|
Name |
Accession |
Description |
Interval |
E-value |
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-331 |
3.54e-138 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 396.11 E-value: 3.54e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 1 MRNLGNTNMKIKRVGFGGIPIQRITQDDTNLVINELEKQGINFIDSARGYTISEEAIGIAIEGKRDKFFLATKSMS--RD 78
Cdd:COG1453 3 YRRLGKTGLEVSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYGDSEEFLGKALKGPRDKVILATKLPPwvRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 79 YDSMKRDVEISLNNFKTDFIDLYQFHNVKEEE-YDNLFKDKMAYSALLEAKEQGKIKHIGITSHN-LNTIEKAIEDGKFD 156
Cdd:COG1453 83 PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEdLEKVLKPGGALEALEKAKAEGKIRHIGFSTHGsLEVIKEAIDTGDFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 157 TIQFPYNIVE---GQADEVFKKAHEKGIGIIVMKPLAGGALDN---------------ATLAIKYILSKDYIDVVIPGME 218
Cdd:COG1453 163 FVQLQYNYLDqdnQAGEEALEAAAEKGIGVIIMKPLKGGRLANppeklvellcpplspAEWALRFLLSHPEVTTVLSGMS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 219 SVEQVRQNVAVLENL-VLDEKDNKEIEEIRNSLGKK---FCRRCEYCMPCAVGINIPLSFLCEGYYTRYGLKEWAKEKYE 294
Cdd:COG1453 243 TPEQLDENLKTADNLePLTEEELAILERLAEELGELlkdFCTGCGYCMPCPQGINIPEVFRLYNLARAYGMREYAKERYN 322
|
330 340 350
....*....|....*....|....*....|....*....
gi 497581396 295 VM--DVKPTECIDCGLCESRCPYELPIREMLKTVVEKLG 331
Cdd:COG1453 323 ALgpGAKASACIECGACEERCPQGLDIPELLKEAHELLG 361
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-228 |
8.30e-103 |
|
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: 301.32 E-value: 8.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 1 MRNLGNTNMKIKRVGFGGIPIQRITQDDTNLVINELEKQGINFIDSARGYTISEEAIGIAIEGKRDKFFLATKSMSRDYD 80
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDSEEKIGKALKGRRDKVFLATKTGARDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 81 SMKRDVEISLNNFKTDFIDLYQFHNV-KEEEYDNLFKDKMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTIQ 159
Cdd:cd19100 81 GAKRDLERSLKRLGTDYIDLYQLHAVdTEEDLDQVFGPGGALEALLEAKEEGKIRFIGISGHSPEVLLRALETGEFDVVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497581396 160 FPYNIVE----GQADEVFKKAHEKGIGIIVMKPLAGGAL-----DNATLAIKYILSKDYIDVVIPGMESVEQVRQNVA 228
Cdd:cd19100 161 FPINPAGdhidSFREELLPLAREKGVGVIAMKVLAGGRLlsgdpLDPEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-230 |
1.69e-71 |
|
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: 222.07 E-value: 1.69e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFGGIPIQRITQDdtnlVINELEKQGINFIDSARGYTI--SEEAIGIAIEG-KRDKFFLATKSMSR- 77
Cdd:cd19105 4 RTLGKTGLKVSRLGFGGGGLPRESPE----LLRRALDLGINYFDTAEGYGNgnSEEIIGEALKGlRRDKVFLATKASPRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 78 ---DYDSMKRDVEISLNNFKTDFIDLYQFHNVKEEEYDnLFKDKMaYSALLEAKEQGKIKHIGITSHN--LNTIEKAIED 152
Cdd:cd19105 80 dkkDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEER-LLNEEL-LEALEKLKKEGKVRFIGFSTHDnmAEVLQAAIES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 153 GKFDTIQFPYNIVEGQA--DEVFKKAHEKGIGIIVMKPLAGGALDNATL-------------AIKYILSKDYIDVVIPGM 217
Cdd:cd19105 158 GWFDVIMVAYNFLNQPAelEEALAAAAEKGIGVVAMKTLAGGYLQPALLsvlkakgfslpqaALKWVLSNPRVDTVVPGM 237
|
250
....*....|...
gi 497581396 218 ESVEQVRQNVAVL 230
Cdd:cd19105 238 RNFAELEENLAAA 250
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
10-229 |
7.30e-62 |
|
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: 196.93 E-value: 7.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 10 KIKRVGFGGIPI-----QRITQDDTNLVINELEKQGINFIDSARGYT--ISEEAIGIAIEGKRDKFFLATK--------- 73
Cdd:cd19086 2 EVSEIGFGTWGLggdwwGDVDDAEAIRALRAALDLGINFFDTADVYGdgHSERLLGKALKGRRDKVVIATKfgnrfdggp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 SMSRDY--DSMKRDVEISLNNFKTDFIDLYQFHNVKEEEYDNlfkDKmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIE 151
Cdd:cd19086 82 ERPQDFspEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDN---DE-LFEALEKLKQEGKIRAYGVSVGDPEEALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 152 DGKFDTIQFPYNIVEGQA-DEVFKKAHEKGIGIIVMKPLAGGALDN--ATLAIKYILSKDYIDVVIPGMESVEQVRQNVA 228
Cdd:cd19086 158 RGGIDVVQVIYNLLDQRPeEELFPLAEEHGVGVIARVPLASGLLTGklAQAALRFILSHPAVSTVIPGARSPEQVEENAA 237
|
.
gi 497581396 229 V 229
Cdd:cd19086 238 A 238
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
12-233 |
1.93e-58 |
|
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: 188.92 E-value: 1.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 12 KRVGFGG-----IPIQRITQDDTNLVINELEKQGINFIDSARGY--TISEEAIGIAI-EGKRDKFFLATKS---MSRDYD 80
Cdd:cd19096 1 SVLGFGTmrlpeSDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYggGKSEEILGEALkEGPREKFYLATKLppwSVKSAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 81 SMKRDVEISLNNFKTDFIDLYQFHNVKEEEYDNLFKDKMAYSALLEAKEQGKIKHIGITSH-NLNTIEKAIEDGKFDTIQ 159
Cdd:cd19096 81 DFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKARKGGLLEFLEKAKKEGLIRHIGFSFHdSPELLKEILDSYDFDFVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 160 FPYNIV---EGQADEVFKKAHEKGIGIIVMKPLAGGALDN----------------ATLAIKYILSKDYIDVVIPGMESV 220
Cdd:cd19096 161 LQYNYLdqeNQAGRPGIEYAAKKGMGVIIMEPLKGGGLANnppealailcgaplspAEWALRFLLSHPEVTTVLSGMSTP 240
|
250
....*....|...
gi 497581396 221 EQVRQNVAVLENL 233
Cdd:cd19096 241 EQLDENIAAADEF 253
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
13-229 |
1.85e-57 |
|
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: 186.29 E-value: 1.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 13 RVGFGGIPIQR----ITQDDTNLVINELEKQGINFIDSARGYTISEEAIGIAIEGK-RDKFFLATK--------SMSRDY 79
Cdd:cd19095 2 VLGLGTSGIGRvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRSEERLGRALAGLrRDDLFIATKvgthgeggRDRKDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 80 --DSMKRDVEISLNNFKTDFIDLYQFHN-VKEEEYDNLFKdkmaysALLEAKEQGKIKHIGITSHNlNTIEKAIEDGKFD 156
Cdd:cd19095 82 spAAIRASIERSLRRLGTDYIDLLQLHGpSDDELTGEVLE------TLEDLKAAGKVRYIGVSGDG-EELEAAIASGVFD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 157 TIQFPYNIVEGQADEVFKKAHEKGIGIIVMKPLAGGAL--------------------------DNATLAIKYILSKDYI 210
Cdd:cd19095 155 VVQLPYNVLDREEEELLPLAAEAGLGVIVNRPLANGRLrrrvrrrplyadyarrpefaaeiggaTWAQAALRFVLSHPGV 234
|
250
....*....|....*....
gi 497581396 211 DVVIPGMESVEQVRQNVAV 229
Cdd:cd19095 235 SSAIVGTTNPEHLEENLAA 253
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-246 |
1.05e-49 |
|
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: 168.05 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 1 MRNLGNTNMKIKRVGFG----GIPIQRITQDDTNLVINE-LEkQGINFIDSARGYTI--SEEAIGIAIEG-KRDKFFLAT 72
Cdd:COG0667 3 YRRLGRSGLKVSRLGLGtmtfGGPWGGVDEAEAIAILDAaLD-AGINFFDTADVYGPgrSEELLGEALKGrPRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 73 K------------SMSRDYdsMKRDVEISLNNFKTDFIDLYQFHNVKE----EEydnlfkdkmAYSALLEAKEQGKIKHI 136
Cdd:COG0667 82 KvgrrmgpgpngrGLSREH--IRRAVEASLRRLGTDYIDLYQLHRPDPdtpiEE---------TLGALDELVREGKIRYI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 137 GITSHNLNTIEKAIE----DGKFDTIQFPYNIVEGQA-DEVFKKAHEKGIGIIVMKPLAGGAL----------------- 194
Cdd:COG0667 151 GVSNYSAEQLRRALAiaegLPPIVAVQNEYSLLDRSAeEELLPAARELGVGVLAYSPLAGGLLtgkyrrgatfpegdraa 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 195 ----------------------------DNATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:COG0667 231 tnfvqgylternlalvdalraiaaehgvTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAAD-LELSAEDLAALDAA 309
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
8-244 |
2.59e-47 |
|
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: 161.15 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 8 NMKIKRVGFGGIPI-----QRITQDDTNLVINELEKQGINFIDSARGYTI--SEEAIGIAIEGKRDKFFLATK------- 73
Cdd:cd19084 1 DLKVSRIGLGTWAIggtwwGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghSEEILGKALKGRRDDVVIATKcglrwdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 --SMSRD--YDSMKRDVEISLNNFKTDFIDLYQFH----NVKEEEydnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNT 145
Cdd:cd19084 81 gkGVTKDlsPESIRKEVEQSLRRLQTDYIDLYQIHwpdpNTPIEE---------TAEALEKLKKEGKIRYIGVSNFSVEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 146 IEKAIEDGKFDTIQFPYNIVEGQA-DEVFKKAHEKGIGIIVMKPLAGGAL------------------------DN---- 196
Cdd:cd19084 152 LEEARKYGPIVSLQPPYSMLEREIeEELLPYCRENGIGVLPYGPLAQGLLtgkykkeptfppddrrsrfpffrgENfekn 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497581396 197 ------------------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIE 244
Cdd:cd19084 232 leivdklkeiaekygkslAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALD-WELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
13-228 |
6.45e-44 |
|
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: 150.36 E-value: 6.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 13 RVGFGGIPI-QRITQDDTNLVINELEKQGINFIDSARGY--TISEEAIGIAIE--GKRDKFFLATK------------SM 75
Cdd:cd06660 2 RLGLGTMTFgGDGDEEEAFALLDAALEAGGNFFDTADVYgdGRSERLLGRWLKgrGNRDDVVIATKgghppggdpsrsRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 76 SRDYdsMKRDVEISLNNFKTDFIDLYQFH----NVKEEEydnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIE 151
Cdd:cd06660 82 SPEH--IRRDLEESLRRLGTDYIDLYYLHrddpSTPVEE---------TLEALNELVREGKIRYIGVSNWSAERLAEALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 152 DGK------FDTIQFPYNIVEGQA--DEVFKKAHEKGIGIIVMKPLAGGAldnATLAIKYILSKDYIDVVIPGMESVEQV 223
Cdd:cd06660 151 YAKahglpgFAAVQPQYSLLDRSPmeEELLDWAEENGLPLLAYSPLARGP---AQLALAWLLSQPFVTVPIVGARSPEQL 227
|
....*
gi 497581396 224 RQNVA 228
Cdd:cd06660 228 EENLA 232
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
14-246 |
6.85e-43 |
|
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: 149.77 E-value: 6.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 14 VGFG----GIPIQRITQDDTNLVINELEKQGINFIDSARGY--TISEEAIGIAI---EGKRDKFFLATKSMSRDYD---- 80
Cdd:pfam00248 1 IGLGtwqlGGGWGPISKEEALEALRAALEAGINFIDTAEVYgdGKSEELLGEALkdyPVKRDKVVIATKVPDGDGPwpsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 81 ----SMKRDVEISLNNFKTDFIDLYQFH----NVKEEEydnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIED 152
Cdd:pfam00248 81 gskeNIRKSLEESLKRLGTDYIDLYYLHwpdpDTPIEE---------TWDALEELKKEGKIRAIGVSNFDAEQIEKALTK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 153 GK--FDTIQFPYNIVEGQAD-EVFKKAHEKGIGIIVMKPLAGGALDN--------------------------------- 196
Cdd:pfam00248 152 GKipIVAVQVEYNLLRRRQEeELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgpgerrrllkkgtplnlealealee 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 497581396 197 ---------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:pfam00248 232 iakehgvspAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE-FPLSDEEVARIDEL 289
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
40-246 |
3.23e-40 |
|
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: 142.73 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 40 GINFIDSARGY--TISEEAIGIAIEGKRDKFFLATKSMSRD--YDSMKRDVEISLNNFKTDFIDLYQFH----NVKEEEY 111
Cdd:cd19085 36 GINFFDTAEAYgdGHSEEVLGKALKGRRDDVVIATKVSPDNltPEDVRKSCERSLKRLGTDYIDLYQIHwpssDVPLEET 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 112 dnlfkdkmaYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTIQFPYNI----VEgqaDEVFKKAHEKGIGIIVMK 187
Cdd:cd19085 116 ---------MEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRIDSNQLPYNLlwraIE---YEILPFCREHGIGVLAYS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 188 PLAGGAL-------------DN----------------------------------ATLAIKYILSKDYIDVVIPGMESV 220
Cdd:cd19085 184 PLAQGLLtgkfssaedfppgDArtrlfrhfepgaeeetfealeklkeiadelgvtmAQLALAWVLQQPGVTSVIVGARNP 263
|
250 260
....*....|....*....|....*.
gi 497581396 221 EQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:cd19085 264 EQLEENAAAVD-LELSPSVLERLDEI 288
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
2-231 |
5.23e-38 |
|
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: 136.91 E-value: 5.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFGGIPI----QRITQDDTNLVINELEKQGINFIDSA--RGYTISEEAIGIAIEG-KRDKFFLATK- 73
Cdd:cd19163 4 RKLGKTGLKVSKLGFGASPLggvfGPVDEEEAIRTVHEALDSGINYIDTApwYGQGRSETVLGKALKGiPRDSYYLATKv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 -----SMSRDYD-SMKR---DVEISLNNFKTDFIDLYQFHNVkeeEYDNLFKDKM--AYSALLEAKEQGKIKHIGITSHN 142
Cdd:cd19163 84 gryglDPDKMFDfSAERitkSVEESLKRLGLDYIDIIQVHDI---EFAPSLDQILneTLPALQKLKEEGKVRFIGITGYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 143 LNTIEKAIED--GKFDTIQF--PYNIVEGQADEVFKKAHEKGIGIIVMKPLAGGALDN---------------------- 196
Cdd:cd19163 161 LDVLKEVLERspVKIDTVLSycHYTLNDTSLLELLPFFKEKGVGVINASPLSMGLLTErgppdwhpaspeikeacakaaa 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 497581396 197 ---------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLE 231
Cdd:cd19163 241 ycksrgvdiSKLALQFALSNPDIATTLVGTASPENLRKNLEAAE 284
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
40-231 |
2.96e-36 |
|
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: 131.91 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 40 GINFIDSARGYTISEEAIGIAIEG-KRDKFFLATKsMSR--------DYDSMKRDVEISLNNFKTDFIDLYQFHNVKEEE 110
Cdd:cd19090 33 GINYIDTAPAYGDSEERLGLALAElPREPLVLSTK-VGRlpedtadySADRVRRSVEESLERLGRDRIDLLMIHDPERVP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 111 YDNLFKDKMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTI--QFPYNIVEGQA-DEVFKKAHEKGIGIIVMK 187
Cdd:cd19090 112 WVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGDFDVVltANRYTLLDQSAaDELLPAAARHGVGVINAS 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497581396 188 PLAGGALDN-----------------------------------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLE 231
Cdd:cd19090 192 PLGMGLLAGrppervrytyrwlspelldrakrlyelcdehgvplPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-247 |
3.95e-36 |
|
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: 132.77 E-value: 3.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFGGIPIQ----RITQDDTNLVINELEKQGINFIDSARGY--TISEEAIGIAIEGKRDKFFLATK-- 73
Cdd:cd19104 3 RRFGRTGLKVSELTFGGGGIGglmgRTTREEQIAAVRRALDLGINFFDTAPSYgdGKSEENLGRALKGLPAGPYITTKvr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 ----SMSRDYDSMKRDVEISLNNFKTDFIDLYQFHN-----------VKEEEYDNLFKDKMAySALLEAKEQGKIKHIGI 138
Cdd:cd19104 83 ldpdDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHNrigderdkpvgGTLSTTDVLGLGGVA-DAFERLRSEGKIRFIGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 139 TS-HNLNTIEKAIEDGKFDTIQFPYNIVEGQA-------------DEVFKKAHEKGIGIIVMKPLAGGAL---------- 194
Cdd:cd19104 162 TGlGNPPAIRELLDSGKFDAVQVYYNLLNPSAaearprgwsaqdyGGIIDAAAEHGVGVMGIRVLAAGALttsldrgrea 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 195 ---------------------------DNATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLENLVLDEKDNKEIEEIR 247
Cdd:cd19104 242 pptsdsdvaidfrraaafralarewgeTLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAGPLPAENLARLEALW 321
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-235 |
3.99e-35 |
|
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: 128.41 E-value: 3.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 23 RITQDDTNLVINELEKQGINFIDSARGYTISEEAIGIAIEGKrDKFFLATK------SMSRDYDSMKRDVEISLNNFKTD 96
Cdd:cd19097 22 KPSEKEAKKILEYALKAGINTLDTAPAYGDSEKVLGKFLKRL-DKFKIITKlpplkeDKKEDEAAIEASVEASLKRLKVD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 97 FIDLYQFHNVKeeeyDNLFKDKMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTIQFPYNIVEGQADE--VFK 174
Cdd:cd19097 101 SLDGLLLHNPD----DLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDIIQLPFNILDQRFLKsgLLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 175 KAHEKGIGIIV----------MKP--------------------LAGGALDNATLAIKYILSKDYIDVVIPGMESVEQVR 224
Cdd:cd19097 177 KLKKKGIEIHArsvflqglllMEPdklpakfapakpllkklhelAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLK 256
|
250
....*....|.
gi 497581396 225 QNVAVLENLVL 235
Cdd:cd19097 257 EIIAAFKKPPL 267
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
2-246 |
1.77e-30 |
|
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: 117.13 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFGgipiqritqddTNLV--------INELE---------KQGINFIDSARGYTI--SEEAIGIAIE 62
Cdd:cd19083 2 VKLGKSDIDVNPIGLG-----------TNAVgghnlypnLDEEEgkdlvrealDNGVNLLDTAFIYGLgrSEELVGEVLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 63 G-KRDKFFLATKS----------MSRDYDSMKRDVEISLNNFKTDFIDLYQFHNVKEEeydnLFKDKmAYSALLEAKEQG 131
Cdd:cd19083 71 EyNRNEVVIATKGahkfggdgsvLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGE----TPKAE-AVGALQELKDEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 132 KIKHIGITSHNLNTIEKAIEDGKFDTIQFPYNIVEGQADE-VFKKAHEKGIGIIVMKPLAGGAL---------------- 194
Cdd:cd19083 146 KIRAIGVSNFSLEQLKEANKDGYVDVLQGEYNLLQREAEEdILPYCVENNISFIPYFPLASGLLagkytkdtkfpdndlr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 195 ------------------------------DNATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLeNLVLDEKDNKEIE 244
Cdd:cd19083 226 ndkplfkgerfsenldkvdklksiadekgvTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKAL-DVTLTEEEIAFID 304
|
..
gi 497581396 245 EI 246
Cdd:cd19083 305 AL 306
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
2-246 |
6.56e-30 |
|
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: 115.75 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFGGIPIQRITQDDTNLVI-NELEKQGINFIDSARGYT--ISEEAIGIAIEGKRDKFFLATK---SM 75
Cdd:cd19087 4 RTLGRTGLKVSRLCLGTMNFGGRTDEETSFAImDRALDAGINFFDTADVYGggRSEEIIGRWIAGRRDDIVLATKvfgPM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 76 SRDYDSM-------KRDVEISLNNFKTDFIDLYQFHNvkeeeydnlFKDKMAYSALLEAKE----QGKIKHIGITSHNLN 144
Cdd:cd19087 84 GDDPNDRglsrrhiRRAVEASLRRLQTDYIDLYQMHH---------FDRDTPLEETLRALDdlvrQGKIRYIGVSNFAAW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 145 TIEKAIEDGK------FDTIQFPYNIVEGQAD-EVFKKAHEKGIGIIVMKPLAGGAL----------------------- 194
Cdd:cd19087 155 QIAKAQGIAArrgllrFVSEQPMYNLLKRQAElEILPAARAYGLGVIPYSPLAGGLLtgkygkgkrpesgrlveraryqa 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497581396 195 -----------------------DNATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:cd19087 235 rygleeyrdiaerfealaaeaglTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALE-ITLTPELLAEIDEL 308
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
1-245 |
5.21e-29 |
|
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: 113.52 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 1 MRNLGNTNMKIKRVGFG-----GIPIQRITqdDTNLVINELEKQ---GINFIDSARGYTI--SEEAIGIAIEGKRDKFFL 70
Cdd:cd19149 1 YRKLGKSGIEASVIGLGtwaigGGPWWGGS--DDNESIRTIHAAldlGINLIDTAPAYGFghSEEIVGKAIKGRRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 71 ATK------------SMSRDY---------DSMKRDVEISLNNFKTDFIDLYQFH----NVKEEEydnlfkdKMAysALL 125
Cdd:cd19149 79 ATKcglrwdreggsfFFVRDGvtvyknlspESIREEVEQSLKRLGTDYIDLYQTHwqdvETPIEE-------TME--ALE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 126 EAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTIQFPYNIV-EGQADEVFKKAHEKGIGIIVMKPLAGGAL---------- 194
Cdd:cd19149 150 ELKRQGKIRAIGASNVSVEQIKEYVKAGQLDIIQEKYSMLdRGIEKELLPYCKKNNIAFQAYSPLEQGLLtgkitpdref 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 195 --------------DN----------------------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLeNLVLDEK 238
Cdd:cd19149 230 dagdarsgipwfspENrekvlallekwkplcekygctlAQLVIAWTLAQPGITSALCGARKPEQAEENAKAG-DIRLSAE 308
|
....*..
gi 497581396 239 DNKEIEE 245
Cdd:cd19149 309 DIATMRS 315
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-228 |
1.17e-28 |
|
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: 112.41 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 13 RVGFGGIPIQRITQDDTNLV--INELEKQGINFIDSAR--GYTISEEAIGIAIEG-------KRDKFFLATK-------- 73
Cdd:cd19099 5 SLGLGTYRGDSDDETDEEYReaLKAALDSGINVIDTAInyRGGRSERLIGKALREliekggiKRDEVVIVTKagyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 -----------------------------SMSRDYdsMKRDVEISLNNFKTDFIDLYQFHN--------VKEEEYDNLFK 116
Cdd:cd19099 85 deplrplkyleeklgrglidvadsaglrhCISPAY--LEDQIERSLKRLGLDTIDLYLLHNpeeqllelGEEEFYDRLEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 117 dkmAYSALLEAKEQGKIKHIGITS-------------HNLNTIEKAIEDGK-----FDTIQFPYNIVE-----------G 167
Cdd:cd19099 163 ---AFEALEEAVAEGKIRYYGISTwdgfrappalpghLSLEKLVAAAEEVGgdnhhFKVIQLPLNLLEpealtekntvkG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497581396 168 QADEVFKKAHEKGIGIIVMKPLAGGAL----------------DNATLAIKYILSKDYIDVVIPGMESVEQVRQNVA 228
Cdd:cd19099 240 EALSLLEAAKELGLGVIASRPLNQGQLlgelrladllalpggaTLAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
1-246 |
2.23e-28 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 111.79 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 1 MRNLGNTNMKIKRVGFGGIPIQR----ITQDDTNLVINELEKQGINFIDSARGY--TISEEAIGIAIEGK---RDKFFLA 71
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLGSvfgpVSEEDAIASVREAFRLGINFFDTSPYYggTLSEKVLGKALKALgipREKYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 72 TK----SMSRDY--DSMKRDVEISLNNFKTDFIDLYQFHNVKEEEYDNLFKDKMAysALLEAKEQGKIKHIGITSHNLNT 145
Cdd:PLN02587 81 TKcgryGEGFDFsaERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIVNETIP--ALQKLKESGKVRFIGITGLPLAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 146 ---IEKAIEDGKFDTI--QFPYNIVEGQADEVFKKAHEKGIGIIVMKPLAGGALDN------------------------ 196
Cdd:PLN02587 159 ftyVLDRVPPGTVDVIlsYCHYSLNDSSLEDLLPYLKSKGVGVISASPLAMGLLTEngppewhpappelksacaaaathc 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 197 -------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAV---LENLVLDEKDNKEIEEI 246
Cdd:PLN02587 239 kekgkniSKLALQYSLSNKDISTTLVGMNSVQQVEENVAAateLETSGIDEELLSEVEAI 298
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
11-236 |
8.40e-28 |
|
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: 108.84 E-value: 8.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 11 IKRVGFGG--IPIQRITQDDTNL-----VINELEKQGINFIDSARGYTI--SEEAIGIAIEGKRDKFFLATK-SMSRDYD 80
Cdd:cd19088 1 VSRLGYGAmrLTGPGIWGPPADReeaiaVLRRALELGVNFIDTADSYGPdvNERLIAEALHPYPDDVVIATKgGLVRTGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 81 ----------SMKRDVEISLNNFKTDFIDLYQFHNVkEEEYDnlFKDKMaySALLEAKEQGKIKHIGITSHNLNTIEKAI 150
Cdd:cd19088 81 gwwgpdgspeYLRQAVEASLRRLGLDRIDLYQLHRI-DPKVP--FEEQL--GALAELQDEGLIRHIGLSNVTVAQIEEAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 151 EDGKFDTIQFPYNIVEGQADEVFKKAHEKGIGIIVMKPLAGGAL----------------DNATLAIKYILSK-DYIdVV 213
Cdd:cd19088 156 AIVRIVSVQNRYNLANRDDEGVLDYCEAAGIAFIPWFPLGGGDLaqpggllaevaarlgaTPAQVALAWLLARsPVM-LP 234
|
250 260
....*....|....*....|...
gi 497581396 214 IPGMESVEQVRQNVAVLEnLVLD 236
Cdd:cd19088 235 IPGTSSVEHLEENLAAAG-LRLS 256
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
40-244 |
2.81e-26 |
|
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: 105.00 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 40 GINFIDSARGY--TISEEAIGIAIEG-KRDKFFLATKsMSRD---YDSMKRDVEISLNNFKTDFIDLYQFH----NVKEE 109
Cdd:cd19072 39 GINLIDTAEMYggGHAEELVGKAIKGfDREDLFITTK-VSPDhlkYDDVIKAAKESLKRLGTDYIDLYLIHwpnpSIPIE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 110 EydnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIE---DGKFDTIQFPYNIVE-GQADEVFKKAHEKGIGIIV 185
Cdd:cd19072 118 E---------TLRAMEELVEEGKIRYIGVSNFSLEELEEAQSylkKGPIVANQVEYNLFDrEEESGLLPYCQKNGIAIIA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497581396 186 MKPLAGGALDN------------------ATLAIKYILSKDYIdVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIE 244
Cdd:cd19072 189 YSPLEKGKLSNakgsplldeiakkygktpAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG-WELSEEDLQRLD 263
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
39-246 |
2.89e-26 |
|
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: 106.11 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 39 QGINFIDSARGYTI---------SEEAIG--IAIEGKRDKFFLATKSMSR--------------DYDSMKRDVEISLNNF 93
Cdd:cd19094 30 EGVNFIDTAEMYPVppspetqgrTEEIIGswLKKKGNRDKVVLATKVAGPgegitwprgggtrlDRENIREAVEGSLKRL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 94 KTDFIDLYQFH-------NVKEEEYDNLFKDKMAYS------ALLEAKEQGKIKHIGITSHN----LNTIEKAIEDG--K 154
Cdd:cd19094 110 GTDYIDLYQLHwpdrytpLFGGGYYTEPSEEEDSVSfeeqleALGELVKAGKIRHIGLSNETpwgvMKFLELAEQLGlpR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 155 FDTIQFPYNI-----VEGQAdEVfkkAHEKGIGIIVMKPLAGGAL----------------------------------- 194
Cdd:cd19094 190 IVSIQNPYSLlnrnfEEGLA-EA---CHRENVGLLAYSPLAGGVLtgkyldgaarpeggrlnlfpgymaryrspqaleav 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497581396 195 ------------DNATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLeNLVLDEKDNKEIEEI 246
Cdd:cd19094 266 aeyvklarkhglSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAF-DVPLSDELLAEIDAV 328
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-246 |
2.90e-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: 103.14 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 11 IKRVGFGGIPI-------QRITQDDTNLV--INELEKQGINFIDSARGY--TISEEAIGIAIEGKRDKFFLATK------ 73
Cdd:cd19102 1 LTTIGLGTWAIggggwggGWGPQDDRDSIaaIRAALDLGINWIDTAAVYglGHSEEVVGRALKGLRDRPIVATKcgllwd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 ---SMSRDYD--SMKRDVEISLNNFKTDFIDLYQFHNVKEEEydNLfkdKMAYSALLEAKEQGKIKHIGITSHNLNTIEK 148
Cdd:cd19102 81 eegRIRRSLKpaSIRAECEASLRRLGVDVIDLYQIHWPDPDE--PI---EEAWGALAELKEEGKVRAIGVSNFSVDQMKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 149 AIEDGKFDTIQFPYNIVE-GQADEVFKKAHEKGIGIIVMKPLAGGAL---------------DN---------------- 196
Cdd:cd19102 156 CQAIHPIASLQPPYSLLRrGIEAEILPFCAEHGIGVIVYSPMQSGLLtgkmtpervaslpadDWrrrspffqepnlarnl 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497581396 197 -----------------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:cd19102 236 alvdalrpiaerhgrtvAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAAD-LRLTPEELAEIEAL 301
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
4-239 |
1.96e-23 |
|
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: 98.06 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 4 LGNTNMKIKRVGFGGIPI-QRITQDDTNLVINELEKQGINFIDSARGYTI---------SEEAIG--IAIEGKRDKFFLA 71
Cdd:cd19081 2 LGRTGLSVSPLCLGTMVFgWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnaggeSETIIGrwLKSRGKRDRVVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 72 TKS----------MSRDYdsMKRDVEISLNNFKTDFIDLYQFH----NVKEEEYdnlfkdkmaYSALLEAKEQGKIKHIG 137
Cdd:cd19081 82 TKVgfpmgpngpgLSRKH--IRRAVEASLRRLQTDYIDLYQAHwddpATPLEET---------LGALNDLIRQGKVRYIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 138 ITSHNLNTIEKAIEDGK------FDTIQFPYNIV-----EGqadEVFKKAHEKGIGIIVMKPLAGG-------------- 192
Cdd:cd19081 151 ASNYSAWRLQEALELSRqhglprYVSLQPEYNLVdresfEG---ELLPLCREEGIGVIPYSPLAGGfltgkyrseadlpg 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497581396 193 ---------------------ALDN---------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVlENLVLDEKD 239
Cdd:cd19081 228 strrgeaakrylnerglrildALDEvaaehgatpAQVALAWLLARPGVTAPIAGARTVEQLEDLLAA-AGLRLTDEE 303
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
44-244 |
2.86e-23 |
|
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: 96.40 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 44 IDSARGYTiSEEAIGIAIEG---KRDKFFLATK--SMSRDYDSMKRDVEISLNNFKTDFIDLYQFHN---VKEEEYDNLF 115
Cdd:cd19071 31 IDTAAAYG-NEAEVGEAIREsgvPREELFITTKlwPTDHGYERVREALEESLKDLGLDYLDLYLIHWpvpGKEGGSKEAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 116 KDkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKF--DTIQF---PYNivegQADEVFKKAHEKGIGIIVMKPLA 190
Cdd:cd19071 110 LE--TWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIkpAVNQIelhPYL----QQKELVEFCKEHGIVVQAYSPLG 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497581396 191 GGA---LDNATL--------------AIKYILSKDYidVVIPGMESVEQVRQNVAVLeNLVLDEKDNKEIE 244
Cdd:cd19071 184 RGRrplLDDPVLkeiakkygktpaqvLLRWALQRGV--VVIPKSSNPERIKENLDVF-DFELSEEDMAAID 251
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
14-244 |
2.93e-22 |
|
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: 93.49 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 14 VGFGgipIQRITQDDTNLVINELEKQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATK--SMSRDYDSMKRDVEI 88
Cdd:cd19073 4 LGLG---TWQLRGDDCANAVKEALELGYRHIDTAEIYN-NEAEVGEAIAEsgvPREDLFITTKvwRDHLRPEDLKKSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 89 SLNNFKTDFIDLYQFH----NVKEEEydnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDG--KFDTIQFPY 162
Cdd:cd19073 80 SLEKLGTDYVDLLLIHwpnpTVPLEE---------TLGALKELKEAGKVKSIGVSNFTIELLEEALDISplPIAVNQVEF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 163 NIVEGQAdEVFKKAHEKGIGIIVMKPLA-GGALDN--------------ATLAIKYILSKDYidVVIPGMESVEQVRQNV 227
Cdd:cd19073 151 HPFLYQA-ELLEYCRENDIVITAYSPLArGEVLRDpviqeiaekydktpAQVALRWLVQKGI--VVIPKASSEDHLKENL 227
|
250
....*....|....*..
gi 497581396 228 AVLeNLVLDEKDNKEIE 244
Cdd:cd19073 228 AIF-DWELTSEDVAKID 243
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-246 |
1.25e-21 |
|
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: 93.45 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 1 MRNLGNTNMKIKRVGFG--------GIP--IQRITQDDTNLVINELEKQGINFIDSARGYT--ISEEAIGIAIEGKRDKF 68
Cdd:cd19091 3 YRTLGRSGLKVSELALGtmtfggggGFFgaWGGVDQEEADRLVDIALDAGINFFDTADVYSegESEEILGKALKGRRDDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 69 FLATK---SMSRDYDS-------MKRDVEISLNNFKTDFIDLYQFHNvkeeeYDNLFKDKMAYSALLEAKEQGKIKHIGI 138
Cdd:cd19091 83 LIATKvrgRMGEGPNDvglsrhhIIRAVEASLKRLGTDYIDLYQLHG-----FDALTPLEETLRALDDLVRQGKVRYIGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 139 TSHNLNTIEKA--IED----GKFDTIQFPYNIVEGQAD-EVFKKAHEKGIGIIVMKPLAGG------------------- 192
Cdd:cd19091 158 SNFSAWQIMKAlgISErrglARFVALQAYYSLLGRDLEhELMPLALDQGVGLLVWSPLAGGllsgkyrrgqpapegsrlr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 193 -------------------ALDN---------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIE 244
Cdd:cd19091 238 rtgfdfppvdrergydvvdALREiaketgatpAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAG-LSLTPEEIARLD 316
|
..
gi 497581396 245 EI 246
Cdd:cd19091 317 KV 318
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
39-194 |
3.56e-20 |
|
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: 88.90 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 39 QGINFIDSA--RGYTISEEAIGIAIE--GKRDKFFLATK---------SMSRDY--DSMKRDVEISLNNFKTDFIDLYQF 103
Cdd:cd19148 37 LGINLIDTApvYGFGLSEEIVGKALKeyGKRDRVVIATKvglewdeggEVVRNSspARIRKEVEDSLRRLQTDYIDLYQV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 104 H----NVKEEEydnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTIQFPYNIVEGQADE-VFKKAHE 178
Cdd:cd19148 117 HwpdpLVPIEE---------TAEALKELLDEGKIRAIGVSNFSPEQMETFRKVAPLHTVQPPYNLFEREIEKdVLPYARK 187
|
170
....*....|....*.
gi 497581396 179 KGIGIIVMKPLAGGAL 194
Cdd:cd19148 188 HNIVTLAYGALCRGLL 203
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-246 |
3.67e-20 |
|
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: 88.08 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 10 KIKRVGFGgipIQRITQDDTNLVINELEKQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATKSMSRDY--DSMKR 84
Cdd:cd19140 7 RIPALGLG---TYPLTGEECTRAVEHALELGYRHIDTAQMYG-NEAQVGEAIAAsgvPRDELFLTTKVWPDNYspDDFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 85 DVEISLNNFKTDFIDLYQFH----NVKEEEydnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIE--DGKFDTI 158
Cdd:cd19140 83 SVEESLRKLRTDYVDLLLLHwpnkDVPLAE---------TLGALNEAQEAGLARHIGVSNFTVALLREAVElsEAPLFTN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 159 QFPYNIVEGQADeVFKKAHEKGIGIIVMKPLA-GGALDNATL--------------AIKYILSKDYIdVVIPGMESVEQV 223
Cdd:cd19140 154 QVEYHPYLDQRK-LLDAAREHGIALTAYSPLArGEVLKDPVLqeigrkhgktpaqvALRWLLQQEGV-AAIPKATNPERL 231
|
250 260
....*....|....*....|...
gi 497581396 224 RQNVAVLeNLVLDEKDNKEIEEI 246
Cdd:cd19140 232 EENLDIF-DFTLSDEEMARIAAL 253
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
13-237 |
5.14e-20 |
|
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: 88.44 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 13 RVGFGGIPI----QRITQDDTNLVINELEKQGINFIDSA--RGYTISEEAIGIAI-EGKRDKFFLATK------------ 73
Cdd:cd19152 2 KLGFGTAPLgnlyEAVSDEEAKATLVAAWDLGIRYFDTApwYGAGLSEERLGAALrELGREDYVISTKvgrllvplqeve 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 -------------SMSRDY--DSMKRDVEISLNNFKTDFIDLYQFHNVKEEEYDNLFKDKM------AYSALLEAKEQGK 132
Cdd:cd19152 82 ptfepgfwnplpfDAVFDYsyDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFaqaikgAFRALEELREEGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 133 IKHIGITSHNLNTIEKAIEDGKFDTIQFP--YNIVE-GQADEVFKKAHEKGIGIIVMKPLAGGAL--------------- 194
Cdd:cd19152 162 IKAIGLGVNDWEVILRILEEADLDWVMLAgrYTLLDhSAARELLPECEKRGVKVVNAGPFNSGFLaggdnfdyyeygpap 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497581396 195 -------------------DNATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLENLVLDE 237
Cdd:cd19152 242 peliarrdriealceqhgvSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
2-246 |
6.73e-20 |
|
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: 88.65 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFGGIPIQ-----RITQDDTNLVINELEKQGINFIDSARGYTISEEAIGI---AIEGKRDKFFLATK 73
Cdd:cd19144 4 RTLGRNGPSVPALGFGAMGLSafygpPKPDEERFAVLDAAFELGCTFWDTADIYGDSEELIGRwfkQNPGKREKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 ------------SMSRDYDSMKRDVEISLNNFKTDFIDLYQFHNVkeeeyDNLFKDKMAYSALLEAKEQGKIKHIGITSH 141
Cdd:cd19144 84 fgieknvetgeySVDGSPEYVKKACETSLKRLGVDYIDLYYQHRV-----DGKTPIEKTVAAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 142 NLNTIEKAIEDGKFDTIQFPYNI----VEGQADEVFKKAHEKGIGIIVMKPLAGGAL----------------------- 194
Cdd:cd19144 159 SAETLRRAHAVHPIAAVQIEYSPfsldIERPEIGVLDTCRELGVAIVAYSPLGRGFLtgairspddfeegdfrrmaprfq 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497581396 195 --------------------DNAT---LAIKYILSKDYIDVVIPGMESVEQVRQNVAVLeNLVLDEKDNKEIEEI 246
Cdd:cd19144 239 aenfpknlelvdkikaiakkKNVTagqLTLAWLLAQGDDIIPIPGTTKLKRLEENLGAL-KVKLTEEEEKEIREI 312
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
40-246 |
1.73e-19 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 86.26 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 40 GINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATKSMSRD--YDSMKRDVEISLNNFKTDFIDLYQFH---NVKEEEy 111
Cdd:COG0656 31 GYRHIDTAAMYG-NEEGVGEAIAAsgvPREELFVTTKVWNDNhgYDDTLAAFEESLERLGLDYLDLYLIHwpgPGPYVE- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 112 dnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIE--DGKFDTIQFPYNIVEGQaDEVFKKAHEKGIGIIVMKPL 189
Cdd:COG0656 109 --------TWRALEELYEEGLIRAIGVSNFDPEHLEELLAetGVKPAVNQVELHPYLQQ-RELLAFCREHGIVVEAYSPL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497581396 190 A-GGALDNATL--------------AIKYILSKDYIdvVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:COG0656 180 GrGKLLDDPVLaeiaekhgktpaqvVLRWHLQRGVV--VIPKSVTPERIRENLDAFD-FELSDEDMAAIDAL 248
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
32-244 |
1.94e-19 |
|
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: 86.90 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 32 VINELEKQGINFIDSAR--GYTISEEAIGIAIE--GKRDKFFLATKSM----SRDYDSMKRDVEISLNNFKTDFIDLYQF 103
Cdd:cd19093 31 AFDAALEAGVNLFDTAEvyGTGRSERLLGRFLKelGDRDEVVIATKFAplpwRLTRRSVVKALKASLERLGLDSIDLYQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 104 HNVkeeeYDNLFKDKMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTI-----QFPYNIVEGQA--DEVFKKA 176
Cdd:cd19093 111 HWP----GPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERGVplasnQVEYSLLYRDPeqNGLLPAC 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 177 HEKGIGIIVMKPLAGGAL------DN------------------------------------ATLAIKYILSKDYIdvVI 214
Cdd:cd19093 187 DELGITLIAYSPLAQGLLtgkyspENpppggrrrlfgrknlekvqplldaleeiaekygktpAQVALNWLIAKGVV--PI 264
|
250 260 270
....*....|....*....|....*....|
gi 497581396 215 PGMESVEQVRQNVAVLeNLVLDEKDNKEIE 244
Cdd:cd19093 265 PGAKNAEQAEENAGAL-GWRLSEEEVAELD 293
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
3-244 |
3.87e-19 |
|
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: 86.10 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 3 NLGNTNMKIKRVGFG----GIPIQR---ITQDDTNLVINE-LEKqGINFIDSARGYT--ISEEAIGIAIE--GKRDKFFL 70
Cdd:cd19079 4 RLGNSGLKVSRLCLGcmsfGDPKWRpwvLDEEESRPIIKRaLDL-GINFFDTANVYSggASEEILGRALKefAPRDEVVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 71 ATK---SMSRDYD----SMK---RDVEISLNNFKTDFIDLYQFHNVkeeEYDNLFKDKMaySALLEAKEQGKIKHIGITS 140
Cdd:cd19079 83 ATKvyfPMGDGPNgrglSRKhimAEVDASLKRLGTDYIDLYQIHRW---DYETPIEETL--EALHDVVKSGKVRYIGASS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 141 ------HNLNTIEKAIEDGKFDTIQFPYNIVEGQAD-EVFKKAHEKGIGIIVMKPLAGGAL------------------- 194
Cdd:cd19079 158 myawqfAKALHLAEKNGWTKFVSMQNHYNLLYREEErEMIPLCEEEGIGVIPWSPLARGRLarpwgdtterrrsttdtak 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497581396 195 --------------------------DNATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIE 244
Cdd:cd19079 238 lkydyfteadkeivdrveevakergvSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALD-IKLSEEEIKYLE 312
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
11-246 |
1.60e-18 |
|
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: 83.17 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 11 IKRVGFGGIpiqRITQDD-TNLVINELEkQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATKSMSRDY--DSMKR 84
Cdd:cd19139 1 IPAFGLGTF---RLKDDVvIDSVRTALE-LGYRHIDTAQIYD-NEAAVGQAIAEsgvPRDELFITTKIWIDNLskDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 85 DVEISLNNFKTDFIDLYQFH------NVKEEEYDNlfkdkmaysALLEAKEQGKIKHIGITSHNLNTIEKAIE---DGKF 155
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHwpspndEVPVEEYIG---------ALAEAKEQGLTRHIGVSNFTIALLDEAIAvvgAGAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 156 DTIQF---PYNivegQADEVFKKAHEKGIGIIVMKPLA-GGALD-----------NAT---LAIKYILSKDYIdvVIPGM 217
Cdd:cd19139 147 ATNQIelsPYL----QNRKLVAHCKQHGIHVTSYMTLAyGKVLDdpvlaaiaerhGATpaqIALAWAMARGYA--VIPSS 220
|
250 260
....*....|....*....|....*....
gi 497581396 218 ESVEQVRQNVAVLeNLVLDEKDNKEIEEI 246
Cdd:cd19139 221 TKREHLRSNLLAL-DLTLDADDMAAIAAL 248
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-243 |
2.48e-18 |
|
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: 83.80 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFG--GIPIQRITQDD-TNL-VINELEKQGINFIDSAR--GYTISEEAIGIAIEGKRDKFFLATK-- 73
Cdd:cd19076 3 RKLGTQGLEVSALGLGcmGMSAFYGPADEeESIaTLHRALELGVTFLDTADmyGPGTNEELLGKALKDRRDEVVIATKfg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 ------------SMSRDYdsMKRDVEISLNNFKTDFIDLYQFH----NVKEEEydnlfkdkmAYSALLEAKEQGKIKHIG 137
Cdd:cd19076 83 ivrdpgsgfrgvDGRPEY--VRAACEASLKRLGTDVIDLYYQHrvdpNVPIEE---------TVGAMAELVEEGKVRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 138 ITSHNLNTIEKAIEDGKFDTIQFPYNIVEGQA-DEVFKKAHEKGIGIIVMKPLAGGAL---------------------- 194
Cdd:cd19076 152 LSEASADTIRRAHAVHPITAVQSEYSLWTRDIeDEVLPTCRELGIGFVAYSPLGRGFLtgaikspedlpeddfrrnnprf 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497581396 195 --DN----------------------ATLAIKYILSKDYiDVV-IPGMESVEQVRQNVAVLeNLVLDEKDNKEI 243
Cdd:cd19076 232 qgENfdknlklvekleaiaaekgctpAQLALAWVLAQGD-DIVpIPGTKRIKYLEENVGAL-DVVLTPEELAEI 303
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
2-239 |
4.35e-18 |
|
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: 82.97 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFGGIPIQRI-----TQDDTNLVINELEKQGINFIDSARGY--TISEEAIGIAI---EGKRDKFFLA 71
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVygdglEQDEAVAIVAEAFAAGINHFDTSPYYgaESSEAVLGKALaalQVPRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 72 TK-----SMSRDY--DSMKRDVEISLNNFKTDFIDLYQFHNVKEEEYDNLFKDkmAYSALLEAKEQGKIKHIGITSHNLN 144
Cdd:cd19153 83 TKvgryrDSEFDYsaERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTLVDE--ALPALRTLKDEGVIKRIGIAGYPLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 145 TIEKAIED---GKFDTIQfPYNIVEGQADEVFKKA----HEKGIGIIVMKPLAGGAL----------------------- 194
Cdd:cd19153 161 TLTRATRRcspGSLDAVL-SYCHLTLQDARLESDApglvRGAGPHVINASPLSMGLLtsqgpppwhpasgelrhyaaaad 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 497581396 195 --------DNATLAIKYILS-KDYIDVVIPGMESVEQVRQNVAVLENLVLDEKD 239
Cdd:cd19153 240 avcasveaSLPDLALQYSLAaHAGVGTVLLGPSSLAQLRSMLAAVDAVASLGAA 293
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
8-245 |
8.63e-17 |
|
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: 79.20 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 8 NMKIKRVGFG--------GIPIQRitQDDTNLVINELEKqGINFIDSARGYT--ISEEAIGIAIEGKRDKFFLATK---- 73
Cdd:cd19078 1 GLEVSAIGLGcmgmshgyGPPPDK--EEMIELIRKAVEL-GITFFDTAEVYGpyTNEELVGEALKPFRDQVVIATKfgfk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 74 -------SMSRD--YDSMKRDVEISLNNFKTDFIDLYQFH----NVKEEEydnlfkdkMAySALLEAKEQGKIKHIGITS 140
Cdd:cd19078 78 idggkpgPLGLDsrPEHIRKAVEGSLKRLQTDYIDLYYQHrvdpNVPIEE--------VA-GTMKELIKEGKIRHWGLSE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 141 HNLNTIEKAIEDGKFDTIQFPYNIVE-GQADEVFKKAHEKGIGIIVMKPLA----GGALD-------------------- 195
Cdd:cd19078 149 AGVETIRRAHAVCPVTAVQSEYSMMWrEPEKEVLPTLEELGIGFVPFSPLGkgflTGKIDentkfdegddraslprftpe 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497581396 196 -------------------NAT---LAIKYILSKDYIDVVIPGMESVEQVRQNVAVLeNLVLDEKDNKEIEE 245
Cdd:cd19078 229 aleanqalvdllkefaeekGATpaqIALAWLLAKKPWIVPIPGTTKLSRLEENIGAA-DIELTPEELREIED 299
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
40-194 |
1.31e-16 |
|
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: 78.80 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 40 GINFIDSARGYT--ISEEAIGIAIEGKRDKFFLATK-SMSRDYD----------SMKRDVEISLNNFKTDFIDLYQFHnv 106
Cdd:cd19080 44 GGNFIDTANNYTngTSERLLGEFIAGNRDRIVLATKyTMNRRPGdpnaggnhrkNLRRSVEASLRRLQTDYIDLLYVH-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 107 keeeydnlFKDKMA-----YSALLEAKEQGKIKHIGITS------HNLNTIEKAIEDGKFDTIQFPYNIVEGQAD-EVFK 174
Cdd:cd19080 122 --------AWDFTTpveevMRALDDLVRAGKVLYVGISDtpawvvARANTLAELRGWSPFVALQIEYSLLERTPErELLP 193
|
170 180
....*....|....*....|
gi 497581396 175 KAHEKGIGIIVMKPLAGGAL 194
Cdd:cd19080 194 MARALGLGVTPWSPLGGGLL 213
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
15-244 |
2.93e-16 |
|
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: 77.23 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 15 GFGGIPIQRITQDDTnlVINELEKQ---GINFIDSARGYTI--SEEAIGIAIEG-KRDKFFLATKSMSRD--YDSMKRDV 86
Cdd:cd19137 13 GIGGFLTPDYSRDEE--MVELLKTAielGYTHIDTAEMYGGghTEELVGKAIKDfPREDLFIVTKVWPTNlrYDDLLRSL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 87 EISLNNFKTDFIDLYQFH----NVKEEEydnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTI--QF 160
Cdd:cd19137 91 QNSLRRLDTDYIDLYLIHwpnpNIPLEE---------TLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVcnQV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 161 PYNIVEG--QADEVFKKAHEKGIGIIVMKPLAGGALDN---------------ATLAIKYILSKDYIdVVIPGMESVEQV 223
Cdd:cd19137 162 KYNLEDRdpERDGLLEYCQKNGITVVAYSPLRRGLEKTnrtleeiaknygktiAQIALAWLIQKPNV-VAIPKAGRVEHL 240
|
250 260
....*....|....*....|.
gi 497581396 224 RQNVAVLEnLVLDEKDNKEIE 244
Cdd:cd19137 241 KENLKATE-IKLSEEEMKLLD 260
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-247 |
4.75e-16 |
|
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: 381324 [Multi-domain] Cd Length: 318 Bit Score: 77.38 E-value: 4.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 26 QDDTNLVINELEKQGINFIDSARGYTISEEAIGIAIEGKRDKFFLATKSMSRDY--------DSMKRDV-EISLNNFKT- 95
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSYGRAEEFLGSWLRSRNIAPDAVFVGSKWGYtytadwqvDAAVHEVkDHSLARLLKq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 96 ---------DFIDLYQFHNVKEEEydNLFKDKMAYSALLEAKEQGkIKhIGIT---SHNLNTIEKAIE---DGK--FDTI 158
Cdd:cd19098 114 weetrsllgKHLDLYQIHSATLES--GVLEDADVLAALAELKAEG-VK-IGLSlsgPQQAETLRRALEieiDGArlFDSV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 159 QFPYNIVEGQADEVFKKAHEKGIGIIVMKPLAGGALD----------------------NAT---LAIKYILSKDYIDVV 213
Cdd:cd19098 190 QATWNLLEQSAGEALEEAHEAGMGVIVKEALANGRLTdrnpspelaplmavlkavadrlGVTpdaLALAAVLAQPFVDVV 269
|
250 260 270
....*....|....*....|....*....|....
gi 497581396 214 IPGMESVEQVRQNVAVLEnLVLDEKDNKEIEEIR 247
Cdd:cd19098 270 LSGAATPEQLRSNLRALD-VSLDLELLAALADLA 302
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
6-244 |
1.41e-15 |
|
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: 75.10 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 6 NTNMKIKRVGFGgipIQRITQDDTNLVINELEKQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATK--SMSRDYD 80
Cdd:cd19131 5 NDGNTIPQLGLG---VWQVSNDEAASAVREALEVGYRSIDTAAIYG-NEEGVGKAIRAsgvPREELFITTKlwNSDQGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 81 SMKRDVEISLNNFKTDFIDLYQFHnvkeeeYDNLFKDKM--AYSALLEAKEQGKIKHIGITSHNLNTIEKAI-EDGKFDT 157
Cdd:cd19131 81 STLRAFDESLRKLGLDYVDLYLIH------WPVPAQDKYveTWKALIELKKEGRVKSIGVSNFTIEHLQRLIdETGVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 158 IqfpyNIVE----GQADEVfKKAHEK-GIGIIVMKPLA-GGALDNATL---AIKY------ILSKDYID---VVIPGMES 219
Cdd:cd19131 155 V----NQIElhprFQQREL-RAFHAKhGIQTESWSPLGqGGLLSDPVIgeiAEKHgktpaqVVIRWHLQnglVVIPKSVT 229
|
250 260
....*....|....*....|....*
gi 497581396 220 VEQVRQNVAVLEnLVLDEKDNKEIE 244
Cdd:cd19131 230 PSRIAENFDVFD-FELDADDMQAIA 253
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
39-244 |
1.17e-14 |
|
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: 72.67 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 39 QGINFIDSARGYT--ISEEAIGIAIEGKRDKFFLATKSMSR--DYDSMKRDVEISLNNFKTDFIDLYQFH---NVKEEEy 111
Cdd:cd19138 41 LGMTLIDTAEMYGdgGSEELVGEAIRGRRDKVFLVSKVLPSnaSRQGTVRACERSLRRLGTDYLDLYLLHwrgGVPLAE- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 112 dnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTI---QFPYNIVE-GQADEVFKKAHEKGIGIIVMK 187
Cdd:cd19138 120 --------TVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCaanQVLYNLGSrGIEYDLLPWCREHGVPVMAYS 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497581396 188 PLA-GGALDN-------------------ATLAIKYILSKDYIdVVIPGMESVEQVRQNVAVLeNLVLDEKDNKEIE 244
Cdd:cd19138 192 PLAqGGLLRRgllenptlkeiaarhgatpAQVALAWVLRDGNV-IAIPKSGSPEHARENAAAA-DLELTEEDLAELD 266
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
13-137 |
8.95e-14 |
|
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: 70.66 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 13 RVGFGGIPI-QRITQDDTNLVINELEKQGINFIDSARGY------TISEEAIG--IAIEGKRDKFFLATK-------SMS 76
Cdd:cd19082 2 RIVLGTADFgTRIDEEEAFALLDAFVELGGNFIDTARVYgdwverGASERVIGewLKSRGNRDKVVIATKgghpdleDMS 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497581396 77 RDY---DSMKRDVEISLNNFKTDFIDLYQFHnvkeeeYDNLfkdKMAYSALLEA----KEQGKIKHIG 137
Cdd:cd19082 82 RSRlspEDIRADLEESLERLGTDYIDLYFLH------RDDP---SVPVGEIVDTlnelVRAGKIRAFG 140
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-237 |
2.09e-13 |
|
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: 69.66 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 14 VGFGGIPI----QRITQDDTNLVINELEKQGINFIDSA--RGYTISEEAIGIAIEGK-RDKFFLATK----------SMS 76
Cdd:cd19161 3 LGLGTAGLgnlyTAVSNADADATLDAAWDSGIRYFDTApmYGHGLAEHRLGDFLREKpRDEFVLSTKvgrllkpareGSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 77 RD-----------------YDSMKRDVEISLNNFKTDFIDLYQFHNVK-----EEEYDNLFKDKM--AYSALLEAKEQGK 132
Cdd:cd19161 83 PDpngfvdplpfeivydysYDGIMRSFEDSLQRLGLNRIDILYVHDIGvythgDRKERHHFAQLMsgGFKALEELKKAGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 133 IKHIGITSHNLNTIEKAIEDGKFDT--IQFPYNIVE-GQADEVFKKAHEKGIGIIVMKPLAGGALDN------------- 196
Cdd:cd19161 163 IKAFGLGVNEVQICLEALDEADLDCflLAGRYSLLDqSAEEEFLPRCEQRGTSLVIGGVFNSGILATgtksgakfnygda 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497581396 197 ----------------------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLENLVLDE 237
Cdd:cd19161 243 paeiisrvmeiekicdaynvplAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTDIPEE 305
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-231 |
1.18e-12 |
|
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: 67.23 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 10 KIKRVGFGGIPI--QRITQDDTNLVINELEKQGINFIDSARGY--TISEEAIGIAIEG-KRDKFFLATK---SMSRD-YD 80
Cdd:cd19074 3 KVSELSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYaaGQAEEVLGKALKGwPRESYVISTKvfwPTGPGpND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 81 ---SMKRDVE---ISLNNFKTDFIDLYQFH----NVKEEEydnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAI 150
Cdd:cd19074 83 rglSRKHIFEsihASLKRLQLDYVDIYYCHrydpETPLEE---------TVRAMDDLIRQGKILYWGTSEWSAEQIAEAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 151 EDGK------FDTIQFPYNIVEGQA-DEVFKKAHEKGIGIIVMKPLAGGALDN--------------------------- 196
Cdd:cd19074 154 DLARqfglipPVVEQPQYNMLWREIeEEVIPLCEKNGIGLVVWSPLAQGLLTGkyrdgipppsrsratdednrdkkrrll 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 497581396 197 ----------------------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLE 231
Cdd:cd19074 234 tdenlekvkklkpiadelgltlAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASG 290
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-201 |
2.61e-12 |
|
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: 66.10 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 10 KIKRVGFG------GIPIQRITQDDTNLVINELeKQGINFIDSARGYTiSEEAIGIAI---EGKRDKFFLATKsMSRDYD 80
Cdd:cd19120 3 KIPAIAFGtgtawyKSGDDDIQRDLVDSVKLAL-KAGFRHIDTAEMYG-NEKEVGEALkesGVPREDLFITTK-VSPGIK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 81 SMKRDVEISLNNFKTDFIDLYQFHN---VKEEEYDNlfkdKMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGK--- 154
Cdd:cd19120 80 DPREALRKSLAKLGVDYVDLYLIHSpffAKEGGPTL----AEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKikp 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497581396 155 -FDTIQF-PYNIVEGQADEVFKKAHekgiGIIVM-----KPL---AGGALDNATLAI 201
Cdd:cd19120 156 aVNQIEFhPYLYPQQPALLEYCREH----GIVVSaysplSPLtrdAGGPLDPVLEKI 208
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
1-237 |
5.60e-11 |
|
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: 62.27 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 1 MRNLGNTNMKIKRVGFGgipIQRITQDDTNL-----VINELEKQGINFIDSARGYTIS----EEAIGIAIE----GKRDK 67
Cdd:cd19089 1 YRRCGRSGLHLPAISLG---LWHNFGDYTSPeeareLLRTAFDLGITHFDLANNYGPPpgsaEENFGRILKrdlrPYRDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 68 FFLATK---SM---------SRDYdsMKRDVEISLNNFKTDFIDLYQFH----NVKEEEydnlfkdkmAYSALLEAKEQG 131
Cdd:cd19089 78 LVISTKagyGMwpgpygdggSRKY--LLASLDQSLKRMGLDYVDIFYHHrydpDTPLEE---------TMTALADAVRSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 132 KIKHIGITSHNLNTIEKAI----EDG-KFDTIQFPYNIVEGQADE-VFKKAHEKGIGIIVMKPLAGGALDN--------- 196
Cdd:cd19089 147 KALYVGISNYPGAKARRAIallrELGvPLIIHQPRYSLLDRWAEDgLLEVLEEAGIGFIAFSPLAQGLLTDkylngippd 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497581396 197 -------------------------------------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLENLVLDE 237
Cdd:cd19089 227 srraaeskflteealtpekleqlrklnkiaakrgqslAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDFSE 304
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
6-243 |
1.57e-10 |
|
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: 60.67 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 6 NTNMKIKRVGFGgipIQRITQDDT--NLVINELeKQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATKSMSRD-- 78
Cdd:cd19133 4 NNGVEMPILGFG---VFQIPDPEEceRAVLEAI-KAGYRLIDTAAAYG-NEEAVGRAIKKsgiPREELFITTKLWIQDag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 79 YDSMKRDVEISLNNFKTDFIDLYQFHnvkeEEYDNLFkdkMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKF--- 155
Cdd:cd19133 79 YEKAKKAFERSLKRLGLDYLDLYLIH----QPFGDVY---GAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVkpa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 156 -DTIQF-PYNivegQADEVFKKAHEKGIGIIVMKPLAGG---ALDNATL---AIKY-------ILSKDYID--VVIPGME 218
Cdd:cd19133 152 vNQIEThPFN----QQIEAVEFLKKYGVQIEAWGPFAEGrnnLFENPVLteiAEKYgksvaqvILRWLIQRgiVVIPKSV 227
|
250 260
....*....|....*....|....*
gi 497581396 219 SVEQVRQNVAVLEnLVLDEKDNKEI 243
Cdd:cd19133 228 RPERIAENFDIFD-FELSDEDMEAI 251
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
40-233 |
5.41e-10 |
|
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: 59.37 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 40 GINFIDSARGY--TISEEAIGIAIEGK-RDKFFLATKSMSRDYDSMKRDV-----------EISLNNFKTDFIDLYQFHN 105
Cdd:cd19145 46 GVTFLDTSDIYgpNTNEVLLGKALKDGpREKVQLATKFGIHEIGGSGVEVrgdpayvraacEASLKRLDVDYIDLYYQHR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 106 VkeeeyDNLFKDKMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTIQFPYNI----VEgqaDEVFKKAHEKGI 181
Cdd:cd19145 126 I-----DTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAVHPITAVQLEWSLwtrdIE---EEIIPTCRELGI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497581396 182 GIIVMKPLAGGALDNATLAIKyILSKDYIDVVIPGMESvEQVRQNVAVLENL 233
Cdd:cd19145 198 GIVPYSPLGRGFFAGKAKLEE-LLENSDVRKSHPRFQG-ENLEKNKVLYERV 247
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
33-196 |
5.53e-10 |
|
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: 59.11 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 33 INELEKQGINFIDSAR--GYTISEEAIGIAIE---GKRDKFFLATK-----------SMSRDYDSMK----RDVEISLNN 92
Cdd:cd19092 30 IEAALELGITTFDHADiyGGGKCEELFGEALAlnpGLREKIEIQTKcgirlgddprpGRIKHYDTSKehilASVEGSLKR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 93 FKTDFIDLYQFHNVkeeeyDNLFK-DKMAySALLEAKEQGKIKHIGITSHN----------------LNTIE------KA 149
Cdd:cd19092 110 LGTDYLDLLLLHRP-----DPLMDpEEVA-EAFDELVKSGKVRYFGVSNFTpsqiellqsyldqplvTNQIElsllhtEA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497581396 150 IEDGKFDTIQfpynivegqadevfkkahEKGIGIIVMKPLAGGALDN 196
Cdd:cd19092 184 IDDGTLDYCQ------------------LLDITPMAWSPLGGGRLFG 212
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-151 |
7.00e-10 |
|
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: 59.27 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 16 FGGipiqRITQDDTNLVINELEKQGINFIDSARGYTI--SEEAIGIAI-EGKRDKFFLATK---SMSRDY-DSMKRDVEI 88
Cdd:cd19103 25 FGN----HLDEDTLKAVFDKAMAAGLNLWDTAAVYGMgaSEKILGEFLkRYPREDYIISTKftpQIAGQSaDPVADMLEG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497581396 89 SLNNFKTDFIDLYQFHNVKEEEYDNLFkdkmaysaLLEAKEQGKIKHIGITSHNLNTIEKAIE 151
Cdd:cd19103 101 SLARLGTDYIDIYWIHNPADVERWTPE--------LIPLLKSGKVKHVGVSNHNLAEIKRANE 155
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
39-246 |
8.23e-10 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 59.10 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 39 QGINFIDSARGYTI---------SEEAIG--IAIEGKRDKFFLATK--------------SMSRDYDSMKRDVEISLNNF 93
Cdd:PRK10625 42 QGINLIDVAEMYPVpprpetqglTETYIGnwLAKRGSREKLIIASKvsgpsrnndkgirpNQALDRKNIREALHDSLKRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 94 KTDFIDLYQFHNVKEEEydNLFkDKMAYS---------------ALLEAKEQGKIKHIGITSHN-------LNTIEKAiE 151
Cdd:PRK10625 122 QTDYLDLYQVHWPQRPT--NCF-GKLGYSwtdsapavslletldALAEQQRAGKIRYIGVSNETafgvmryLHLAEKH-D 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 152 DGKFDTIQFPYNIV----EGQADEVfkkAHEKGIGIIVMKPLAGGA---------------------------------- 193
Cdd:PRK10625 198 LPRIVTIQNPYSLLnrsfEVGLAEV---SQYEGVELLAYSCLAFGTltgkylngakpagarntlfsrftrysgeqtqkav 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497581396 194 -----------LDNATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLeNLVLDEKDNKEIEEI 246
Cdd:PRK10625 275 aayvdiakrhgLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESL-HLTLSEEVLAEIEAV 337
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
6-250 |
1.22e-09 |
|
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: 58.17 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 6 NTNMKIKRVGFGGIPIqritqDDTNLVINELE---KQGINFIDSARGYTiSEEAIGIAI-EG--KRDKFFLATKSMSRD- 78
Cdd:cd19157 5 NNGVKMPWLGLGVFKV-----EEGSEVVNAVKtalKNGYRSIDTAAIYG-NEEGVGKGIkESgiPREELFITSKVWNADq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 79 -YDSMKRDVEISLNNFKTDFIDLYQFHNVKEEEYdnlfkdKMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKfdt 157
Cdd:cd19157 79 gYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKY------KETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 158 IQFPYNIVEGQ----ADEVFKKAHEKGIGIIVMKPL-AGGALDNATL---AIKY-------ILSKDYID--VVIPGMESV 220
Cdd:cd19157 150 IVPMVNQVEFHprltQKELRDYCKKQGIQLEAWSPLmQGQLLDNPVLkeiAEKYnksvaqvILRWDLQNgvVTIPKSIKE 229
|
250 260 270
....*....|....*....|....*....|
gi 497581396 221 EQVRQNVAVLEnLVLDEKDNKEIEEIRNSL 250
Cdd:cd19157 230 HRIIENADVFD-FELSQEDMDKIDALNENL 258
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-239 |
1.43e-09 |
|
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: 57.67 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 10 KIKRVGFGGIPIQriTQDDTNLVINELEkQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATKSMSRD--YDSMKR 84
Cdd:cd19132 6 QIPAIGFGTYPLK--GDEGVEAVVAALQ-AGYRLLDTAFNYE-NEGAVGEAVRRsgvPREELFVTTKLPGRHhgYEEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 85 DVEISLNNFKTDFIDLYQFH--NVKEEEYDNlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEdgkfDTIQFP- 161
Cdd:cd19132 82 TIEESLYRLGLDYVDLYLIHwpNPSRDLYVE------AWQALIEAREEGLVRSIGVSNFLPEHLDRLID----ETGVTPa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 162 YNIVE---GQADEVFKKAHEKgIGIIVM--KPLAGGA--LDNATL-AIKYILSKDYIDVV-----------IPGMESVEQ 222
Cdd:cd19132 152 VNQIElhpYFPQAEQRAYHRE-HGIVTQswSPLGRGSglLDEPVIkAIAEKHGKTPAQVVlrwhvqlgvvpIPKSANPER 230
|
250
....*....|....*..
gi 497581396 223 VRQNVAVLeNLVLDEKD 239
Cdd:cd19132 231 QRENLAIF-DFELSDED 246
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
9-243 |
2.04e-09 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 57.34 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 9 MKIKRVGFGGIPIQRITQDDTnlVINELEkQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATKSMSRDY--DSMK 83
Cdd:PRK11172 1 MSIPAFGLGTFRLKDQVVIDS--VKTALE-LGYRAIDTAQIYD-NEAAVGQAIAEsgvPRDELFITTKIWIDNLakDKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 84 RDVEISLNNFKTDFIDLYQFH------NVKEEEYdnlfkdkMAysALLEAKEQGKIKHIGITSHNLNTIEKAIE---DGK 154
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHwpspndEVSVEEF-------MQ--ALLEAKKQGLTREIGISNFTIALMKQAIAavgAEN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 155 FDTIQF---PYNivegQADEVFKKAHEKGIGIIVMKPLAGG------------ALDNAT---LAIKYILSKDYidVVIPG 216
Cdd:PRK11172 148 IATNQIelsPYL----QNRKVVAFAKEHGIHVTSYMTLAYGkvlkdpviariaAKHNATpaqVILAWAMQLGY--SVIPS 221
|
250 260
....*....|....*....|....*..
gi 497581396 217 MESVEQVRQNVAVLEnLVLDEKDNKEI 243
Cdd:PRK11172 222 STKRENLASNLLAQD-LQLDAEDMAAI 247
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
32-229 |
3.10e-09 |
|
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: 56.95 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 32 VINELEKQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATKSMSRDY--DSMKRDVEISLNNFKTDFIDLYQFH-- 104
Cdd:cd19135 31 VVYALKECGYRHIDTAKRYG-CEELLGKAIKEsgvPREDLFLTTKLWPSDYgyESTKQAFEASLKRLGVDYLDLYLLHwp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 105 -------NVKEEEYDnlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGkfdTIQFPYNIVE----GQADEVF 173
Cdd:cd19135 110 dcpssgkNVKETRAE-------TWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDC---SVVPHVNQVEfhpfQNPVELI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497581396 174 KKAHEKGIGIIVMKPLAGG-ALDNAT---LAIKY------ILSKDYID---VVIPGMESVEQVRQNVAV 229
Cdd:cd19135 180 EYCRDNNIVFEGYCPLAKGkALEEPTvteLAKKYqktpaqILIRWSIQngvVTIPKSTKEERIKENCQV 248
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
254-318 |
1.05e-08 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 50.92 E-value: 1.05e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497581396 254 FCRRCEYCMP-CAVGINIPLsflcEGYYTRYGLKEWAKEKYEVMDVkPTECIDCGLCESRCPYELP 318
Cdd:pfam13534 1 RCIQCGCCVDeCPRYLLNGD----EPKKLMRAAYLGDLEELQANKV-ANLCSECGLCEYACPMGLD 61
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
40-146 |
1.49e-08 |
|
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: 54.98 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 40 GINFIDSARGYTISEEAIGIAI-----EGKRDKFFLATKSmSR------DY--DSMKRDVEISLNNFKTDFIDLYQFHNV 106
Cdd:cd19164 47 GIRAFDTSPYYGPSEIILGRALkalrdEFPRDTYFIITKV-GRygpddfDYspEWIRASVERSLRRLHTDYLDLVYLHDV 125
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 497581396 107 ---KEEEYDNlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTI 146
Cdd:cd19164 126 efvADEEVLE------ALKELFKLKDEGKIRNVGISGYPLPVL 162
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-149 |
2.33e-08 |
|
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: 54.65 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 39 QGINFIDSARGYTI---------SEEAIG--IAIEGKRDKFFLATK---------SMSRDYDSMKRD-----VEISLNNF 93
Cdd:cd19752 29 AGGNFLDTANNYAFwteggvggeSERLIGrwLKDRGNRDDVVIATKvgagprdpdGGPESPEGLSAEtieqeIDKSLRRL 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 497581396 94 KTDFIDLYQFHnVKEEEYDnlFKDKMAysALLEAKEQGKIKHIGITSHNLNTIEKA 149
Cdd:cd19752 109 GTDYIDLYYAH-VDDRDTP--LEETLE--AFNELVKAGKVRAIGASNFAAWRLERA 159
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
6-200 |
5.06e-08 |
|
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: 53.21 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 6 NTNMKIKRVGFGGIPIQriTQDDTNLVINELEKQGINFIDSARGYTiSEEAIGIAIEGK---RDKFFLATKSMSRD--YD 80
Cdd:cd19126 4 NNGTRMPWLGLGVFQTP--DGDETERAVQTALENGYRSIDTAAIYK-NEEGVGEAIRESgvpREELFVTTKLWNDDqrAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 81 SMKRDVEISLNNFKTDFIDLYQFH-NVKEEeydnlFKDkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKF---- 155
Cdd:cd19126 81 RTEDAFQESLDRLGLDYVDLYLIHwPGKDK-----FID--TWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVvpav 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497581396 156 DTIQF-PYNivegQADEVFKKAHEKGIGIIVMKPLA-GGALDNATLA 200
Cdd:cd19126 154 NQVEFhPYL----TQKELRGYCKSKGIVVEAWSPLGqGGLLSNPVLA 196
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-246 |
9.83e-08 |
|
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: 52.60 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 28 DTNLVINELEK---QGINFIDSARGYTISEEAIGIAIEGKRDKFFLA------TK--------SMSRDYdsMKRDVEISL 90
Cdd:cd19101 21 DEDAAVRAMAAyvdAGLTTFDCADIYGPAEELIGEFRKRLRRERDAAddvqihTKwvpdpgelTMTRAY--VEAAIDRSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 91 NNFKTDFIDLYQFH----NVKEeeydnlFKDKMAYsaLLEAKEQGKIKHIGITshNLNTI--EKAIEDG-KFDTIQFPYN 163
Cdd:cd19101 99 KRLGVDRLDLVQFHwwdySDPG------YLDAAKH--LAELQEEGKIRHLGLT--NFDTErlREILDAGvPIVSNQVQYS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 164 IVE-----GQADevFKKAHekGIGIIVMKPLAGGALDN------------------------------------------ 196
Cdd:cd19101 169 LLDrrpenGMAA--LCEDH--GIKLLAYGTLAGGLLSEkylgvpeptgpaletrslqkyklmidewggwdlfqellrtlk 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 197 ----------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:cd19101 245 aiadkhgvsiANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFS-FRLDDEDRAAIDAV 303
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
6-151 |
2.27e-07 |
|
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: 51.25 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 6 NTNMKIKRVGFGgipIQRITQDDTNLVINELEKQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATKSMSRDY--D 80
Cdd:cd19127 4 NNGVEMPALGLG---VFQTPPEETADAVATALADGYRLIDTAAAYG-NEREVGEGIRRsgvDRSDIFVTTKLWISDYgyD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497581396 81 SMKRDVEISLNNFKTDFIDLYQFHNVKEEEYDNLFKdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIE 151
Cdd:cd19127 80 KALRGFDASLRRLGLDYVDLYLLHWPVPNDFDRTIQ---AYKALEKLLAEGRVRAIGVSNFTPEHLERLID 147
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
18-152 |
2.55e-07 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 51.23 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 18 GIPIQRITQDDTNLVINELEKQGINFIDSARGYTiSEEAIGIAIEGK---RDKFFLATKSMSRDYDSMKRDVEISLNNFK 94
Cdd:PRK11565 19 GLGVWQASNEEVITAIHKALEVGYRSIDTAAIYK-NEEGVGKALKEAsvaREELFITTKLWNDDHKRPREALEESLKKLQ 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 497581396 95 TDFIDLYQFHNVKEEEydNLFKDkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIED 152
Cdd:PRK11565 98 LDYVDLYLMHWPVPAI--DHYVE--AWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDE 151
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
38-154 |
4.36e-07 |
|
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: 50.32 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 38 KQGINFIDSARGYTiSEEAIGIAIEG-------KRDKFFLATKSMSRD--YDSMKRDVEISLNNFKTDFIDLYQFH---- 104
Cdd:cd19136 26 KAGYRLIDTASVYR-NEADIGKALRDllpkyglSREDIFITSKLAPKDqgYEKARAACLGSLERLGTDYLDLYLIHwpgv 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 497581396 105 -NVKEEEYDNLFKDKMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGK 154
Cdd:cd19136 105 qGLKPSDPRNAELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCE 155
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
13-244 |
5.94e-07 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 50.32 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 13 RVGFG-------GIPIqriTQDDTNLVINELEKQGINFIDSARGYTISEEAIGIAIEGK--------RDKFFL------- 70
Cdd:cd19077 7 PIGLGlmgltwrPNPT---PDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANLKLLARffrkypeyADKVVLsvkggld 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 71 -ATKSMSRDYDSMKRDVEISLNNFK-TDFIDLYQF----HNVKEEEYDnlfkdkmaySALLEAKEQGKIKHIGITSHNLN 144
Cdd:cd19077 84 pDTLRPDGSPEAVRKSIENILRALGgTKKIDIFEParvdPNVPIEETI---------KALKELVKEGKIRGIGLSEVSAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 145 TIEKAIEDGKFDTIQ-----FPYNIVEgqaDEVFKKAHEKGIGIIVMKPLAGGAL------------------------D 195
Cdd:cd19077 155 TIRRAHAVHPIAAVEveyslFSREIEE---NGVLETCAELGIPIIAYSPLGRGLLtgriksladipegdfrrhldrfngE 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497581396 196 N----------------------ATLAIKYILSKDYIDVV-IPGMESVEQVRQNVAVLeNLVLDEKDNKEIE 244
Cdd:cd19077 232 NfeknlklvdalqelaekkgctpAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAA-NVELTDEELKEIN 302
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
18-231 |
6.96e-07 |
|
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: 49.85 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 18 GIPIQRITQDDTNLVINELEKQGINFIDSARGYTiSEEAIGIAIEGK---RDKFFLATKSMSRD--YDSMKRDVEISLNN 92
Cdd:cd19134 15 GLGVGELSDDEAERSVSAALEAGYRLIDTAAAYG-NEAAVGRAIAASgipRGELFVTTKLATPDqgFTASQAACRASLER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 93 FKTDFIDLYQFH--NVKEEEYDNlfkdkmAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTI--QFPYNIVEGQ 168
Cdd:cd19134 94 LGLDYVDLYLIHwpAGREGKYVD------SWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAvnQIELHPLLNQ 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497581396 169 ADevFKKAHEK-GIGIIVMKPLA-GGALDNAT---LAIKYILSKDYI---------DVVIPGMESVEQVRQNVAVLE 231
Cdd:cd19134 168 AE--LRKVNAQhGIVTQAYSPLGvGRLLDNPAvtaIAAAHGRTPAQVllrwslqlgNVVISRSSNPERIASNLDVFD 242
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
25-246 |
1.30e-06 |
|
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: 49.09 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 25 TQDDTNLVINELEKQGINFIDSARGYTI--SEEAIGIAIEGKRDkFFLATKSMSR-----DYDSMKRDVEISLNNFKTDF 97
Cdd:cd19075 18 TAEAAAELLDAFLERGHTEIDTARVYPDgtSEELLGELGLGERG-FKIDTKANPGvggglSPENVRKQLETSLKRLKVDK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 98 IDLYQFH------NVKE--EEYDNLFKdkmaysalleakeQGKIKHIGITSHNLNTIEKAIEDGKFD-----TI-QFPYN 163
Cdd:cd19075 97 VDVFYLHapdrstPLEEtlAAIDELYK-------------EGKFKEFGLSNYSAWEVAEIVEICKENgwvlpTVyQGMYN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 164 -IVEGQADEVFKKAHEKGIGIIVMKPLAGGAL------------------------------------------------ 194
Cdd:cd19075 164 aITRQVETELFPCLRKLGIRFYAYSPLAGGFLtgkykysedkagggrfdpnnalgklyrdrywkpsyfealekveeaaek 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 195 ---DNATLAIKYI-----LSKDYIDVVIPGMESVEQVRQNVAVLENLVLDEKDNKEIEEI 246
Cdd:cd19075 244 egiSLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEA 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
38-249 |
1.42e-06 |
|
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: 49.03 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 38 KQGINFIDSARGYTiSEEAIGIAI-----EG--KRDKFFLATK--SMSRDYDSMKRDVEISLNNFKTDFIDLYQFH---- 104
Cdd:cd19111 28 FVGYRHIDTALSYQ-NEKAIGEALkwwlkNGklKREEVFITTKlpPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcg 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 105 -NVK--EEEYDNLFKDKMAYSALLEAK-EQGKIKHIGITSHNLNTIEKAIEDGKFdtiqFPYNI-VEG----QADEVFKK 175
Cdd:cd19111 107 fVNKkdKGERELASSDVTSVWRAMEALvSEGKVKSIGLSNFNPRQINKILAYAKV----KPSNLqLEChaylQQRELRKF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 176 AHEKGIGIIVMKPLAGGALDNAT--------------LAI-------------KYILSKDYIdvVIPGMESVEQVRQNVA 228
Cdd:cd19111 183 CNKKNIVVTAYAPLGSPGRANQSlwpdqpdlledptvLAIakeldktpaqvllRFVLQRGTG--VLPKSTNKERIEENFE 260
|
250 260
....*....|....*....|.
gi 497581396 229 VLEnLVLDEKDNKEIEEIRNS 249
Cdd:cd19111 261 VFD-FELTEEHFKKLKTLDRN 280
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
6-254 |
3.70e-06 |
|
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: 47.88 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 6 NTNMKIKRVGFGgiPIQRITQDDTNLVINELeKQGINFIDSARGYTiSEEAIGIAIEGK---RDKFFLATKSmsrdYDSM 82
Cdd:cd19117 9 NTGAEIPAVGLG--TWQSKPNEVAKAVEAAL-KAGYRHIDTAAIYG-NEEEVGQGIKDSgvpREEIFITTKL----WCTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 83 KRDVEI----SLNNFKTDFIDLYQFH-----NVKEEEYDNLFKDKMA-----------YSALLEAKEQGKIKHIGITSHN 142
Cdd:cd19117 81 HRRVEEaldqSLKKLGLDYVDLYLMHwpvplDPDGNDFLFKKDDGTKdhepdwdfiktWELMQKLPATGKVKAIGVSNFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 143 LNTIEKAIEDGKFDTIQ-------FPYNivegQADEVFKKAHEKGIGIIVMKPL--AGGAL---------------DNAT 198
Cdd:cd19117 161 IKNLEKLLASPSAKIVPavnqielHPLL----PQPKLVDFCKSKGIHATAYSPLgsTNAPLlkepviikiakkhgkTPAQ 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 497581396 199 LAIKYILSKDYidVVIPGMESVEQVRQNVAVLEnlvLDEKDNKEIeeirNSLGKKF 254
Cdd:cd19117 237 VIISWGLQRGY--SVLPKSVTPSRIESNFKLFT---LSDEEFKEI----DELHKEY 283
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
39-104 |
5.16e-06 |
|
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: 47.42 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 39 QGINFIDSARGYT--ISEEAIG--IAIEGKRDKFFLATK-SMS-RDYD--------------SMKRDVEISLNNFKTDFI 98
Cdd:cd19146 47 QGGNFIDTANNYQgeESERWVGewMASRGNRDEMVLATKyTTGyRRGGpikiksnyqgnhakSLRLSVEASLKKLQTSYI 126
|
....*.
gi 497581396 99 DLYQFH 104
Cdd:cd19146 127 DILYVH 132
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
3-246 |
6.90e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 46.89 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 3 NLGNTNmkIKRVGFG----------GIPIQRitqDDTNLVINELEKQGINFIDSARGYT--ISEEAIGIAIEGKRDKFFL 70
Cdd:PRK10376 11 TLGGRS--VNRLGYGamqlagpgvfGPPKDR---DAAIAVLREAVALGVNHIDTSDFYGphVTNQLIREALHPYPDDLTI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 71 ATK-SMSRDYD----------SMKRDVEISLNNFKTDFIDLYQF------HNVKE---EEydnlfkdkmAYSALLEAKEQ 130
Cdd:PRK10376 86 VTKvGARRGEDgswlpafspaELRRAVHDNLRNLGLDVLDVVNLrlmgdgHGPAEgsiEE---------PLTVLAELQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 131 GKIKHIGITSHNLNTIEKAIEDGKFDTIQFPYNIVEGQADEVFKKAHEKGIGIIVMKPLAG------GALD------NAT 198
Cdd:PRK10376 157 GLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNLAHRADDALIDALARDGIAYVPFFPLGGftplqsSTLSdvaaslGAT 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 497581396 199 ---LAIKYILSKDYIDVVIPGMESVEQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:PRK10376 237 pmqVALAWLLQRSPNILLIPGTSSVAHLRENLAAAE-LVLSEEVLAELDGI 286
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
65-245 |
9.85e-06 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 46.91 E-value: 9.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 65 RDKFFLATKS------------MSRDYdsMKRDVEISLNNFKTDFIDLYQFHNVKEeeydNLFKDKMAySALLEAKEQGK 132
Cdd:PRK09912 89 RDELIISTKAgydmwpgpygsgGSRKY--LLASLDQSLKRMGLEYVDIFYSHRVDE----NTPMEETA-SALAHAVQSGK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 133 IKHIGITSHNLNTIEKAIE---DGKFDTI--QFPYNIVEGQADE--VFKKAHEKGIGIIVMKPLAGGALDN--------- 196
Cdd:PRK09912 162 ALYVGISSYSPERTQKMVEllrEWKIPLLihQPSYNLLNRWVDKsgLLDTLQNNGVGCIAFTPLAQGLLTGkylngipqd 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 197 ----------------------------------------ATLAIKYILSKDYIDVVIPGMESVEQVRQNVAVLENLVLD 236
Cdd:PRK09912 242 srmhregnkvrgltpkmlteanlnslrllnemaqqrgqsmAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLTFS 321
|
....*....
gi 497581396 237 EKDNKEIEE 245
Cdd:PRK09912 322 TEELAQIDQ 330
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-246 |
1.22e-05 |
|
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: 45.97 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 4 LGNTNMkIKRVGFGGIPIQritqdDTNLVINELE---KQGINFIDSARGYTiSEEAIGIAIEG---KRDKFFLATKSMSR 77
Cdd:cd19156 3 LANGVE-MPRLGLGVWRVQ-----DGAEAENAVKwaiEAGYRHIDTAAIYK-NEEGVGQGIREsgvPREEVFVTTKLWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 78 D--YDSMKRDVEISLNNFKTDFIDLYQFHNVKEEEYdnlfkdKMAYSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKF 155
Cdd:cd19156 76 DqgYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKF------KDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 156 ----DTIQF-PYNivegQADEVFKKAHEKGIGIIVMKPLAGGA-LDNATLA--------------IKYILSKDYIdvVIP 215
Cdd:cd19156 150 apmvNQIELhPLL----TQEPLRKFCKEKNIAVEAWSPLGQGKlLSNPVLKaigkkygksaaqviIRWDIQHGII--TIP 223
|
250 260 270
....*....|....*....|....*....|.
gi 497581396 216 GMESVEQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:cd19156 224 KSVHEERIQENFDVFD-FELTAEEIRQIDGL 253
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
38-154 |
1.57e-05 |
|
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: 45.87 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 38 KQGINFIDSARGYTiSEEAIGIAIE-------GKRDKFFLATK-SMSRDY-DSMKRDVEISLNNFKTDFIDLYQFH---N 105
Cdd:cd19154 36 KAGYRLIDTAFLYQ-NEEAIGEALAelleegvVKREDLFITTKlWTHEHApEDVEEALRESLKKLQLEYVDLYLIHapaA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 106 VKEEE-------YDNLFKDKMA----YSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGK 154
Cdd:cd19154 115 FKDDEgesgtmeNGMSIHDAVDvedvWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNAR 174
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
2-246 |
2.90e-05 |
|
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: 45.28 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFGGIpiqrIT---QDDTNLVINELEK---QGINFIDSARGYT--ISEEAIGIAI-EG--KRDKFFL 70
Cdd:cd19143 4 RRLGRSGLKVSALSFGSW----VTfgnQVDVDEAKECMKAaydAGVNFFDNAEVYAngQSEEIMGQAIkELgwPRSDYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 71 ATK-------------SMSRDY--DSMKRdveiSLNNFKTDFIDLYQFH----NVKEEE----YDNLFKDKMAY------ 121
Cdd:cd19143 80 STKifwggggpppndrGLSRKHivEGTKA----SLKRLQLDYVDLVFCHrpdpATPIEEtvraMNDLIDQGKAFywgtse 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 122 -SAlleakEQgkIKH-IGItSHNLNTIEKAIEdgkfdtiQFPYNI-----VEGQADEVFKKAhekGIGIIVMKPLAGG-- 192
Cdd:cd19143 156 wSA-----QQ--IEEaHEI-ADRLGLIPPVME-------QPQYNLfhrerVEVEYAPLYEKY---GLGTTTWSPLASGll 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 193 --------------ALDN---------------------------------ATLAIKYILSKDYIDVVIPGMESVEQVRQ 225
Cdd:cd19143 218 tgkynngipegsrlALPGyewlkdrkeelgqekiekvrklkpiaeelgcslAQLAIAWCLKNPNVSTVITGATKVEQLEE 297
|
330 340
....*....|....*....|..
gi 497581396 226 NVAVLENL-VLDEKDNKEIEEI 246
Cdd:cd19143 298 NLKALEVLpKLTPEVMEKIEAI 319
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
40-139 |
3.18e-05 |
|
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: 45.20 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 40 GINFIDSARGYT--ISEEAIG--IAIEGKRDKFFLATKsMSRDYD------------------SMKRDVEISLNNFKTDF 97
Cdd:cd19147 47 GGNFIDTANNYQdeQSETWIGewMKSRKNRDQIVIATK-FTTDYKayevgkgkavnycgnhkrSLHVSVRDSLRKLQTDW 125
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 497581396 98 IDLYQFHnvkEEEYDNLFKDKMaySALLEAKEQGKIKHIGIT 139
Cdd:cd19147 126 IDILYVH---WWDYTTSIEEVM--DSLHILVQQGKVLYLGVS 162
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-247 |
3.21e-05 |
|
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: 44.86 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 10 KIKRVGFGgipIQRITQDDTNLVINELEKQGINFIDSARGYTiSEEAIGIAI-----EG--KRDKFFLATKSMSRDY--D 80
Cdd:cd19114 3 KMPLVGFG---TAKIKANETEEVIYNAIKVGYRLIDGALLYG-NEAEVGRGIrkaiqEGlvKREDLFIVTKLWNNFHgkD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 81 SMKRDVEISLNNFKTDFIDLYQFHNVKEEEYDN-------LFKDKMAYSALLEAK-------------EQGKIKHIGITS 140
Cdd:cd19114 79 HVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaenypfLWKDKELKKFPLEQSpmqecwremeklvDAGLVRNIGIAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 141 HNLNTIEKAIEDGKF--DTIQF---PYNivegQADEVFKKAHEKGIGIIVMKPLAGGALD-----NATLA-------IKY 203
Cdd:cd19114 159 FNVQLILDLLTYAKIkpAVLQIehhPYL----QQKRLIDWAKKQGIQITAYSSFGNAVYTkvtkhLKHFTnllehpvVKK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 497581396 204 ILSKDYID--------------VVIPGMESVEQVRQNVAVLeNLVLDEKDNKEIEEIR 247
Cdd:cd19114 235 LADKHKRDtgqvllrwavqrniTVIPKSVNVERMKTNLDIT-SYKLDEEDMEALYELE 291
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
38-254 |
4.01e-05 |
|
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: 44.80 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 38 KQGINFIDSARGYTiSEEAIGIAI-------EGKRDKFFLATKSMSRDYDSMKRDVEISLNNFKTDFIDLYQFH------ 104
Cdd:cd19119 38 KEGYRHIDTAYAYE-TEDFVGEAIkraiddgSIKREELFITTKVWPTFYDEVERSLDESLKALGLDYVDLLLVHwpvcfe 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 105 -------NVKEEEYDNLFKDKMA-------YSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFDTI--QFPYNIVEGQ 168
Cdd:cd19119 117 kdsddsgKPFTPVNDDGKTRYAAsgdhittYKQLEKIYLDGRAKAIGVSNYSIVYLERLIKECKVVPAvnQVELHPHLPQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 169 ADEV-FKKAHekGIGIIVMKPLAGG---ALDN---ATLAIKYILSKDYI---------DVVIPGMESVEQVRQNvavLEN 232
Cdd:cd19119 197 MDLRdFCFKH--GILVTAYSPLGSHgapNLKNplvKKIAEKYNVSTGDIlisyhvrqgVIVLPKSLKPVRIVSN---GKI 271
|
250 260
....*....|....*....|..
gi 497581396 233 LVLDEKDNKEIEEIRNSLGKKF 254
Cdd:cd19119 272 VSLTKEDLQKLDDIGEKYPVRF 293
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
255-314 |
5.88e-05 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 40.31 E-value: 5.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 255 CRRCEYCMpcAVginiplsflCEGYYTRYGLKEWAKEKYEVmDVKPTECIDCGLCESRCP 314
Cdd:pfam13237 9 CIGCGRCT--AA---------CPAGLTRVGAIVERLEGEAV-RIGVWKCIGCGACVEACP 56
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-139 |
6.45e-05 |
|
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: 43.97 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 6 NTNMKIKRVGFGGIPIQRITQDDTnlvINELEKQGINFIDSARGYTiSEEAIGIAI-----EG--KRDKFFLATKSMS-- 76
Cdd:cd19113 6 NSGYKMPSVGFGCWKLDNATAADQ---IYQAIKAGYRLFDGAEDYG-NEKEVGEGVnraidEGlvKREELFLTSKLWNnf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 77 RDYDSMKRDVEISLNNFKTDFIDLYQFH---NVK----EEEYDNLF----KDKMAYS---------ALLEAKEQGKIKHI 136
Cdd:cd19113 82 HDPKNVETALNKTLSDLKLDYVDLFLIHfpiAFKfvpiEEKYPPGFycgdGDNFVYEdvpildtwkALEKLVDAGKIKSI 161
|
...
gi 497581396 137 GIT 139
Cdd:cd19113 162 GVS 164
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
255-317 |
1.75e-04 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 39.22 E-value: 1.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497581396 255 CRRCEYCMP-CAVGINIPLSFLcegYYTRYGLKEWAKEKYEVMDVKPT--ECIDCGLCESRCPYEL 317
Cdd:pfam13183 2 CIRCGACLAaCPVYLVTGGRFP---GDPRGGAAALLGRLEALEGLAEGlwLCTLCGACTEVCPVGI 64
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
287-316 |
2.20e-04 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 38.92 E-value: 2.20e-04
10 20 30
....*....|....*....|....*....|
gi 497581396 287 EWAKEKYEVMDVKPTECIDCGLCESRCPYE 316
Cdd:COG1146 26 ELDEEGKKALVINPEECIGCGACELVCPVG 55
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
255-315 |
3.80e-04 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 37.89 E-value: 3.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497581396 255 CRRCEYCMP-CAVGIniplsflcegyytRYGLKEWAKEKYEVMDVKPTECIDCGLCESRCPY 315
Cdd:pfam12838 1 CIGCGACVAaCPVGA-------------ITLDEVGEKKGTKTVVIDPERCVGCGACVAVCPT 49
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
6-154 |
3.99e-04 |
|
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: 41.45 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 6 NTNMKIKRVGFGGIPIQRITQDDTNLVINELeKQGINFIDSArGYTISEEAIGIAIEG--------KRDKFFLATKSMSR 77
Cdd:cd19122 4 NNGVKIPAVGFGTFANEGAKGETYAAVTKAL-DVGYRHLDCA-WFYLNEDEVGDAVRDflkenpsvKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 78 --DYDSMKRDVEISLNNFKTDFIDLYQFH--NVKEEEYDNLFK----------------DKMAYSALLEAKEQGKIKHIG 137
Cdd:cd19122 82 lhEPEDVKWSIDNSLKNLKLDYIDLFLVHwpIAAEKNDQRSPKlgpdgkyvilkdltenPEPTWRAMEEIYESGKAKAIG 161
|
170
....*....|....*..
gi 497581396 138 ITSHNLNTIEKAIEDGK 154
Cdd:cd19122 162 VSNWTIPGLKKLLSFAK 178
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
40-197 |
5.74e-04 |
|
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: 40.97 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 40 GINFIDSARGYTiSEEAIGIAIEG-------KRDKFFLATK--SMSRDYDSMKRDVEISLNNFKTDFIDLYQFH---NVK 107
Cdd:cd19155 38 GYRHIDTAYVYR-NEAAIGNVLKKwidsgkvKREELFIVTKlpPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHfpvGSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 108 EEEYDNLFKD-----KMAYS--------ALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKFD--TIQFPYNIVEGQADEV 172
Cdd:cd19155 117 SKEDDSGKLDptgehKQDYTtdlldiwkAMEAQVDQGLTRSIGLSNFNREQMARILKNARIKpaNLQVELHVYLQQKDLV 196
|
170 180
....*....|....*....|....*.
gi 497581396 173 -FKKAHekGIGIIVMKPLAGGALDNA 197
Cdd:cd19155 197 dFCSTH--SITVTAYAPLGSPGAAHF 220
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
30-246 |
1.11e-03 |
|
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: 40.16 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 30 NLVINELeKQGINFIDSARGYTiSEEAIGIAI-----EG--KRDKFFLATKSMSRDYDSMKRDVEISLNNFKTDFIDLYQ 102
Cdd:cd19112 28 ELILNAI-KIGYRHFDCAADYK-NEKEVGEALaeafkTGlvKREDLFITTKLWNSDHGHVIEACKDSLKKLQLDYLDLYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 103 FH---NVKEEEYDN----LFKDKMA-----------YSALLEAKEQGKIKHIGITSHNLNTIEKAIEDGKfdtIQFPYNI 164
Cdd:cd19112 106 VHfpvATKHTGVGTtgsaLGEDGVLdidvtislettWHAMEKLVSAGLVRSIGISNYDIFLTRDCLAYSK---IKPAVNQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 165 VEG----QADEVFKKAHEKGIGIIVMKPLAGGA-----------LDNATL---AIKYILSKDYI---------DVVIPGM 217
Cdd:cd19112 183 IEThpyfQRDSLVKFCQKHGISVTAHTPLGGAAanaewfgsvspLDDPVLkdlAKKYGKSAAQIvlrwgiqrnTAVIPKS 262
|
250 260
....*....|....*....|....*....
gi 497581396 218 ESVEQVRQNVAVLEnLVLDEKDNKEIEEI 246
Cdd:cd19112 263 SKPERLKENIDVFD-FQLSKEDMKLIKSL 290
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
38-153 |
1.69e-03 |
|
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: 39.70 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 38 KQGINFIDSARGYTiSEEAIGIAIEG--------KRDKFFLATKSMSRDY--DSMKRDVEISLNNFKTDFIDLYQFH--- 104
Cdd:cd19118 31 KAGYRHLDLAKVYQ-NQHEVGQALKEllkeepgvKREDLFITSKLWNNSHrpEYVEPALDDTLKELGLDYLDLYLIHwpv 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497581396 105 --------NVKEEEYDNlfKDKMA----------YSALLEAKEQGKIKHIGITSHNLNTIEKAIEDG 153
Cdd:cd19118 110 afkptgdlNPLTAVPTN--GGEVDldlsvslvdtWKAMVELKKTGKVKSIGVSNFSIDHLQAIIEET 174
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
2-104 |
3.69e-03 |
|
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: 38.60 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 2 RNLGNTNMKIKRVGFGGIPI--QRITQDDTNLVINELEKQGINFIDSARGYT--ISEEAIGIAIEGK---RDKFFLATK- 73
Cdd:cd19142 4 RNLGKSGLRVSNVGLGTWSTfsTAISEEQAEEIVTLAYENGINYFDTSDAFTsgQAETELGRILKKKgwkRSSYIVSTKi 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 497581396 74 ---------SMSRDYdsMKRDVEISLNNFKTDFIDLYQFH 104
Cdd:cd19142 84 ywsygseerGLSRKH--IIESVRASLRRLQLDYIDIVIIH 121
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
298-322 |
4.87e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 38.12 E-value: 4.87e-03
10 20
....*....|....*....|....*
gi 497581396 298 VKPTECIDCGLCESRCPYELPIREM 322
Cdd:COG0348 207 YDRGDCIDCGLCVKVCPMGIDIRKG 231
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
208-330 |
8.75e-03 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 37.77 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497581396 208 DYIDVVIPG--MESVEQVRQnVAVLENLVLDEKDNKEIEEIRNSLGKKFCRRCEYCMPCAvginiplsFLC-EGYYTRYG 284
Cdd:cd01916 316 DLVSGKIPGvlILDPEKVGE-VAVEVAMAVKPKRKGEKKLPTDEEFQELAAKCTDCGWCT--------RACpNSLRIKEA 386
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 497581396 285 LKEWAKEKYEVMDVKPTECIDCGLCESRCPYELPIREMLKTVVEKL 330
Cdd:cd01916 387 MEAAKEGDFSGLADLFDQCVGCGRCEQECPKEIPIINMIEKAARER 432
|
|
| |
