAHKVQVQAYSPLG-----SPAGVQSLLSNADVLRA 211
Cdd:cd19145 179 LWtrdiEEEIIPTCRELGIGIVPYSPLGrgffaGKAKLEELLENSDVRKS 228
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
29-103 |
1.61e-03 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 39.42 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 29 QAMEL-------GYRAIDTASIYRNEE-DIAMG-LAASGVRREDVFITSKLAPN----EQGYSKA-----------MSAL 84
Cdd:cd19147 35 QAFELldafyeaGGNFIDTANNYQDEQsETWIGeWMKSRKNRDQIVIATKFTTDykayEVGKGKAvnycgnhkrslHVSV 114
|
90
....*....|....*....
gi 428171326 85 TSSLQRLNTSYLDLYLIHW 103
Cdd:cd19147 115 RDSLRKLQTDWIDILYVHW 133
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
81-205 |
1.74e-03 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 39.31 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 81 MSALTSSLQRLNTSYLDLYLIHWPGaAKTPLEspankrlrlESWQALEDALKLGMIRRAGVSNFCVRHLQELLA-CSEL- 158
Cdd:cd19151 104 IASLDQSLKRMGLDYVDIFYHHRPD-PETPLE---------ETMGALDQIVRQGKALYVGISNYPPEEAREAAAiLKDLg 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 428171326 159 VPCVnqveLHPACF-------QEELLRFCEAHKVQVQAYSPLGspagvQSLLSN 205
Cdd:cd19151 174 TPCL----IHQPKYsmfnrwvEEGLLDVLEEEGIGCIAFSPLA-----QGLLTD 218
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
9-102 |
5.26e-03 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 37.69 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428171326 9 PPLFFGTFQLRG-------EEASRATQQAMELGYRAIDTASIYRN-EEDIAMGLAASGVRREDVFITSKL---------- 70
Cdd:cd19161 1 SELGLGTAGLGNlytavsnADADATLDAAWDSGIRYFDTAPMYGHgLAEHRLGDFLREKPRDEFVLSTKVgrllkpareg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 428171326 71 -APNEQGYSKA--------------MSALTSSLQRLNTSYLDLYLIH 102
Cdd:cd19161 81 sVPDPNGFVDPlpfeivydysydgiMRSFEDSLQRLGLNRIDILYVH 127
|
|
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