|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-298 |
7.13e-180 |
|
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: 498.01 E-value: 7.13e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 14 SQMGLGCLYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYSHWIsDQTQGGESEKMIGKWLKERNNREDVIIASKVGFPY 93
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWT-EGGVGGESERLIGRWLKDRGNRDDVVIATKVGAGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 94 PG------TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERA 167
Cdd:cd19752 80 RDpdggpeSPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 168 RQIAKQNHWQSYSAIQQRYSYLRPKSGWDFGDQVAANQDLFEFVEDTG-ISLVAYSPLLQGAYTNPNKEFKEQYQGPDTD 246
Cdd:cd19752 160 RQIARQQGWAEFSAIQQRHSYLRPRPGADFGVQRIVTDELLDYASSRPdLTLLAYSPLLSGAYTRPDRPLPEQYDGPDSD 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1001929468 247 KRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLE 298
Cdd:cd19752 240 ARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-310 |
3.68e-105 |
|
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: 309.53 E-value: 3.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 5 QLGKTGLQVSQMGLGCLYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYSHWIsDQTQGGESEKMIGKWLKERNNREDVI 84
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAWV-PGNAGGESETIIGRWLKSRGKRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 85 IASKVGFPYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRL 164
Cdd:cd19081 80 IATKVGFPMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 165 ERARQIAKQNHWQSYSAIQQRYSYLRPKSgwdfgdqvaANQDLFEFVEDTGISLVAYSPL----LQGAYTNPNK------ 234
Cdd:cd19081 160 QEALELSRQHGLPRYVSLQPEYNLVDRES---------FEGELLPLCREEGIGVIPYSPLaggfLTGKYRSEADlpgstr 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001929468 235 --EFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELSEDMLRAMT 310
Cdd:cd19081 231 rgEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-312 |
3.42e-101 |
|
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: 299.40 E-value: 3.42e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGCLYFGA---RDSKEKSFRRMDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKER 77
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGP--------GRSEELLGEALKGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 78 NnREDVIIASKVGFPYPG--TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIG 155
Cdd:COG0667 73 P-RDDVVIATKVGRRMGPgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 156 ASNFKAWRLERARQIAKqnHWQSYSAIQQRYSYLRPKsgwdfgdqvaANQDLFEFVEDTGISLVAYSPLLQG----AYTN 231
Cdd:COG0667 152 VSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRS----------AEEELLPAARELGVGVLAYSPLAGGlltgKYRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 232 PNK---------EFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELS 302
Cdd:COG0667 220 GATfpegdraatNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELS 299
|
330
....*....|
gi 1001929468 303 EDMLRAMTEA 312
Cdd:COG0667 300 AEDLAALDAA 309
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-295 |
3.15e-98 |
|
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: 289.03 E-value: 3.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 14 SQMGLGCLYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYSHWisdqtqggESEKMIGKWLKERNNREDVIIASKVGFPY 93
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDG--------RSERLLGRWLKGRGNRDDVVIATKGGHPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 94 PGT--EYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIA 171
Cdd:cd06660 73 GGDpsRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 172 KQNHWQSYSAIQQRYSYLRPKsgwdfgdqvAANQDLFEFVEDTGISLVAYSPLLQGAytnpnkefkeqyqgpdtdkrlav 251
Cdd:cd06660 153 KAHGLPGFAAVQPQYSLLDRS---------PMEEELLDWAEENGLPLLAYSPLARGP----------------------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1001929468 252 ldeiaaetgatrNQLVYYWLMNRKPNAIPLIAATTDEQFKEALG 295
Cdd:cd06660 201 ------------AQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-309 |
4.78e-89 |
|
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: 268.30 E-value: 4.78e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 2 KKVQLGKTGLQVSQMGLGCLYFGARDS------KEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLK 75
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGDPKWrpwvldEEESRPIIKRALDLGINFFDTANVYS--------GGASEEILGRALK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 76 ERNNREDVIIASKVGFPY-PGTE-YGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRA 153
Cdd:cd19079 73 EFAPRDEVVIATKVYFPMgDGPNgRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 154 IGASNFKAWRLERARQIAKQNHWQSYSAIQQRYSYL-----RpksgwdfgdqvaanqDLFEFVEDTGISLVAYSPLLQGA 228
Cdd:cd19079 153 IGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLyreeeR---------------EMIPLCEEEGIGVIPWSPLARGR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 229 YTNPNKEFKEQYQGPDTDKR-------------LAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALG 295
Cdd:cd19079 218 LARPWGDTTERRRSTTDTAKlkydyfteadkeiVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVA 297
|
330
....*....|....
gi 1001929468 296 SLELELSEDMLRAM 309
Cdd:cd19079 298 ALDIKLSEEEIKYL 311
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-311 |
1.71e-85 |
|
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: 259.43 E-value: 1.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGCLYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERnnR 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYG--------GGRSEEIIGRWIAGR--R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 81 EDVIIASKVGFPyPGT---EYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGAS 157
Cdd:cd19087 71 DDIVLATKVFGP-MGDdpnDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 158 NFKAWRLERARQIAKQNHWQSYSAIQQRYSYLrpksgwdfgdQVAANQDLFEFVEDTGISLVAYSPL----LQGAYTN-- 231
Cdd:cd19087 150 NFAAWQIAKAQGIAARRGLLRFVSEQPMYNLL----------KRQAELEILPAARAYGLGVIPYSPLagglLTGKYGKgk 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 232 --------PNKEFKEQYQgpdTDKRLAVLDE---IAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELE 300
Cdd:cd19087 220 rpesgrlvERARYQARYG---LEEYRDIAERfeaLAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEIT 296
|
330
....*....|.
gi 1001929468 301 LSEDMLRAMTE 311
Cdd:cd19087 297 LTPELLAEIDE 307
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-298 |
3.27e-83 |
|
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: 252.86 E-value: 3.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 14 SQMGLGCLYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYSHWISDqtqgGESEKMIGKWLKERNNREDVIIASKVGFPY 93
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVER----GASERVIGEWLKSRGNRDKVVIATKGGHPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 94 PGTEYGT--SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNfkaWRLER---AR 168
Cdd:cd19082 77 LEDMSRSrlSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASN---WSTERiaeAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 169 QIAKQNHWQSYSAIQQRYSYLRPKSG-WDFGDQVAANQDLFEFVEDTGISLVAYSPLLQGAYT-------NPNKEFKEQY 240
Cdd:cd19082 154 AYAKAHGLPGFAASSPQWSLARPNEPpWPGPTLVAMDEEMRAWHEENQLPVFAYSSQARGFFSkraaggaEDDSELRRVY 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1001929468 241 QGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLE 298
Cdd:cd19082 234 YSEENFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-312 |
9.62e-83 |
|
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: 252.53 E-value: 9.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGCLYFGARDSKEKSFRRMDQYLA---------AGGNFLDTANMYShwisdqtqGGESEKMIG 71
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFFGAWGGVDQEEAdrlvdialdAGINFFDTADVYS--------EGESEEILG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 72 KWLKerNNREDVIIASKVGFPYPG--TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEG 149
Cdd:cd19091 73 KALK--GRRDDVLIATKVRGRMGEgpNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 150 KVRAIGASNFKAWRLERARQIAKQNHWQSYSAIQQRYSYLrpksGWDFgdqvaaNQDLFEFVEDTGISLVAYSPL----L 225
Cdd:cd19091 151 KVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLL----GRDL------EHELMPLALDQGVGLLVWSPLagglL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 226 QGAYTNPNKE------FKEQYQGPDTDKR-----LAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEAL 294
Cdd:cd19091 221 SGKYRRGQPApegsrlRRTGFDFPPVDRErgydvVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNL 300
|
330
....*....|....*...
gi 1001929468 295 GSLELELSEDMLRAMTEA 312
Cdd:cd19091 301 GAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-307 |
3.34e-77 |
|
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: 237.89 E-value: 3.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 6 LGKTGLQVSQMGLGCLYFGAR----DSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtQGGESEKMIGKWLKErnNRE 81
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNY--------TNGTSERLLGEFIAG--NRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 82 DVIIASKVGFPYPGTE---YGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASN 158
Cdd:cd19080 73 RIVLATKYTMNRRPGDpnaGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 159 FKAWRLERARQIAKQNHWQSYSAIQQRYSYLrpksgwdfgdQVAANQDLFEFVEDTGISLVAYSPL----LQGAYT---- 230
Cdd:cd19080 153 TPAWVVARANTLAELRGWSPFVALQIEYSLL----------ERTPERELLPMARALGLGVTPWSPLggglLTGKYQrgee 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 231 -----NPNKEFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELSEDM 305
Cdd:cd19080 223 grageAKGVTVGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQ 302
|
..
gi 1001929468 306 LR 307
Cdd:cd19080 303 LA 304
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-305 |
4.75e-68 |
|
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: 214.38 E-value: 4.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGC-LYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERNnREDVIIASK 88
Cdd:cd19074 1 GLKVSELSLGTwLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYA--------AGQAEEVLGKALKGWP-RESYVISTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 89 VGFPYPG--TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLER 166
Cdd:cd19074 72 VFWPTGPgpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 167 ARQIAKQNHWQSYSAIQQRYSYL-RPKSgwdfgdqvaanQDLFEFVEDTGISLVAYSPLLQG----------------AY 229
Cdd:cd19074 152 AHDLARQFGLIPPVVEQPQYNMLwREIE-----------EEVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsRA 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001929468 230 TNP-NKEFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELSEDM 305
Cdd:cd19074 221 TDEdNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPEV 297
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-312 |
8.97e-68 |
|
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: 213.33 E-value: 8.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 16 MGLGCLYFGARD---SKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtQGGESEKMIGKWLKERNN-REDVIIASKVGF 91
Cdd:pfam00248 1 IGLGTWQLGGGWgpiSKEEALEALRAALEAGINFIDTAEVY--------GDGKSEELLGEALKDYPVkRDKVVIATKVPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 92 PYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARqia 171
Cdd:pfam00248 73 GDGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKAL--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 172 kqNHWQS-YSAIQQRYSYLRPksgwdfgdqvAANQDLFEFVEDTGISLVAYSPLLQGAYT-----NPNKEFKEQ-----Y 240
Cdd:pfam00248 150 --TKGKIpIVAVQVEYNLLRR----------RQEEELLEYCKKNGIPLIAYSPLGGGLLTgkytrDPDKGPGERrrllkK 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001929468 241 QGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELSEDMLRAMTEA 312
Cdd:pfam00248 218 GTPLNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-308 |
2.93e-66 |
|
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: 210.88 E-value: 2.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 13 VSQMGLGCLYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYSHWISDQTQGgESEKMIGKWLKERNNREDVIIASKV--- 89
Cdd:cd19094 1 VSEICLGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPSPETQG-RTEEIIGSWLKKKGNRDKVVLATKVagp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 90 --GFPYP-GTEYGTSKKQIKEECHKSLERLGTDYIDLYYAH-----TDDFN-------------TPLEETLEAFNELITE 148
Cdd:cd19094 80 geGITWPrGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHwpdryTPLFGggyytepseeedsVSFEEQLEALGELVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 149 GKVRAIGASNFKAWRLERARQIAKQNHWQSYSAIQQRYSYLrpksgwdfgdqvaaNQ----DLFEFVEDTGISLVAYSPL 224
Cdd:cd19094 160 GKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLL--------------NRnfeeGLAEACHRENVGLLAYSPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 225 ----LQGAYTNPN-----------KEFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQ 289
Cdd:cd19094 226 aggvLTGKYLDGAarpeggrlnlfPGYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQ 305
|
330
....*....|....*....
gi 1001929468 290 FKEALGSLELELSEDMLRA 308
Cdd:cd19094 306 LKENIDAFDVPLSDELLAE 324
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-309 |
1.01e-65 |
|
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: 208.15 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLYFGARD----SKEKSFRRMDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKERnnREDVII 85
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTWwgevDDQESIEAIKAAIDLGINFFDTAPVYGF--------GHSEEILGKALKGR--RDDVVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 86 ASKVGFPYPGTEYGT---SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAW 162
Cdd:cd19084 71 ATKCGLRWDGGKGVTkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 163 RLERARQIAKqnhwqsYSAIQQRYSYLRPKsgwdfgdqvaANQDLFEFVEDTGISLVAYSPL----LQGAYTNPNKeFKE 238
Cdd:cd19084 151 QLEEARKYGP------IVSLQPPYSMLERE----------IEEELLPYCRENGIGVLPYGPLaqglLTGKYKKEPT-FPP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 239 --------QYQGPDTDK---RLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELSEDMLR 307
Cdd:cd19084 214 ddrrsrfpFFRGENFEKnleIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELK 293
|
..
gi 1001929468 308 AM 309
Cdd:cd19084 294 EI 295
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-308 |
4.58e-62 |
|
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: 198.98 E-value: 4.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 2 KKVQLGKTGLQVSQMGLGCL----YFGARDSKEkSFRRMDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKER 77
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMgmsaFYGPADEEE-SIATLHRALELGVTFLDTADMYGP--------GTNEELLGKALKDR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 78 nnREDVIIASKVGFPYPGTEYGT----SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRA 153
Cdd:cd19076 72 --RDEVVIATKFGIVRDPGSGFRgvdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 154 IGASNFKAWRLERARQIAKqnhwqsYSAIQQRYSYlrpksgWDFGdqvaANQDLFEFVEDTGISLVAYSPL----LQGAY 229
Cdd:cd19076 150 IGLSEASADTIRRAHAVHP------ITAVQSEYSL------WTRD----IEDEVLPTCRELGIGFVAYSPLgrgfLTGAI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 230 TNPNKE-------FKEQYQGPDTDKRLAVLD---EIAAETGATRNQLVYYWLMNRKPNAIPlIAATTDEQF-KEALGSLE 298
Cdd:cd19076 214 KSPEDLpeddfrrNNPRFQGENFDKNLKLVEkleAIAAEKGCTPAQLALAWVLAQGDDIVP-IPGTKRIKYlEENVGALD 292
|
330
....*....|
gi 1001929468 299 LELSEDMLRA 308
Cdd:cd19076 293 VVLTPEELAE 302
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-312 |
5.22e-60 |
|
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: 193.57 E-value: 5.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 13 VSQMGLGC------LYFGARDSKEkSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERnnREDVIIA 86
Cdd:cd19085 1 VSRLGLGCwqfgggYWWGDQDDEE-SIATIHAALDAGINFFDTAEAYG--------DGHSEEVLGKALKGR--RDDVVIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 87 SKVGFPYPgteygtSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLER 166
Cdd:cd19085 70 TKVSPDNL------TPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 167 ARQIAKqnhwqsYSAIQQRYSYLrpksgWdfgdqVAANQDLFEFVEDTGISLVAYSPLLQGAYTnpnKEFKEQYQGPDTD 246
Cdd:cd19085 144 ALDAGR------IDSNQLPYNLL-----W-----RAIEYEILPFCREHGIGVLAYSPLAQGLLT---GKFSSAEDFPPGD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 247 KR------------------LAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELSEDMLRA 308
Cdd:cd19085 205 ARtrlfrhfepgaeeetfeaLEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLER 284
|
....
gi 1001929468 309 MTEA 312
Cdd:cd19085 285 LDEI 288
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-311 |
1.87e-57 |
|
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: 187.48 E-value: 1.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 3 KVQLGKTGLQVSQMGLGCL-----YFGARDSKEKSFRRMDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKER 77
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWaigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGF--------GHSEEIVGKAIKGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 78 nnREDVIIASKVG---------FPYPGTEY----GTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNE 144
Cdd:cd19149 73 --RDKVVLATKCGlrwdreggsFFFVRDGVtvykNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 145 LITEGKVRAIGASNFKAWRLERARQIAkqnhwqSYSAIQQRYSYLRPKsgwdfgdqvaANQDLFEFVEDTGISLVAYSPL 224
Cdd:cd19149 151 LKRQGKIRAIGASNVSVEQIKEYVKAG------QLDIIQEKYSMLDRG----------IEKELLPYCKKNNIAFQAYSPL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 225 LQGAYTN---PNKEFKEQ--------YQGPDTDKRLAVLDE---IAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQF 290
Cdd:cd19149 215 EQGLLTGkitPDREFDAGdarsgipwFSPENREKVLALLEKwkpLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQA 294
|
330 340
....*....|....*....|.
gi 1001929468 291 KEALGSLELELSEDMLRAMTE 311
Cdd:cd19149 295 EENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-307 |
2.98e-56 |
|
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: 182.81 E-value: 2.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLYFGARDSKEKSFRRMD----QY-LAAGGNFLDTANMYshwisdqtQGGESEKMIGKWLKERNnREDVI 84
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSDDKKAiealRYaIELGINLIDTAEMY--------GGGHAEELVGKAIKGFD-REDLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 85 IASKVgfpYPgteYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRL 164
Cdd:cd19072 72 ITTKV---SP---DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 165 ERARQIAKQNHwqsYSAIQQRYSYLrpksgwdfgDQVAANqDLFEFVEDTGISLVAYSPLLQGAYTNpnkefkeqyqgpd 244
Cdd:cd19072 146 EEAQSYLKKGP---IVANQVEYNLF---------DREEES-GLLPYCQKNGIAIIAYSPLEKGKLSN------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001929468 245 tDKRLAVLDEIAAETGATRNQLVYYWLMnRKPNAIPLIAATTDEQFKEALGSLELELS-EDMLR 307
Cdd:cd19072 200 -AKGSPLLDEIAKKYGKTPAQIALNWLI-SKPNVIAIPKASNIEHLEENAGALGWELSeEDLQR 261
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-312 |
7.31e-56 |
|
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: 183.20 E-value: 7.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCL----YFGARDSKEKSFRRMDQYLAAGGNFLDTANMYSHWISdqtqggesEKMIGKWLKERnnREDVII 85
Cdd:cd19078 1 GLEVSAIGLGCMgmshGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTN--------EELVGEALKPF--RDQVVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 86 ASKVGFPYPGTEYGT-----SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFK 160
Cdd:cd19078 71 ATKFGFKIDGGKPGPlgldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 161 AWRLERARQIakqnhwQSYSAIQQRYSYLRPKsgwdfgdqvaANQDLFEFVEDTGISLVAYSPL----LQGAYtNPNKEF 236
Cdd:cd19078 151 VETIRRAHAV------CPVTAVQSEYSMMWRE----------PEKEVLPTLEELGIGFVPFSPLgkgfLTGKI-DENTKF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 237 KEqyqgpdTDKR-----------------LAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLEL 299
Cdd:cd19078 214 DE------GDDRaslprftpealeanqalVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI 287
|
330
....*....|...
gi 1001929468 300 ELSEDMLRAMTEA 312
Cdd:cd19078 288 ELTPEELREIEDA 300
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-312 |
5.57e-54 |
|
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: 178.79 E-value: 5.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGCL----YFGARDSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqgGESEKMIGKWLKe 76
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsaFYGPPKPDEERFAVLDAAFELGCTFWDTADIY----------GDSEELIGRWFK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 77 RN--NREDVIIASKVGF--PYPGTEYGT--SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGK 150
Cdd:cd19144 70 QNpgKREKIFLATKFGIekNVETGEYSVdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 151 VRAIGASNFKAWRLERARQIakqnhwQSYSAIQQRYSylrPksgwdFGDQVAANQ-DLFEFVEDTGISLVAYSPL----L 225
Cdd:cd19144 150 IKHIGLSECSAETLRRAHAV------HPIAAVQIEYS---P-----FSLDIERPEiGVLDTCRELGVAIVAYSPLgrgfL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 226 QGAYTNPN----KEFKE---QYQGPDTDKRLAVLDEI---AAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALG 295
Cdd:cd19144 216 TGAIRSPDdfeeGDFRRmapRFQAENFPKNLELVDKIkaiAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLG 295
|
330
....*....|....*..
gi 1001929468 296 SLELELSEDMLRAMTEA 312
Cdd:cd19144 296 ALKVKLTEEEEKEIREI 312
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
11-309 |
8.53e-52 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 173.89 E-value: 8.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 11 LQVSQMGLGCLYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYSHWISDQTQGgESEKMIGKWLKERNNREDVIIASKVG 90
Cdd:PRK10625 11 LEVSTLGLGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPRPETQG-LTETYIGNWLAKRGSREKLIIASKVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 91 FPYPGTEYGT------SKKQIKEECHKSLERLGTDYIDLYYAH-----TDDF---------NTP---LEETLEAFNELIT 147
Cdd:PRK10625 90 GPSRNNDKGIrpnqalDRKNIREALHDSLKRLQTDYLDLYQVHwpqrpTNCFgklgyswtdSAPavsLLETLDALAEQQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 148 EGKVRAIGASNFKAWRLERARQIAKQNHWQSYSAIQQRYSYLrpKSGWDFGdqvaanqdLFEFVEDTGISLVAYSPL--- 224
Cdd:PRK10625 170 AGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLL--NRSFEVG--------LAEVSQYEGVELLAYSCLafg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 225 -LQGAYTN---P----NKEFKE--QYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEAL 294
Cdd:PRK10625 240 tLTGKYLNgakPagarNTLFSRftRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNI 319
|
330
....*....|....*
gi 1001929468 295 GSLELELSEDMLRAM 309
Cdd:PRK10625 320 ESLHLTLSEEVLAEI 334
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-312 |
7.71e-50 |
|
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: 168.37 E-value: 7.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLYFGARD-------SKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtQGGESEKMIGKWLKERNNRED 82
Cdd:cd19146 8 GVRVSPLCLGAMSFGEAWksmmgecDKETAFKLLDAFYEQGGNFIDTANNY--------QGEESERWVGEWMASRGNRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 83 VIIASKVGFPYPGTEY--------GTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAI 154
Cdd:cd19146 80 MVLATKYTTGYRRGGPikiksnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 155 GASNFKAWRLERARQIAKQNHWQSYSAIQQRYSylrpksgwdfgdqvAANQDlFE-----FVEDTGISLVAYSPLLQGAY 229
Cdd:cd19146 160 GVSDTPAWVVSKANAYARAHGLTQFVVYQGHWS--------------AAFRD-FErdilpMCEAEGMALAPWGVLGQGQF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 230 TNPnKEFKEQ-----YQGPDTDKRL---AVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELEL 301
Cdd:cd19146 225 RTE-EEFKRRgrsgrKGGPQTEKERkvsEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISL 303
|
330
....*....|.
gi 1001929468 302 SEDMLRAMTEA 312
Cdd:cd19146 304 SDEEIQEIEDA 314
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-304 |
1.30e-49 |
|
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: 166.63 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 12 QVSQMGLGCLYFGAR------DSKEKSFRR-MDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERNNREDVI 84
Cdd:cd19093 1 EVSPLGLGTWQWGDRlwwgygEYGDEDLQAaFDAALEAGVNLFDTAEVYG--------TGRSERLLGRFLKELGDRDEVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 85 IASKVgFPYPGTeygTSKKQIKEECHKSLERLGTDYIDLYYAH-TDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWR 163
Cdd:cd19093 73 IATKF-APLPWR---LTRRSVVKALKASLERLGLDSIDLYQLHwPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 164 LERARQIAKQnHWQSYSAIQQRYSYLRPKsgwdfgdqvAANQDLFEFVEDTGISLVAYSPLLQGA----YTNPN------ 233
Cdd:cd19093 149 LRRAHKALKE-RGVPLASNQVEYSLLYRD---------PEQNGLLPACDELGITLIAYSPLAQGLltgkYSPENpppggr 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001929468 234 KEFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRkpNAIPLIAATTDEQFKEALGSLELELSED 304
Cdd:cd19093 219 RRLFGRKNLEKVQPLLDALEEIAEKYGKTPAQVALNWLIAK--GVVPIPGAKNAEQAEENAGALGWRLSEE 287
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
3-304 |
2.25e-49 |
|
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: 166.44 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 3 KVQLGKTGLQVSQMGLGCLYFGARD-----SKEKSFRRMDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKER 77
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTNAVGGHNlypnlDEEEGKDLVREALDNGVNLLDTAFIYGL--------GRSEELVGEVLKEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 78 NnREDVIIASKVG--FPYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIG 155
Cdd:cd19083 73 N-RNEVVIATKGAhkFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 156 ASNFKAWRLERArqiakqNHWQSYSAIQQRYSYLrpksgwdfgdQVAANQDLFEFVEDTGISLVAYSPL----LQGAYTn 231
Cdd:cd19083 152 VSNFSLEQLKEA------NKDGYVDVLQGEYNLL----------QREAEEDILPYCVENNISFIPYFPLasglLAGKYT- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 232 PNKEF--------KEQYQGPDTDKRLAVLD---EIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELE 300
Cdd:cd19083 215 KDTKFpdndlrndKPLFKGERFSENLDKVDklkSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVT 294
|
....
gi 1001929468 301 LSED 304
Cdd:cd19083 295 LTEE 298
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-227 |
3.31e-48 |
|
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: 161.11 E-value: 3.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 11 LQVSQMGLGCLYFGARD----SKEKSFRRMDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKERnnREDVIIA 86
Cdd:cd19086 1 LEVSEIGFGTWGLGGDWwgdvDDAEAIRALRAALDLGINFFDTADVYGD--------GHSERLLGKALKGR--RDKVVIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 87 SKVG---FPYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAH---TDDFNTplEETLEAFNELITEGKVRAIGASnfk 160
Cdd:cd19086 71 TKFGnrfDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnppDEVLDN--DELFEALEKLKQEGKIRAYGVS--- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001929468 161 AWRLERARQIAKQNHwqsYSAIQQRYSYLRPKSGwdfgdqvaanQDLFEFVEDTGISLVAYSPLLQG 227
Cdd:cd19086 146 VGDPEEALAALRRGG---IDVVQVIYNLLDQRPE----------EELFPLAEEHGVGVIARVPLASG 199
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-302 |
3.89e-47 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 160.32 E-value: 3.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGCLYFGARD-SKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERN- 78
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDlSPAEAAALIEAALELGITTFDHADIYG--------GYTCEALFGEALKLSPs 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 79 NREDVIIASKVGFPYPGTE-------YGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDfntPL---EETLEAFNELITE 148
Cdd:COG4989 73 LREKIELQTKCGIRLPSEArdnrvkhYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPD---PLmdpEEVAEAFDELKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 149 GKVRAIGASNFKAWrlerarQIAkqnhwqsysAIQqrySYLRPKsgwdfgdqVAANQ-------------DLFEFVEDTG 215
Cdd:COG4989 150 GKVRHFGVSNFTPS------QFE---------LLQ---SALDQP--------LVTNQielsllhtdafddGTLDYCQLNG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 216 ISLVAYSPLLQGAYTNpnkEFKEQYQgpdtdkRL-AVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEAL 294
Cdd:COG4989 204 ITPMAWSPLAGGRLFG---GFDEQFP------RLrAALDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAA 274
|
....*...
gi 1001929468 295 GSLELELS 302
Cdd:COG4989 275 AALDIELT 282
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-299 |
3.26e-46 |
|
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: 158.53 E-value: 3.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGC-LYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERN- 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYA--------NGQSEEIMGQAIKELGw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 79 NREDVIIASKV--GFPYPG-TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIG 155
Cdd:cd19143 73 PRSDYVVSTKIfwGGGGPPpNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 156 ASNFKAWRLERARQIAKQNHWQSYSAIQQRYSYL-RPKSGWDFGdqvaanqDLFefvEDTGISLVAYSPL----LQGAYT 230
Cdd:cd19143 153 TSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFhRERVEVEYA-------PLY---EKYGLGTTTWSPLasglLTGKYN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 231 N----------PNKEFKEQYQGPDTDKRLAVLDE---IAAETGATRNQLVYYWLMnRKPNAIPLI-AATTDEQFKEALGS 296
Cdd:cd19143 223 NgipegsrlalPGYEWLKDRKEELGQEKIEKVRKlkpIAEELGCSLAQLAIAWCL-KNPNVSTVItGATKVEQLEENLKA 301
|
...
gi 1001929468 297 LEL 299
Cdd:cd19143 302 LEV 304
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
16-312 |
1.78e-44 |
|
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: 153.48 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 16 MGLGclYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKwLKERNnrEDVIIASKVgfpYPG 95
Cdd:cd19075 8 MTFG--SQGRFTTAEAAAELLDAFLERGHTEIDTARVYP--------DGTSEELLGE-LGLGE--RGFKIDTKA---NPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 96 TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAKQNH 175
Cdd:cd19075 72 VGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 176 WQSYSAIQQRYSYL-RpksgwdfgdqvAANQDLFEFVEDTGISLVAYSPL----LQGAYTNPNKE--------------- 235
Cdd:cd19075 152 WVLPTVYQGMYNAItR-----------QVETELFPCLRKLGIRFYAYSPLaggfLTGKYKYSEDKagggrfdpnnalgkl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 236 FKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMN------RKPNAIpLIAATTDEQFKEALGSLEL-ELSEDMLRA 308
Cdd:cd19075 221 YRDRYWKPSYFEALEKVEEAAEKEGISLAEAALRWLYHhsaldgEKGDGV-ILGASSLEQLEENLAALEKgPLPEEVVKA 299
|
....
gi 1001929468 309 MTEA 312
Cdd:cd19075 300 IDEA 303
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-312 |
7.53e-44 |
|
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: 152.06 E-value: 7.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 24 GARDSKEkSFRRMDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKERnnREDVIIASKVGfPYPGTE----YG 99
Cdd:cd19102 21 GPQDDRD-SIAAIRAALDLGINWIDTAAVYGL--------GHSEEVVGRALKGL--RDRPIVATKCG-LLWDEEgrirRS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 100 TSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAkqnhwqSY 179
Cdd:cd19102 89 LKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIH------PI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 180 SAIQQRYSYLRPksgwdfgdqvAANQDLFEFVEDTGISLVAYSP----LLQGAYT---------NPNKEFKEQYQGPDTD 246
Cdd:cd19102 163 ASLQPPYSLLRR----------GIEAEILPFCAEHGIGVIVYSPmqsgLLTGKMTpervaslpaDDWRRRSPFFQEPNLA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001929468 247 KRLAVLDE---IAAETGATRNQLVYYWLMnRKPN---AIPliAATTDEQFKEALGSLELELSEDMLRAMTEA 312
Cdd:cd19102 233 RNLALVDAlrpIAERHGRTVAQLAIAWVL-RRPEvtsAIV--GARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-302 |
9.15e-43 |
|
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: 148.86 E-value: 9.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 8 KTGLQVSQMGLGCLYFG-ARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERNN-REDVII 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLAdWGESAEELLSLIEAALELGITTFDHADIYG--------GGKCEELFGEALALNPGlREKIEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 86 ASKVG-------FPYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDfntPL---EETLEAFNELITEGKVRAIG 155
Cdd:cd19092 73 QTKCGirlgddpRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPD---PLmdpEEVAEAFDELVKSGKVRYFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 156 ASNFKAWRLErarqiAKQNHW-QSYSAIQQRYSYLRPkSGWDFGDQVAANQDlfefvedtGISLVAYSPLLQGAYTNPNK 234
Cdd:cd19092 150 VSNFTPSQIE-----LLQSYLdQPLVTNQIELSLLHT-EAIDDGTLDYCQLL--------DITPMAWSPLGGGRLFGGFD 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 235 EfkeqyqgpdTDKRL-AVLDEIAAETGATRNQLVYYWLMnRKP-NAIPLIAATTDEQFKEALGSLELELS 302
Cdd:cd19092 216 E---------RFQRLrAALEELAEEYGVTIEAIALAWLL-RHPaRIQPILGTTNPERIRSAVKALDIELT 275
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-302 |
1.43e-41 |
|
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: 144.67 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 13 VSQMGLGCL------YFGARDSKEKSFRRMDQYLAAGGNFLDTANMYS-HWisdqtqggeSEKMIGKWLKERnnREDVII 85
Cdd:cd19088 1 VSRLGYGAMrltgpgIWGPPADREEAIAVLRRALELGVNFIDTADSYGpDV---------NERLIAEALHPY--PDDVVI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 86 ASKVGFPYPGTEYGT---SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAW 162
Cdd:cd19088 70 ATKGGLVRTGPGWWGpdgSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 163 RLERARQIAKqnhwqsYSAIQQRYSYLRPKSgwdfgdqvaanQDLFEFVEDTGISLVAYSPLLQGAYTnpnkefkeqyqg 242
Cdd:cd19088 150 QIEEARAIVR------IVSVQNRYNLANRDD-----------EGVLDYCEAAGIAFIPWFPLGGGDLA------------ 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 243 pdtdKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELS 302
Cdd:cd19088 201 ----QPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-309 |
1.05e-40 |
|
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: 143.60 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGC------LYFGARDskEKSFRRMDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKERNNREDV 83
Cdd:cd19148 1 DLPVSRIALGTwaiggwMWGGTDE--KEAIETIHKALDLGINLIDTAPVYGF--------GLSEEIVGKALKEYGKRDRV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 84 IIASKVGFPY-PGTEYG--TSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFK 160
Cdd:cd19148 71 VIATKVGLEWdEGGEVVrnSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 161 AWRLERARQIAKqnhwqsYSAIQQRYSYLRPksgwdfgdqvAANQDLFEFVEDTGISLVAYSPLLQGAYT---NPNKEFK 237
Cdd:cd19148 151 PEQMETFRKVAP------LHTVQPPYNLFER----------EIEKDVLPYARKHNIVTLAYGALCRGLLSgkmTKDTKFE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 238 E--------QYQGPDTDKRL-AV--LDEIAAETGATR-NQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELSEDM 305
Cdd:cd19148 215 GddlrrtdpKFQEPRFSQYLaAVeeLDKLAQERYGKSvIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDED 294
|
....
gi 1001929468 306 LRAM 309
Cdd:cd19148 295 MKEI 298
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
6-306 |
1.25e-40 |
|
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: 143.55 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 6 LGKTGLQVSQ--MGLGCLyFGARDSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqG---GESEKMIGKWLKE--RN 78
Cdd:cd19089 4 CGRSGLHLPAisLGLWHN-FGDYTSPEEARELLRTAFDLGITHFDLANNY---------GpppGSAEENFGRILKRdlRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 79 NREDVIIASKVGFPYPGTEYGT--SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGA 156
Cdd:cd19089 74 YRDELVISTKAGYGMWPGPYGDggSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 157 SNFKAWRLERArqIAKQNHWQSYSAIQQ-RYSYLRPKsgwdfgdqvaANQDLFEFVEDTGISLVAYSPLLQGAYTN---- 231
Cdd:cd19089 154 SNYPGAKARRA--IALLRELGVPLIIHQpRYSLLDRW----------AEDGLLEVLEEAGIGFIAFSPLAQGLLTDkyln 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 232 ----------PNKEFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLE-LE 300
Cdd:cd19089 222 gippdsrraaESKFLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKnLD 301
|
....*.
gi 1001929468 301 LSEDML 306
Cdd:cd19089 302 FSEEEL 307
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
2-308 |
2.94e-40 |
|
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: 141.62 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 2 KKVQLGkTGLQVSQMGLGCLYFG-ARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERnnR 80
Cdd:cd19138 1 RTVTLP-DGTKVPALGQGTWYMGeDPAKRAQEIEALRAGIDLGMTLIDTAEMYG--------DGGSEELVGEAIRGR--R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 81 EDVIIASKVgfpYPGTeygTSKKQIKEECHKSLERLGTDYIDLYYAHTDDfNTPLEETLEAFNELITEGKVRAIGASNFK 160
Cdd:cd19138 70 DKVFLVSKV---LPSN---ASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 161 AWRLERARQIAKqnhwqsysaiqqrysylrpksgwdfGDQVAANQ------------DLFEFVEDTGISLVAYSPLLQGa 228
Cdd:cd19138 143 TDDMEELWAVPG-------------------------GGNCAANQvlynlgsrgieyDLLPWCREHGVPVMAYSPLAQG- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 229 ytnpnkefkeqyqGPDTDKRLA--VLDEIAAETGATRNQLVYYWLMnRKPNAIPLIAATTDEQFKEALGSLELELSEDML 306
Cdd:cd19138 197 -------------GLLRRGLLEnpTLKEIAARHGATPAQVALAWVL-RDGNVIAIPKSGSPEHARENAAAADLELTEEDL 262
|
..
gi 1001929468 307 RA 308
Cdd:cd19138 263 AE 264
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-313 |
3.61e-40 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 143.81 E-value: 3.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGCLYFGARDskEKSFRRM-DQYLAAGGNFLDTANMYshwisdqtqgGESEKMIGKWLKERnn 79
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPRKD--EEEAEALiRRAIDNGINYIDTARGY----------GDSEEFLGKALKGP-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 80 REDVIIASKVgfpypgTEYGTSKKQIKEECHKSLERLGTDYIDLYYAH----TDDFNTPLEET--LEAFNELITEGKVRA 153
Cdd:COG1453 67 RDKVILATKL------PPWVRDPEDMRKDLEESLKRLQTDYIDLYLIHglntEEDLEKVLKPGgaLEALEKAKAEGKIRH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 154 IGASNFKawRLERARQIAKQNHWqsySAIQQRYSYLrpksgwDFGDQvaANQDLFEFVEDTGISLVAYSPLLQGAYTNPN 233
Cdd:COG1453 141 IGFSTHG--SLEVIKEAIDTGDF---DFVQLQYNYL------DQDNQ--AGEEALEAAAEKGIGVIIMKPLKGGRLANPP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 234 KEFKEQYQGPDTDKRLAvldeiaaetgatrnqlvYYWLMNRKPNAIPLIAATTDEQFKEALGSLELE--LSEDMLRAMTE 311
Cdd:COG1453 208 EKLVELLCPPLSPAEWA-----------------LRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLepLTEEELAILER 270
|
..
gi 1001929468 312 AK 313
Cdd:COG1453 271 LA 272
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
40-312 |
1.16e-39 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 139.81 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERN-NREDVIIASKVgfpyPGTEYGtsKKQIKEECHKSLERLGT 118
Cdd:COG0656 28 LEAGYRHIDTAAMY-----------GNEEGVGEAIAASGvPREELFVTTKV----WNDNHG--YDDTLAAFEESLERLGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 119 DYIDLYYAHTDdFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAkqnhwqsysaiqqrysylrpksgwdfG 198
Cdd:COG0656 91 DYLDLYLIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAET--------------------------G 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 199 DQVAANQ----------DLFEFVEDTGISLVAYSPLLQGA-YTNPnkefkeqyqgpdtdkrlaVLDEIAAETGATRNQLV 267
Cdd:COG0656 144 VKPAVNQvelhpylqqrELLAFCREHGIVVEAYSPLGRGKlLDDP------------------VLAEIAEKHGKTPAQVV 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1001929468 268 YYWLMNRkpNAIPLIAATTDEQFKEALGSLELELSEDMLRAMTEA 312
Cdd:COG0656 206 LRWHLQR--GVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDAL 248
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-305 |
1.73e-38 |
|
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: 137.95 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 3 KVQLGKTGLQVSQMGLGCLYFGARDSKEKSFRRMDQYL----AAGGNFLDTANMYshwisdqtqGGES-EKMIGKWLKEr 77
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGLSGDYGAPKPEEEGIALIhhafNSGVTFLDTSDIY---------GPNTnEVLLGKALKD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 78 NNREDVIIASKVGFPYP---GTEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAI 154
Cdd:cd19145 72 GPREKVQLATKFGIHEIggsGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 155 GASNFKAWRLERARQIakqnhwQSYSAIQQRYSYlrpksgW--DfgdqvaANQDLFEFVEDTGISLVAYSPLLQGAYT-- 230
Cdd:cd19145 152 GLSEASADTIRRAHAV------HPITAVQLEWSL------WtrD------IEEEIIPTCRELGIGIVPYSPLGRGFFAgk 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 231 -----NP-NKEFKEQ---YQGPDTDKRLAV---LDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLE 298
Cdd:cd19145 214 akleeLLeNSDVRKShprFQGENLEKNKVLyerVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALS 293
|
....*...
gi 1001929468 299 LELS-EDM 305
Cdd:cd19145 294 VKLTkEDL 301
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
6-304 |
1.37e-37 |
|
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: 136.11 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 6 LGKT-GLQVSQMGLGCLYFG-ARDS------KEKSFRRMDQYLAAGGNFLDTANMYshwisdqtQGGESEKMIGKWLKER 77
Cdd:cd19147 2 LSKTaGIRVSPLILGAMSIGdAWSGfmgsmdKEQAFELLDAFYEAGGNFIDTANNY--------QDEQSETWIGEWMKSR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 78 NNREDVIIASKVGFPYPGTEYGT---------SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITE 148
Cdd:cd19147 74 KNRDQIVIATKFTTDYKAYEVGKgkavnycgnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 149 GKVRAIGASNFKAWRLERARQIAKQNHWQSYSAIQQRYSYLRPksgwDFgdqvaaNQDLFEFVEDTGISLVAYSPLLQGA 228
Cdd:cd19147 154 GKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNR----DF------ERDIIPMARHFGMALAPWDVLGGGK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 229 YTNP--------NKEFKEQYQGPD--TDKRLAV---LDEIAAETG-ATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEAL 294
Cdd:cd19147 224 FQSKkaveerkkNGEGLRSFVGGTeqTPEEVKIseaLEKVAEEHGtESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNI 303
|
330
....*....|
gi 1001929468 295 GSLELELSED 304
Cdd:cd19147 304 EALSIKLTPE 313
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
40-307 |
5.87e-37 |
|
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: 132.39 E-value: 5.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKE-RNNREDVIIASKVgfPYPGTEYgtskKQIKEECHKSLERLGT 118
Cdd:cd19073 24 LELGYRHIDTAEIY-----------NNEAEVGEAIAEsGVPREDLFITTKV--WRDHLRP----EDLKKSVDRSLEKLGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 119 DYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAKqnhwQSYSAIQQRYS-YLRPksgwdf 197
Cdd:cd19073 87 DYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIAVNQVEFHpFLYQ------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 198 gdqvaanQDLFEFVEDTGISLVAYSPLLQGaytnpnkefkeqyqgpdTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPN 277
Cdd:cd19073 157 -------AELLEYCRENDIVITAYSPLARG-----------------EVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIV 212
|
250 260 270
....*....|....*....|....*....|.
gi 1001929468 278 AIPliAATTDEQFKEALGSLELEL-SEDMLR 307
Cdd:cd19073 213 VIP--KASSEDHLKENLAIFDWELtSEDVAK 241
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-305 |
9.40e-37 |
|
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: 133.52 E-value: 9.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 9 TGLQVSQMGLGCLYFGARD---SKEKSFRRMDQYLAAGGNFLDTANMYSHwiSDQTqggESEKMIGKWLKER-NNREDVI 84
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRPnptPDEEAFETMKAALDAGSNLWNGGEFYGP--PDPH---ANLKLLARFFRKYpEYADKVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 85 IASKVGFPYPGTEYGTSKKQIKEECHKSLERLG-TDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWR 163
Cdd:cd19077 76 LSVKGGLDPDTLRPDGSPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 164 LERARQIAKqnhwqsYSAIQQRYSYlrpksgwdFGDQVAANqDLFEFVEDTGISLVAYSPL----LQGAYTN----PNKE 235
Cdd:cd19077 156 IRRAHAVHP------IAAVEVEYSL--------FSREIEEN-GVLETCAELGIPIIAYSPLgrglLTGRIKSladiPEGD 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001929468 236 FK---EQYQGPDTDKRLA---VLDEIAAETGATRNQLVYYWLMNR-KPNAIPLIAATTDEQFKEALGSLELELS-EDM 305
Cdd:cd19077 221 FRrhlDRFNGENFEKNLKlvdALQELAEKKGCTPAQLALAWILAQsGPKIIPIPGSTTLERVEENLKAANVELTdEEL 298
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-157 |
1.09e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 131.45 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 3 KVQLGKTGLQVSQMGLGCLYFGaRDSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqgGESEKMIGKWLKERnnRED 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLG-RLSQEEAAAIIRRALDLGINYFDTAPSY----------GDSEEKIGKALKGR--RDK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 83 VIIASKVGfpypgteyGTSKKQIKEECHKSLERLGTDYIDLYYAHT----DDFNTPLEE--TLEAFNELITEGKVRAIGA 156
Cdd:cd19100 68 VFLATKTG--------ARDYEGAKRDLERSLKRLGTDYIDLYQLHAvdteEDLDQVFGPggALEALLEAKEEGKIRFIGI 139
|
.
gi 1001929468 157 S 157
Cdd:cd19100 140 S 140
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-157 |
1.74e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 131.17 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGCLYFGARDSKekSFRRMdqyLAAGGNFLDTANMYshwisdqtQGGESEKMIGKWLKeRNNR 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRESPE--LLRRA---LDLGINYFDTAEGY--------GNGNSEEIIGEALK-GLRR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 81 EDVIIASKVGFPypgtEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPL---EETLEAFNELITEGKVRAIGAS 157
Cdd:cd19105 67 DKVFLATKASPR----LDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-307 |
2.28e-34 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 127.13 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 7 GKTGLQVSQMGLGCLY-FGARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqTQGGESEKMIGKWLKE--RNNREDV 83
Cdd:cd19151 6 GRSGLKLPAISLGLWHnFGDVDRYENSRAMLRRAFDLGITHFDLANNYG------PPPGSAEENFGRILKEdlKPYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 84 IIASKVGFP-YPGTeYGT--SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFK 160
Cdd:cd19151 80 IISTKAGYTmWPGP-YGDwgSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 161 AWRLERARQIAKQN------HwqsysaiQQRYSYLrpksgwdfgdQVAANQDLFEFVEDTGISLVAYSPLLQGAYTN--- 231
Cdd:cd19151 159 PEEAREAAAILKDLgtpcliH-------QPKYSMF----------NRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDryl 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 232 -----------PNKEFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLE-L 299
Cdd:cd19151 222 ngipedsraakGSSFLKPEQITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDnR 301
|
....*...
gi 1001929468 300 ELSEDMLR 307
Cdd:cd19151 302 EFSEEELA 309
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-307 |
1.32e-33 |
|
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: 123.83 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLYFG-------ARDskEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERNnRED 82
Cdd:cd19137 1 GEKIPALGLGTWGIGgfltpdySRD--EEMVELLKTAIELGYTHIDTAEMYG--------GGHTEELVGKAIKDFP-RED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 83 VIIASKVgfpYPGTeygTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAW 162
Cdd:cd19137 70 LFIVTKV---WPTN---LRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 163 RLERArqiakqnhwQSYSAI-----QQRYSYLrpksgwdfgDQVAANQDLFEFVEDTGISLVAYSPLLQGAYtnPNKEfk 237
Cdd:cd19137 144 LLEEA---------ISKSQTpivcnQVKYNLE---------DRDPERDGLLEYCQKNGITVVAYSPLRRGLE--KTNR-- 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 238 eqyqgpdtdkrlaVLDEIAAETGATRNQLVYYWLMnRKPNAIPLIAATTDEQFKEALGSLELELSEDMLR 307
Cdd:cd19137 202 -------------TLEEIAKNYGKTIAQIALAWLI-QKPNVVAIPKAGRVEHLKENLKATEIKLSEEEMK 257
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-305 |
3.49e-33 |
|
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: 122.59 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 15 QMGLGClyfgARDSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERN-NREDVIIASKVGFPY 93
Cdd:cd19071 3 LIGLGT----YKLKPEETAEAVLAALEAGYRHIDTAAAY-----------GNEAEVGEAIRESGvPREELFITTKLWPTD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 94 PGTEygtskkQIKEECHKSLERLGTDYIDLYYAH------TDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERA 167
Cdd:cd19071 68 HGYE------RVREALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 168 RQIAKqnhwqsysaiqqrysyLRPksgwdfgdqvAANQ----------DLFEFVEDTGISLVAYSPLlqGAYTNPNKEFK 237
Cdd:cd19071 142 LAAAR----------------IKP----------AVNQielhpylqqkELVEFCKEHGIVVQAYSPL--GRGRRPLLDDP 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1001929468 238 eqyqgpdtdkrlaVLDEIAAETGATRNQLVYYWLMNRkpNAIPLIAATTDEQFKEALGSLELELS-EDM 305
Cdd:cd19071 194 -------------VLKEIAKKYGKTPAQVLLRWALQR--GVVVIPKSSNPERIKENLDVFDFELSeEDM 247
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-227 |
2.02e-31 |
|
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: 119.34 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 11 LQVSQMGLGCLYFGARDSKEKSFRR-MDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKERNN-----REDVI 84
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREaLKAALDSGINVIDTAINYRG--------GRSERLIGKALRELIEkggikRDEVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 85 IASKVGFPYPGTEYGTSKKQ---------------------------IKEECHKSLERLGTDYIDLYYAH---------- 127
Cdd:cd19099 73 IVTKAGYIPGDGDEPLRPLKyleeklgrglidvadsaglrhcispayLEDQIERSLKRLGLDTIDLYLLHnpeeqllelg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 128 TDDFNTPLEETLEAFNELITEGKVRAIG-ASNF-----KAWR----LERARQIAKQ-----NHWQsysAIQQRYSYLRPK 192
Cdd:cd19099 153 EEEFYDRLEEAFEALEEAVAEGKIRYYGiSTWDgfrapPALPghlsLEKLVAAAEEvggdnHHFK---VIQLPLNLLEPE 229
|
250 260 270
....*....|....*....|....*....|....*
gi 1001929468 193 SGWDFGDQVAANQDLFEFVEDTGISLVAYSPLLQG 227
Cdd:cd19099 230 ALTEKNTVKGEALSLLEAAKELGLGVIASRPLNQG 264
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-261 |
4.84e-31 |
|
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: 116.95 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 14 SQMGLGCLYFGARD---SKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqgGESEKMIGKWLKERNnREDVIIASKVG 90
Cdd:cd19095 1 SVLGLGTSGIGRVWgvpSEAEAARLLNTALDLGINLIDTAPAY----------GRSEERLGRALAGLR-RDDLFIATKVG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 91 --FPYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAwRLERAR 168
Cdd:cd19095 70 thGEGGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGE-ELEAAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 169 QiakqnhWQSYSAIQQRYSYLRPksgwdfgdqvaANQDLFEFVEDTGISLVAYSPLLQGAYTnpnKEFKEQYQGPDTDKR 248
Cdd:cd19095 149 A------SGVFDVVQLPYNVLDR-----------EEEELLPLAAEAGLGVIVNRPLANGRLR---RRVRRRPLYADYARR 208
|
250
....*....|...
gi 1001929468 249 LAVLDEIAAETGA 261
Cdd:cd19095 209 PEFAAEIGGATWA 221
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-299 |
7.08e-31 |
|
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: 118.34 E-value: 7.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGCLY-FGARDSKEKSFRRMDQYLAAGGNFLDTanmyshwiSDQTQGGESEKMIGKWLKERN- 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWStFSTAISEEQAEEIVTLAYENGINYFDT--------SDAFTSGQAETELGRILKKKGw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 79 NREDVIIASKVGFPYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASN 158
Cdd:cd19142 73 KRSSYIVSTKIYWSYGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 159 FKAWRLERARQIAKQNHWQSYSAIQQRYSYL-RPKsgwdfgdqvaANQDLFEFVEDTGISLVAYSPL------------- 224
Cdd:cd19142 153 WSPVEIMEAFSIARQFNCPTPICEQSEYHMFcREK----------MELYMPELYNKVGVGLITWSPLslgldpgiseetr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 225 --------LQGAYTNPNKEFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYW-LMNRKPNAIpLIAATTDEQFKEALG 295
Cdd:cd19142 223 rlvtklsfKSSKYKVGSDGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWsLKNENVQCV-LIGASSLEQLYSQLN 301
|
....
gi 1001929468 296 SLEL 299
Cdd:cd19142 302 SLQL 305
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
40-312 |
1.06e-30 |
|
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: 116.56 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYShwisdqtqggeSEKMIGKWLKERN-NREDVIIASKVGfpypgteygTSKKQIKEECHKSLERLGT 118
Cdd:cd19120 35 LKAGFRHIDTAEMYG-----------NEKEVGEALKESGvPREDLFITTKVS---------PGIKDPREALRKSLAKLGV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 119 DYIDLYYAH----TDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAKqnhwqSYSAIQQ--RYSYLRPK 192
Cdd:cd19120 95 DYVDLYLIHspffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK-----IKPAVNQieFHPYLYPQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 193 SgwdfgdqvaanQDLFEFVEDTGISLVAYSPLLqgaytnPnkefkeQYQGPDTDKrLAVLDEIAAETGATRNQLVYYWlm 272
Cdd:cd19120 170 Q-----------PALLEYCREHGIVVSAYSPLS------P------LTRDAGGPL-DPVLEKIAEKYGVTPAQVLLRW-- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1001929468 273 NRKPNAIPLIAATTDEQFKEALGSLELELSEDMLRAMTEA 312
Cdd:cd19120 224 ALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKA 263
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
7-306 |
1.47e-30 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; 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.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 117.17 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 7 GKTGLQVSQMGLGCLY-FG-------ARDSKEKSFRRmdqylaaGGNFLDTANMYShwisdqTQGGESEKMIGKWLKE-- 76
Cdd:cd19150 6 GKSGLKLPALSLGLWHnFGddtpletQRAILRTAFDL-------GITHFDLANNYG------PPPGSAEENFGRILREdf 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 77 RNNREDVIIASKVGF---PYPGTEYGtSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRA 153
Cdd:cd19150 73 AGYRDELIISTKAGYdmwPGPYGEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 154 IGASNFKAWRLERARQIAKQnhWQSYSAIQQ-RYSYLrpkSGWDFGDqvaanqDLFEFVEDTGISLVAYSPLLQGAYT-- 230
Cdd:cd19150 152 VGISSYSPERTREAAAILRE--LGTPLLIHQpSYNML---NRWVEES------GLLDTLQELGVGCIAFTPLAQGLLTdk 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 231 -----------NPNKEFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLE- 298
Cdd:cd19150 221 ylngipegsraSKERSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDn 300
|
....*...
gi 1001929468 299 LELSEDML 306
Cdd:cd19150 301 LTFSADEL 308
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
6-299 |
1.90e-29 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 114.08 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 6 LGKTGLQVSQMGLGC-LYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERN-NREDV 83
Cdd:cd19141 5 LGKSGLRVSCLGLGTwVTFGSQISDEVAEELVTLAYENGINLFDTAEVYA--------AGKAEIVLGKILKKKGwRRSSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 84 IIASKVgfpYPG----TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNF 159
Cdd:cd19141 77 VITTKI---FWGgkaeTERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 160 KAWRLERARQIAKQNHWQSYSAIQQRYSYLRPksgwdfgDQVAANqdLFEFVEDTGISLVAYSPL----LQGAYTNPNKE 235
Cdd:cd19141 154 SAMEIMEAYSVARQFNLIPPIVEQAEYHLFQR-------EKVEMQ--LPELFHKIGVGAMTWSPLacgiLSGKYDDGVPE 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001929468 236 F-----------KEQYQGPDTDKRLAVLDE---IAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLEL 299
Cdd:cd19141 225 YsraslkgyqwlKEKILSEEGRRQQAKLKElqiIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-307 |
2.92e-29 |
|
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: 112.35 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLyfgaRDSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERN-NREDVIIASK 88
Cdd:cd19140 5 GVRIPALGLGTY----PLTGEECTRAVEHALELGYRHIDTAQMY-----------GNEAQVGEAIAASGvPRDELFLTTK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 89 VGFPypgteyGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERAR 168
Cdd:cd19140 70 VWPD------NYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 169 QIAKqnhwQSYSAIQQRYS-YLrpksgwdfgDQVaanqDLFEFVEDTGISLVAYSPLLQG-AYTNPnkefkeqyqgpdtd 246
Cdd:cd19140 144 ELSE----APLFTNQVEYHpYL---------DQR----KLLDAAREHGIALTAYSPLARGeVLKDP-------------- 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001929468 247 krlaVLDEIAAETGATRNQLVYYWLMnRKPNAIPLIAATTDEQFKEALGSLELELS-EDMLR 307
Cdd:cd19140 193 ----VLQEIGRKHGKTPAQVALRWLL-QQEGVAAIPKATNPERLEENLDIFDFTLSdEEMAR 249
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-275 |
9.76e-29 |
|
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: 112.36 E-value: 9.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 6 LGKTGLQVSQMGLGCLYFGA---RDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKErnNRED 82
Cdd:cd19104 5 FGRTGLKVSELTFGGGGIGGlmgRTTREEQIAAVRRALDLGINFFDTAPSYG--------DGKSEENLGRALKG--LPAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 83 VIIASKVGFPypGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAH----------------TDDFNTPlEETLEAFNELI 146
Cdd:cd19104 75 PYITTKVRLD--PDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHnrigderdkpvggtlsTTDVLGL-GGVADAFERLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 147 TEGKVRAIGasnFKAWRLERA-RQIAKQNHWqsySAIQQRYSYLRPKSGW---------DFGD--QVAANQdlfefvedt 214
Cdd:cd19104 152 SEGKIRFIG---ITGLGNPPAiRELLDSGKF---DAVQVYYNLLNPSAAEarprgwsaqDYGGiiDAAAEH--------- 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001929468 215 GISLVAYSPLLQGAYTNP---NKEFKEQYQGPDT-DKRLAV-LDEIAAETGATRNQLVY-YWLMNRK 275
Cdd:cd19104 217 GVGVMGIRVLAAGALTTSldrGREAPPTSDSDVAiDFRRAAaFRALAREWGETLAQLAHrFALSNPG 283
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-155 |
1.29e-28 |
|
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: 111.49 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGCLYFGA--RD-SKEKSFRRMDQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKER 77
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGvfGPvDEEEAIRTVHEALDSGINYIDTAPWYGQ--------GRSETVLGKALKGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 78 nNREDVIIASKVG--FPYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAH----TDDFNTPLEETLEAFNELITEGKV 151
Cdd:cd19163 73 -PRDSYYLATKVGryGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEEGKV 151
|
....
gi 1001929468 152 RAIG 155
Cdd:cd19163 152 RFIG 155
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-304 |
3.51e-28 |
|
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: 109.95 E-value: 3.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 14 SQMGLGCLYFGARD---SKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqgGESEKMIGKWLKErNNREDVIIASKVG 90
Cdd:cd19090 1 SALGLGTAGLGGVFggvDDDEAVATIRAALDLGINYIDTAPAY----------GDSEERLGLALAE-LPREPLVLSTKVG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 91 fPYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAH-----TDDFNTPLEETLEAFNELITEGKVRAIGASnfkAWRLE 165
Cdd:cd19090 70 -RLPEDTADYSADRVRRSVEESLERLGRDRIDLLMIHdpervPWVDILAPGGALEALLELKEEGLIKHIGLG---GGPPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 166 RARQIAKQNHwqsYSAI--QQRYSYLrpksgwdfgDQVAAnQDLFEFVEDTGISLVAYSPLLQGAYTNPNKEF---KEQY 240
Cdd:cd19090 146 LLRRAIETGD---FDVVltANRYTLL---------DQSAA-DELLPAAARHGVGVINASPLGMGLLAGRPPERvryTYRW 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001929468 241 QGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELSED 304
Cdd:cd19090 213 LSPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-299 |
5.57e-28 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 110.52 E-value: 5.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGC-LYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERN- 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--------AGKAEVILGSIIKKKGw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 79 NREDVIIASKVgfpYPG----TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAI 154
Cdd:cd19159 73 RRSSLVITTKL---YWGgkaeTERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 155 GASNFKAWRLERARQIAKQNHWQSYSAIQQRYS-YLRPKsgwdfgdqvaANQDLFEFVEDTGISLVAYSPL----LQGAY 229
Cdd:cd19159 150 GTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHlFQREK----------VEVQLPELYHKIGVGAMTWSPLacgiISGKY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 230 TN--PNKE---------FKEQYQGPDTDKRLAVLDE---IAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALG 295
Cdd:cd19159 220 GNgvPESSraslkcyqwLKERIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLG 299
|
....
gi 1001929468 296 SLEL 299
Cdd:cd19159 300 AIQV 303
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-299 |
5.81e-28 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 110.46 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGC-LYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERN- 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYA--------AGKAERTLGNILKSKGw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 79 NREDVIIASKVgfpYPG----TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAI 154
Cdd:cd19160 75 RRSSYVVTTKI---YWGgqaeTERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 155 GASNFKAWRLERARQIAKQNHWQSYSAIQQRYSYLRPKSgwdfgdqvaANQDLFEFVEDTGISLVAYSP----LLQGAYT 230
Cdd:cd19160 152 GTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREK---------VEMQLPELYHKIGVGSVTWSPlacgLITGKYD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 231 N--PNKE---------FKEQYQGPDTDKRLAVLDE---IAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGS 296
Cdd:cd19160 223 GrvPDTCraavkgyqwLKEKVQSEEGKKQQAKVKElhpIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGS 302
|
...
gi 1001929468 297 LEL 299
Cdd:cd19160 303 IQV 305
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
7-309 |
8.04e-28 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 110.46 E-value: 8.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 7 GKTGLQVSQMGLGCLY-FG---ARDSKEKSFRRMdqyLAAGGNFLDTANMYShwisdqTQGGESEKMIGKWLKE--RNNR 80
Cdd:PRK09912 19 GKSGLRLPALSLGLWHnFGhvnALESQRAILRKA---FDLGITHFDLANNYG------PPPGSAEENFGRLLREdfAAYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 81 EDVIIASKVGFP-YPGTeYGT--SKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGAS 157
Cdd:PRK09912 90 DELIISTKAGYDmWPGP-YGSggSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGIS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 158 NFKAWRLERARQIAKQnhWQSYSAIQQ-RYSYLR---PKSGwdfgdqvaanqdLFEFVEDTGISLVAYSPLLQGAYT--- 230
Cdd:PRK09912 169 SYSPERTQKMVELLRE--WKIPLLIHQpSYNLLNrwvDKSG------------LLDTLQNNGVGCIAFTPLAQGLLTgky 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 231 --------------NPNKEFKEQYQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGS 296
Cdd:PRK09912 235 lngipqdsrmhregNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQA 314
|
330
....*....|....
gi 1001929468 297 LE-LELSEDMLRAM 309
Cdd:PRK09912 315 LNnLTFSTEELAQI 328
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-299 |
5.75e-24 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 99.77 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLGKTGLQVSQMGLGC-LYFGARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERN- 78
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA--------AGKAEVVLGNIIKKKGw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 79 NREDVIIASKVGFPYPG-TEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELITEGKVRAIGAS 157
Cdd:cd19158 73 RRSSLVITTKIFWGGKAeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 158 NFKAWRLERARQIAKQNHWQSYSAIQQRYSYLRPKSgwdfgdqvaANQDLFEFVEDTGISLVAYSPL----LQGAYTNPN 233
Cdd:cd19158 153 RWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREK---------VEVQLPELFHKIGVGAMTWSPLacgiVSGKYDSGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 234 KEFKEQ----YQ----------GPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLEL 299
Cdd:cd19158 224 PPYSRAslkgYQwlkdkilseeGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 303
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-305 |
2.19e-23 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 97.48 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 1 MKKVQLgKTGLQVSQMGLGCLyfgaRDSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqGGESEkmIGKWLKERNN- 79
Cdd:cd19123 1 MKTLPL-SNGDLIPALGLGTW----KSKPGEVGQAVKQALEAGYRHIDCAAIY---------GNEAE--IGAALAEVFKe 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 80 ----REDVIIASKVgfpypgteYGTS--KKQIKEECHKSLERLGTDYIDLYYAH--------------TDDF----NTPL 135
Cdd:cd19123 65 gkvkREDLWITSKL--------WNNShaPEDVLPALEKTLADLQLDYLDLYLMHwpvalkkgvgfpesGEDLlslsPIPL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 136 EETLEAFNELITEGKVRAIGASNFKAWRLE----RARQIAKQNHWQSYSAIQQRysylrpksgwdfgdqvaanqDLFEFV 211
Cdd:cd19123 137 EDTWRAMEELVDKGLCRHIGVSNFSVKKLEdllaTARIKPAVNQVELHPYLQQP--------------------ELLAFC 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 212 EDTGISLVAYSPLLQGaytNPNKEFKEQyqgpDTDKRLA--VLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQ 289
Cdd:cd19123 197 RDNGIHLTAYSPLGSG---DRPAAMKAE----GEPVLLEdpVINKIAEKHGASPAQVLIAWAIQRGTVVIP--KSVNPER 267
|
330
....*....|....*..
gi 1001929468 290 FKEALGSLELELSE-DM 305
Cdd:cd19123 268 IQQNLEAAEVELDAsDM 284
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
37-304 |
4.42e-23 |
|
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: 96.63 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 37 DQYLAAGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKERNnREDVIIASKvgfpYPGTEYGTSKKQIKEECHKSLERL 116
Cdd:cd19103 39 DKAMAAGLNLWDTAAVYGM--------GASEKILGEFLKRYP-REDYIISTK----FTPQIAGQSADPVADMLEGSLARL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 117 GTDYIDLYYAH-TDDfntpLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAKQNHWqSYSAIQQRYSYLRpKSGW 195
Cdd:cd19103 106 GTDYIDIYWIHnPAD----VERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAKAGV-SLSAVQNHYSLLY-RSSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 196 DFGdqvaanqdLFEFVEDTGISLVAYSPLLQGAYT------NPNKEF---KEQYQG--PDTDKRLAVLDEIAAETGATRN 264
Cdd:cd19103 180 EAG--------ILDYCKENGITFFAYMVLEQGALSgkydtkHPLPEGsgrAETYNPllPQLEELTAVMAEIGAKHGASIA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1001929468 265 QLVYYWLMNRkpNAIPLIAATTDEQFKEALGSLELELSED 304
Cdd:cd19103 252 QVAIAWAIAK--GTTPIIGVTKPHHVEDAARAASITLTDD 289
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-298 |
1.33e-22 |
|
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: 94.52 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYshwisdqtqgGESEKMIGKWLKernNREDVIIASKVgfPYPGTEYGTSKKQIKEECHKSLERLGTD 119
Cdd:cd19097 36 LKAGINTLDTAPAY----------GDSEKVLGKFLK---RLDKFKIITKL--PPLKEDKKEDEAAIEASVEASLKRLKVD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 120 YIDLYYAH-TDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAKqnhwqsYSAIQQRYSYLrpksgwdfg 198
Cdd:cd19097 101 SLDGLLLHnPDDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFK------IDIIQLPFNIL--------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 199 DQVAANQDLFEFVEDTGISLVAYSPLLQGAYTNPNKEFKEqyQGPDTDKRLAVLDEIAAETGATRNQLVYYWLMNRKPNA 278
Cdd:cd19097 166 DQRFLKSGLLAKLKKKGIEIHARSVFLQGLLLMEPDKLPA--KFAPAKPLLKKLHELAKKLGLSPLELALGFVLSLPEID 243
|
250 260
....*....|....*....|
gi 1001929468 279 IPLIAATTDEQFKEALGSLE 298
Cdd:cd19097 244 KIVVGVDSLEQLKEIIAAFK 263
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
36-313 |
5.39e-22 |
|
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: 93.33 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 36 MDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGK----WLKE-RNNREDVIIASKVgfpypgTEYGTSKKQIKEECH 110
Cdd:cd19111 23 VDYALFVGYRHIDTALSY-----------QNEKAIGEalkwWLKNgKLKREEVFITTKL------PPVYLEFKDTEKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 111 KSLERLGTDYIDLYYAH-------------TDDFNTPLEETLEAFNELITEGKVRAIGASNF------KAWRLERARQIA 171
Cdd:cd19111 86 KSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFnprqinKILAYAKVKPSN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 172 KQNHWQSYsaIQQRysylrpksgwdfgdqvaanqDLFEFVEDTGISLVAYSPLlqGAYTNPNKeFKEQYQgPDTDKRLAV 251
Cdd:cd19111 166 LQLECHAY--LQQR--------------------ELRKFCNKKNIVVTAYAPL--GSPGRANQ-SLWPDQ-PDLLEDPTV 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001929468 252 LdEIAAETGATRNQLVYYWLMNRkpNAIPLIAATTDEQFKEALGSLELELSEDMLRAMTEAK 313
Cdd:cd19111 220 L-AIAKELDKTPAQVLLRFVLQR--GTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLD 278
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
40-306 |
3.94e-21 |
|
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: 91.32 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERNN-----REDVIIASKVGFPYpgteygTSKKQIKEECHKSLE 114
Cdd:cd19154 35 LKAGYRLIDTAFLY-----------QNEEAIGEALAELLEegvvkREDLFITTKLWTHE------HAPEDVEEALRESLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 115 RLGTDYIDLYYAH--------TDDFNT-----------PLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAK--- 172
Cdd:cd19154 98 KLQLEYVDLYLIHapaafkddEGESGTmengmsihdavDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARvkp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 173 -QNHWQSYSAIQQrysylrpksgwdfgdqvaanQDLFEFVEDTGISLVAYSPLLQGAYTNPNKEFKEQYQGPDTDKrlAV 251
Cdd:cd19154 178 hNNQVECHLYFPQ--------------------KELVEFCKKHNISVTSYATLGSPGRANFTKSTGVSPAPNLLQD--PI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001929468 252 LDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELS-EDML 306
Cdd:cd19154 236 VKAIAEKHGKTPAQVLLRYLLQRGIAVIP--KSATPSRIKENFNIFDFSLSeEDMA 289
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
17-307 |
7.77e-20 |
|
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: 86.92 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 17 GLGClyFGARDSKEkSFRRMDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKE-----RNNREDVIIASKVGf 91
Cdd:cd19136 5 GLGT--FRLRGEEE-VRQAVDAALKAGYRLIDTASVY-----------RNEADIGKALRDllpkyGLSREDIFITSKLA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 92 PYpgtEYGTSKKQikEECHKSLERLGTDYIDLYYAH---------TDDFNTPLE-ETLEAFNELITEGKVRAIGASNFKA 161
Cdd:cd19136 70 PK---DQGYEKAR--AACLGSLERLGTDYLDLYLIHwpgvqglkpSDPRNAELRrESWRALEDLYKEGKLRAIGVSNYTV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 162 WRLERARQiakqnhwqsysaiqqrYSYLRPksgwdfgdqvAANQ----------DLFEFVEDTGISLVAYSPLLQGAY-- 229
Cdd:cd19136 145 RHLEELLK----------------YCEVPP----------AVNQvefhphlvqkELLKFCKDHGIHLQAYSSLGSGDLrl 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 230 -TNPnkefkeqyqgpdtdkrlAVLdEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELS-EDMLR 307
Cdd:cd19136 199 lEDP-----------------TVL-AIAKKYGRTPAQVLLRWALQQGIGVIP--KSTNPERIAENIKVFDFELSeEDMAE 258
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
67-305 |
1.03e-19 |
|
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: 86.61 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 67 EKMIGKWLKERN-NREDVIIASKVgFPypgTEYGTSKkqIKEECHKSLERLGTDYIDLYYAH-------TDDFNTPLEET 138
Cdd:cd19135 52 EELLGKAIKESGvPREDLFLTTKL-WP---SDYGYES--TKQAFEASLKRLGVDYLDLYLLHwpdcpssGKNVKETRAET 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 139 LEAFNELITEGKVRAIGASNFKAWRLERARQIAK-QNHwqsysAIQQRYS-YLRPksgwdfgdqvaanQDLFEFVEDTGI 216
Cdd:cd19135 126 WRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSvVPH-----VNQVEFHpFQNP-------------VELIEYCRDNNI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 217 SLVAYSPLLQG-AYTNPNkefkeqyqgpdtdkrlavLDEIAAETGATRNQLVYYWLMNrkpNAIPLIAATTD-EQFKEAL 294
Cdd:cd19135 188 VFEGYCPLAKGkALEEPT------------------VTELAKKYQKTPAQILIRWSIQ---NGVVTIPKSTKeERIKENC 246
|
250
....*....|..
gi 1001929468 295 GSLELELS-EDM 305
Cdd:cd19135 247 QVFDFSLSeEDM 258
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
40-313 |
6.51e-19 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 84.70 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKER-----NNREDVIIASKVGFPYpgteygTSKKQIKEECHKSLE 114
Cdd:cd19125 34 IKEGYRHIDCAAIY-----------GNEKEIGKALKKLfedgvVKREDLFITSKLWCTD------HAPEDVPPALEKTLK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 115 RLGTDYIDLYYAH--------TDDFN------TPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAKQNhwqsyS 180
Cdd:cd19125 97 DLQLDYLDLYLIHwpvrlkkgAHMPEpeevlpPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVARVP-----P 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 181 AIQQrySYLRPksGWdfgdqvaANQDLFEFVEDTGISLVAYSPLlqgayTNPNKEFKeqyqgpdTDKRLA--VLDEIAAE 258
Cdd:cd19125 172 AVNQ--VECHP--GW-------QQDKLHEFCKSKGIHLSAYSPL-----GSPGTTWV-------KKNVLKdpIVTKVAEK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1001929468 259 TGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELSEDMLRAMTEAK 313
Cdd:cd19125 229 LGKTPAQVALRWGLQRGTSVLP--KSTNEERIKENIDVFDWSIPEEDFAKFSSIE 281
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-194 |
1.44e-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: 84.12 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 6 LGKTGLQVSQMGLGCLYFG-------ARDSKEKSFRrmdQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKE-R 77
Cdd:cd19153 5 LEIALGNVSPVGLGTAALGgvygdglEQDEAVAIVA---EAFAAGINHFDTSPYYG--------AESSEAVLGKALAAlQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 78 NNREDVIIASKVGfPYPGTEYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDF---NTPLEETLEAFNELITEGKVRAI 154
Cdd:cd19153 74 VPRSSYTVATKVG-RYRDSEFDYSAERVRASVATSLERLHTTYLDVVYLHDIEFvdyDTLVDEALPALRTLKDEGVIKRI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001929468 155 GAS----NFKAWRLERArQIAKQNHWQSY-------SAIQQRYSYLRPKSG 194
Cdd:cd19153 153 GIAgyplDTLTRATRRC-SPGSLDAVLSYchltlqdARLESDAPGLVRGAG 202
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
32-307 |
1.56e-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: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 32 SFRRMDQY--------LAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKE-RNNREDVIIASKVgfpypgTEYGTSK 102
Cdd:cd19139 8 TFRLKDDVvidsvrtaLELGYRHIDTAQIY-----------DNEAAVGQAIAEsGVPRDELFITTKI------WIDNLSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 103 KQIKEECHKSLERLGTDYIDLYYAH---TDDfNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAKqnhwqsy 179
Cdd:cd19139 71 DKLLPSLEESLEKLRTDYVDLTLIHwpsPND-EVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVG------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 180 saiqqrysylrpksgwdfGDQVAANQ----------DLFEFVEDTGISLVAYSPLLQGaytnpnKEFKEQyqgpdtdkrl 249
Cdd:cd19139 143 ------------------AGAIATNQielspylqnrKLVAHCKQHGIHVTSYMTLAYG------KVLDDP---------- 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001929468 250 aVLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELS-EDMLR 307
Cdd:cd19139 189 -VLAAIAERHGATPAQIALAWAMARGYAVIP--SSTKREHLRSNLLALDLTLDaDDMAA 244
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
42-309 |
2.02e-18 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 83.49 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 42 AGGNFLDTANMYshwisdqtqggESEKMIGKWLKE---RNN--REDVIIASKVGFPYPgteygtSKKQIKEECHKSLERL 116
Cdd:cd19116 37 AGYRHIDTAYLY-----------GNEAEVGEAIREkiaEGVvkREDLFITTKLWNSYH------EREQVEPALRESLKRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 117 GTDYIDLYYAHT-------DDFNTPLE---------ETLEAFNELITEGKVRAIGASNFKAWRLERARQiakqnhwqsys 180
Cdd:cd19116 100 GLDYVDLYLIHWpvafkenNDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLS----------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 181 aiqqrYSYLRPksgwdfgdqvAANQ----------DLFEFVEDTGISLVAYSPLLQgaytnPNKEFKeqyQGPDTDKRLA 250
Cdd:cd19116 169 -----NCNIKP----------AVNQievhptltqeKLVAYCQSNGIVVMAYSPFGR-----LVPRGQ---TNPPPRLDDP 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001929468 251 VLDEIAAETGATRNQLVYYWLMNRkpNAIPLIAATTDEQFKEALGSLELELSEDMLRAM 309
Cdd:cd19116 226 TLVAIAKKYGKTTAQIVLRYLIDR--GVVPIPKSSNKKRIKENIDIFDFQLTPEEVAAL 282
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
10-305 |
2.17e-18 |
|
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: 83.21 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGClyFGARDSKEkSFRRMDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERN-NREDVIIASK 88
Cdd:cd19157 7 GVKMPWLGLGV--FKVEEGSE-VVNAVKTALKNGYRSIDTAAIY-----------GNEEGVGKGIKESGiPREELFITSK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 89 VGFPYPGteYGTSKKQIKEechkSLERLGTDYIDLYYAHTddfntPLE----ETLEAFNELITEGKVRAIGASNFKAWRL 164
Cdd:cd19157 73 VWNADQG--YDSTLKAFEA----SLERLGLDYLDLYLIHW-----PVKgkykETWKALEKLYKDGRVRAIGVSNFQVHHL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 165 ERARQIAKqnhwqSYSAIQQrySYLRPKsgwdfgdqvAANQDLFEFVEDTGISLVAYSPLLQG-AYTNPnkefkeqyqgp 243
Cdd:cd19157 142 EDLLADAE-----IVPMVNQ--VEFHPR---------LTQKELRDYCKKQGIQLEAWSPLMQGqLLDNP----------- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001929468 244 dtdkrlaVLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELS-EDM 305
Cdd:cd19157 195 -------VLKEIAEKYNKSVAQVILRWDLQNGVVTIP--KSIKEHRIIENADVFDFELSqEDM 248
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-239 |
1.08e-17 |
|
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: 80.68 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 14 SQMGLGCLYFGARDSKEKSFRRM----DQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERNnREDVIIASKV 89
Cdd:cd19096 1 SVLGFGTMRLPESDDDSIDEEKAiemiRYAIDAGINYFDTAYGYG--------GGKSEEILGEALKEGP-REKFYLATKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 90 GfPYPGTEYGTSKKQIKEechkSLERLGTDYIDLYYAH-----TDDFNTPLEETLEAFNELITEGKVRAIGASnFKAwRL 164
Cdd:cd19096 72 P-PWSVKSAEDFRRILEE----SLKRLGVDYIDFYLLHglnspEWLEKARKGGLLEFLEKAKKEGLIRHIGFS-FHD-SP 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001929468 165 ERARQIAKQNHWqsySAIQQRYSYLRPKSGwdfgdqvaANQDLFEFVEDTGISLVAYSPLLQGAYTNPNKEFKEQ 239
Cdd:cd19096 145 ELLKEILDSYDF---DFVQLQYNYLDQENQ--------AGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAI 208
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-310 |
1.24e-17 |
|
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: 80.56 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLYFGARDSKEKSFRRMdqyLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERN-NREDVIIASK 88
Cdd:cd19126 6 GTRMPWLGLGVFQTPDGDETERAVQTA---LENGYRSIDTAAIY-----------KNEEGVGEAIRESGvPREELFVTTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 89 VGFPYPGTEYGtskkqiKEECHKSLERLGTDYIDLYYAH---TDDFntplEETLEAFNELITEGKVRAIGASNFKAWRLE 165
Cdd:cd19126 72 LWNDDQRARRT------EDAFQESLDRLGLDYVDLYLIHwpgKDKF----IDTWKALEKLYASGKVKAIGVSNFQEHHLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 166 R----ARQIAKQNHWQSYSAIQQrysylrpksgwdfgdqvaanQDLFEFVEDTGISLVAYSPLLQGaytnpnkefkeqyq 241
Cdd:cd19126 142 EllahADVVPAVNQVEFHPYLTQ--------------------KELRGYCKSKGIVVEAWSPLGQG-------------- 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1001929468 242 GPDTDKRLAvldEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELSEDMLRAMT 310
Cdd:cd19126 188 GLLSNPVLA---AIGEKYGKSAAQVVLRWDIQHGVVTIP--KSVHASRIKENADIFDFELSEDDMTAID 251
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-227 |
4.84e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 79.95 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 24 GARDSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqgGESEKMIGKWLK----ERNNREDVIIASKVgFPYPGtEYG 99
Cdd:cd19101 17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIY----------GPAEELIGEFRKrlrrERDAADDVQIHTKW-VPDPG-ELT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 100 TSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTP-LEETLEAFNELITEGKVRAIGASNFKAWRLeraRQIAKQ----- 173
Cdd:cd19101 85 MTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERL---REILDAgvpiv 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1001929468 174 -NHWQsYSAIQQrysylRPKSGwdfgdqvaanqdLFEFVEDTGISLVAYSPLLQG 227
Cdd:cd19101 162 sNQVQ-YSLLDR-----RPENG------------MAALCEDHGIKLLAYGTLAGG 198
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-311 |
6.57e-17 |
|
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: 78.99 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLyfgaRDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqggeSEKMIGKWLKERN-NREDVIIASK 88
Cdd:cd19127 6 GVEMPALGLGVF----QTPPEETADAVATALADGYRLIDTAAAYG-----------NEREVGEGIRRSGvDRSDIFVTTK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 89 VGFpypgTEYGTSKKQIKEEchKSLERLGTDYIDLYYAH---TDDFNTPLEeTLEAFNELITEGKVRAIGASNFKAWRLE 165
Cdd:cd19127 71 LWI----SDYGYDKALRGFD--ASLRRLGLDYVDLYLLHwpvPNDFDRTIQ-AYKALEKLLAEGRVRAIGVSNFTPEHLE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 166 RArqIAKQNhwqSYSAIQQrySYLRPksgwdfgdqVAANQDLFEFVEDTGISLVAYSPLlqGAYTNpnkefkeqYQGPDT 245
Cdd:cd19127 144 RL--IDATT---VVPAVNQ--VELHP---------YFSQKDLRAFHRRLGIVTQAWSPI--GGVMR--------YGASGP 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001929468 246 DKRLAVLD-----EIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELSEDMLRAMTE 311
Cdd:cd19127 198 TGPGDVLQdptitGLAEKYGKTPAQIVLRWHLQNGVSAIP--KSVHPERIAENIDIFDFALSAEDMAAIDA 266
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-224 |
1.25e-16 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 78.55 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 14 SQMGLGCLYFG--ARDSKEKSFRRMDQYLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKeRNNREDVIIASKVG- 90
Cdd:cd19162 1 PRLGLGAASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYG--------LGLSERRLGAALA-RHPRAEYVVSTKVGr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 91 ---FPYPGTEYGT------SKKQIKEECHKSLERLGTDYIDLYYAH--TDDFNTPLEETLEAFNELITEGKVRAIGASNf 159
Cdd:cd19162 72 llePGAAGRPAGAdrrfdfSADGIRRSIEASLERLGLDRLDLVFLHdpDRHLLQALTDAFPALEELRAEGVVGAIGVGV- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001929468 160 KAWRLerARQIAKQNHWQSYsAIQQRYSYLRPksgwdfgdqvAANQDLFEFVEDTGISLVAYSPL 224
Cdd:cd19162 151 TDWAA--LLRAARRADVDVV-MVAGRYTLLDR----------RAATELLPLCAAKGVAVVAAGVF 202
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
28-311 |
1.70e-16 |
|
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: 78.34 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 28 SKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKE-----RNNREDVIIASKVgfPYPGTEYGTSK 102
Cdd:cd19155 23 SPEEIETAVDTALEAGYRHIDTAYVY-----------RNEAAIGNVLKKwidsgKVKREELFIVTKL--PPGGNRREKVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 103 KQIKeechKSLERLGTDYIDLYYAHTD---------------------DFNTPLEETLEAFNELITEGKVRAIGASNFKA 161
Cdd:cd19155 90 KFLL----KSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 162 WRLERARQIAK----QNHWQSYSAIQQRysylrpksgwdfgdqvaanqDLFEFVEDTGISLVAYSPLLQGAYTNpnkeFK 237
Cdd:cd19155 166 EQMARILKNARikpaNLQVELHVYLQQK--------------------DLVDFCSTHSITVTAYAPLGSPGAAH----FS 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001929468 238 EQYQGPDTDK----RLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELSEDMLRAMTE 311
Cdd:cd19155 222 PGTGSPSGSSpdllQDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIP--KSTNAARIKENFQVFDFELTEADMAKLSS 297
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
40-157 |
2.80e-16 |
|
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: 77.70 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYshwisdqtqgGESEKMIGKWLKE-RNN--REDVIIASKVGfPYPGTEYGTSKKQIKEECHKSLERL 116
Cdd:cd19164 44 LELGIRAFDTSPYY----------GPSEIILGRALKAlRDEfpRDTYFIITKVG-RYGPDDFDYSPEWIRASVERSLRRL 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1001929468 117 GTDYIDLYYAHTDDFNTPlEETLEAFNELIT---EGKVRAIGAS 157
Cdd:cd19164 113 HTDYLDLVYLHDVEFVAD-EEVLEALKELFKlkdEGKIRNVGIS 155
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-310 |
4.23e-16 |
|
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: 76.26 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLyfgaRDSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERN-NREDVIIASK 88
Cdd:cd19131 7 GNTIPQLGLGVW----QVSNDEAASAVREALEVGYRSIDTAAIY-----------GNEEGVGKAIRASGvPREELFITTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 89 VgfpYPGTEYGTSKKQIKEEchkSLERLGTDYIDLYYAHtddFNTPLE----ETLEAFNELITEGKVRAIGASNFKAWRL 164
Cdd:cd19131 72 L---WNSDQGYDSTLRAFDE---SLRKLGLDYVDLYLIH---WPVPAQdkyvETWKALIELKKEGRVKSIGVSNFTIEHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 165 ER----ARQIAKQNHWQSYSAIQQRysylrpksgwdfgdqvaanqDLFEFVEDTGISLVAYSPLLQG-AYTNPnkefkeq 239
Cdd:cd19131 143 QRlideTGVVPVVNQIELHPRFQQR--------------------ELRAFHAKHGIQTESWSPLGQGgLLSDP------- 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001929468 240 yqgpdtdkrlaVLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELSEDMLRAMT 310
Cdd:cd19131 196 -----------VIGEIAEKHGKTPAQVVIRWHLQNGLVVIP--KSVTPSRIAENFDVFDFELDADDMQAIA 253
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
36-310 |
8.73e-16 |
|
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: 75.38 E-value: 8.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 36 MDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERN-NREDVIIASKVgfpyPGTEYGtsKKQIKEECHKSLE 114
Cdd:cd19132 26 VVAALQAGYRLLDTAFNY-----------ENEGAVGEAVRRSGvPREELFVTTKL----PGRHHG--YEEALRTIEESLY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 115 RLGTDYIDLYYAHTddfntPLE------ETLEAFNELITEGKVRAIGASNFKAWRLERARQiakqnHWQSYSAIQQrySY 188
Cdd:cd19132 89 RLGLDYVDLYLIHW-----PNPsrdlyvEAWQALIEAREEGLVRSIGVSNFLPEHLDRLID-----ETGVTPAVNQ--IE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 189 LRPksGWDFGDQVAANQDLfefvedtGISLVAYSPLLQGaytnpNKEFKEQyqgpdtdkrlaVLDEIAAETGATRNQLVY 268
Cdd:cd19132 157 LHP--YFPQAEQRAYHREH-------GIVTQSWSPLGRG-----SGLLDEP-----------VIKAIAEKHGKTPAQVVL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1001929468 269 YWLMNRkpNAIPLIAATTDEQFKEALGSLELELSEDMLRAMT 310
Cdd:cd19132 212 RWHVQL--GVVPIPKSANPERQRENLAIFDFELSDEDMAAIA 251
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-307 |
6.18e-15 |
|
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: 72.99 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLYFGARDSKEKSfrrMDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERN-NREDVIIASK 88
Cdd:cd19133 6 GVEMPILGFGVFQIPDPEECERA---VLEAIKAGYRLIDTAAAY-----------GNEEAVGRAIKKSGiPREELFITTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 89 VGFPypGTEYGTSKKQIkeecHKSLERLGTDYIDLYYAHT---DDFntpleETLEAFNELITEGKVRAIGASNFKAwrlE 165
Cdd:cd19133 72 LWIQ--DAGYEKAKKAF----ERSLKRLGLDYLDLYLIHQpfgDVY-----GAWRAMEELYKEGKIRAIGVSNFYP---D 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 166 RARQIAKQNHwqsysaiqqrysyLRPksgwdfgdqvAANQ----------DLFEFVEDTGISLVAYSPLLQG---AYTNP 232
Cdd:cd19133 138 RLVDLILHNE-------------VKP----------AVNQiethpfnqqiEAVEFLKKYGVQIEAWGPFAEGrnnLFENP 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001929468 233 nkefkeqyqgpdtdkrlaVLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELS-EDMLR 307
Cdd:cd19133 195 ------------------VLTEIAEKYGKSVAQVILRWLIQRGIVVIP--KSVRPERIAENFDIFDFELSdEDMEA 250
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-274 |
1.21e-14 |
|
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: 73.04 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 9 TGLQVSQMGLGClyFGARDSKEKSFRRMDQYLAAGGNFLDTANMYSHwisdqtqGGESEKMIGKWLKERNN--REDVIIA 86
Cdd:cd19122 5 NGVKIPAVGFGT--FANEGAKGETYAAVTKALDVGYRHLDCAWFYLN-------EDEVGDAVRDFLKENPSvkREDLFIC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 87 SKVgfpypgTEYGTSKKQIKEECHKSLERLGTDYIDLYYAH------TDDFNTPL-----------------EETLEAFN 143
Cdd:cd19122 76 TKV------WNHLHEPEDVKWSIDNSLKNLKLDYIDLFLVHwpiaaeKNDQRSPKlgpdgkyvilkdltenpEPTWRAME 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 144 ELITEGKVRAIGASNFKAWRLERARQIAKqnhwqsysaiqqrysyLRPKSGWDFGDQVAANQDLFEFVEDTGISLVAYSP 223
Cdd:cd19122 150 EIYESGKAKAIGVSNWTIPGLKKLLSFAK----------------VKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSP 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1001929468 224 LlqgaytnpnkefKEQYQGPDTDKRLA---VLDEIAAETGATRNQLVYYWLMNR 274
Cdd:cd19122 214 L------------GSQNQVPSTGERVSenpTLNEVAEKGGYSLAQVLIAWGLRR 255
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
5-157 |
1.46e-14 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 72.89 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 5 QLGKTGLQVSQMGLGCLYFG------ARDSKEKSFRRMdqyLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERN 78
Cdd:PLN02587 3 ELGSTGLKVSSVGFGASPLGsvfgpvSEEDAIASVREA---FRLGINFFDTSPYYG--------GTLSEKVLGKALKALG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 79 -NREDVIIASKVGFPYPGTEYgtSKKQIKEECHKSLERLGTDYIDLYYAHTDDF---NTPLEETLEAFNELITEGKVRAI 154
Cdd:PLN02587 72 iPREKYVVSTKCGRYGEGFDF--SAERVTKSVDESLARLQLDYVDILHCHDIEFgslDQIVNETIPALQKLKESGKVRFI 149
|
...
gi 1001929468 155 GAS 157
Cdd:PLN02587 150 GIT 152
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-280 |
1.72e-14 |
|
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: 72.15 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 9 TGLQVSQMGLGClYFGARDSKEKSfrrMDQYLAAGGNFLDTAnmyshWISDqtqggeSEKMIGKWLKERN-NREDVIIAS 87
Cdd:cd19117 10 TGAEIPAVGLGT-WQSKPNEVAKA---VEAALKAGYRHIDTA-----AIYG------NEEEVGQGIKDSGvPREEIFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 88 KVgfpypgteYGTSKKQIKEECHKSLERLGTDYIDLYYAH-------TDDFNTPLEE--------------TLEAFNELI 146
Cdd:cd19117 75 KL--------WCTWHRRVEEALDQSLKKLGLDYVDLYLMHwpvpldpDGNDFLFKKDdgtkdhepdwdfikTWELMQKLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 147 TEGKVRAIGASNFKAWRLER--ARQIAKqnhwqsysaiqqrysyLRPksgwdfgdqvAANQ----------DLFEFVEDT 214
Cdd:cd19117 147 ATGKVKAIGVSNFSIKNLEKllASPSAK----------------IVP----------AVNQielhpllpqpKLVDFCKSK 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001929468 215 GISLVAYSPLlqGAYTNPnkEFKEQyqgpdtdkrlaVLDEIAAETGATRNQLVYYWLMNRKPNAIP 280
Cdd:cd19117 201 GIHATAYSPL--GSTNAP--LLKEP-----------VIIKIAKKHGKTPAQVIISWGLQRGYSVLP 251
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
40-309 |
1.06e-13 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 70.00 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYSHWISDQtqggesekMIGKWLkeRNNREDVIIASKVGFPYpGTEYG----TSKKQIKEECHKSLER 115
Cdd:PRK10376 50 VALGVNHIDTSDFYGPHVTNQ--------LIREAL--HPYPDDLTIVTKVGARR-GEDGSwlpaFSPAELRRAVHDNLRN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 116 LGTDYID-----LYYAHTDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAK----QNHWQsysaiqqry 186
Cdd:PRK10376 119 LGLDVLDvvnlrLMGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEivcvQNHYN--------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 187 syLRPKSGWDFGDQVAANqdlfefvedtGISLVAYSPLlqGAYTnPNKEfkeqyqgpdtdkrlAVLDEIAAETGATRNQL 266
Cdd:PRK10376 190 --LAHRADDALIDALARD----------GIAYVPFFPL--GGFT-PLQS--------------STLSDVAASLGATPMQV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1001929468 267 VYYWLMNRKPNaIPLIAATTD-EQFKEALGSLELELSEDMLRAM 309
Cdd:PRK10376 241 ALAWLLQRSPN-ILLIPGTSSvAHLRENLAAAELVLSEEVLAEL 283
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
40-304 |
1.35e-13 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 70.11 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYshwisdqtqGGESEkmIGKWLKER------NNREDVIIASKVgfpypgteYGTSKK--QIKEECHK 111
Cdd:cd19106 30 LDAGYRHIDCAAVY---------GNEQE--VGEALKEKvgpgkaVPREDLFVTSKL--------WNTKHHpeDVEPALRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 112 SLERLGTDYIDLYYAH--------TDDF-----------NTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAK 172
Cdd:cd19106 91 TLKDLQLDYLDLYLIHwpyafergDNPFpknpdgtirydSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 173 QNhwqsySAIQQR--YSYLrpksgwdfgdqvaANQDLFEFVEDTGISLVAYSPLlqgayTNPNKEFKEqyqgPDTDKRL- 249
Cdd:cd19106 171 IK-----PAVLQVecHPYL-------------AQNELIAHCKARGLVVTAYSPL-----GSPDRPWAK----PDEPVLLe 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001929468 250 -AVLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELSED 304
Cdd:cd19106 224 ePKVKALAKKYNKSPAQILLRWQVQRGVVVIP--KSVTPSRIKQNIQVFDFTLSPE 277
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
10-311 |
7.60e-13 |
|
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: 67.16 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLYFGARDSKEKSFRRMdqyLAAGGNFLDTANMYSHwisdqtqggesEKMIGKWLKERN-NREDVIIASK 88
Cdd:cd19156 6 GVEMPRLGLGVWRVQDGAEAENAVKWA---IEAGYRHIDTAAIYKN-----------EEGVGQGIRESGvPREEVFVTTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 89 VGFPYPGTEYGTSKKQikeechKSLERLGTDYIDLYYAH---TDDFntplEETLEAFNELITEGKVRAIGASNFKAWRLE 165
Cdd:cd19156 72 LWNSDQGYESTLAAFE------ESLEKLGLDYVDLYLIHwpvKGKF----KDTWKAFEKLYKEKKVRAIGVSNFHEHHLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 166 RARQIAK----QNHWQSYSAIQQRysylrpksgwdfgdqvaanqDLFEFVEDTGISLVAYSPLLQGA-YTNPnkefkeqy 240
Cdd:cd19156 142 ELLKSCKvapmVNQIELHPLLTQE--------------------PLRKFCKEKNIAVEAWSPLGQGKlLSNP-------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001929468 241 qgpdtdkrlaVLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELSEDMLRAMTE 311
Cdd:cd19156 194 ----------VLKAIGKKYGKSAAQVIIRWDIQHGIITIP--KSVHEERIQENFDVFDFELTAEEIRQIDG 252
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
65-305 |
8.52e-13 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 67.83 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 65 ESEKMIGKWLKERNN-----REDVIIASKVGFPYpgteygTSKKQIKEECHKSLERLGTDYIDLYYAH-------TDDF- 131
Cdd:cd19107 41 QNENEVGEAIQEKIKeqvvkREDLFIVSKLWCTF------HEKGLVKGACQKTLSDLKLDYLDLYLIHwptgfkpGKELf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 132 -----------NTPLEETLEAFNELITEGKVRAIGASNFKAWRLERarqIAKQNHWQSYSAIQQR--YSYLrpksgwdfg 198
Cdd:cd19107 115 pldesgnvipsDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER---ILNKPGLKYKPAVNQIecHPYL--------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 199 dqvaANQDLFEFVEDTGISLVAYSPLlqgayTNPNKEF-KEQYQGPDTDKRlavLDEIAAETGATRNQLVYYWLMNRKPN 277
Cdd:cd19107 183 ----TQEKLIQYCQSKGIVVTAYSPL-----GSPDRPWaKPEDPSLLEDPK---IKEIAAKHNKTTAQVLIRFPIQRNLV 250
|
250 260
....*....|....*....|....*....
gi 1001929468 278 AIPliAATTDEQFKEALGSLELELS-EDM 305
Cdd:cd19107 251 VIP--KSVTPERIAENFKVFDFELSsEDM 277
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
111-307 |
1.27e-12 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 66.59 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 111 KSLERLGTDYIDLYYAH--TDDFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLERARQIAKQNHwqsySAIQQ--RY 186
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAEN----IATNQieLS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 187 SYLRpksgwdfgdqvaaNQDLFEFVEDTGISLVAYSPLlqgAYtnpNKEFKEqyqgpdtdkrlAVLDEIAAETGATRNQL 266
Cdd:PRK11172 157 PYLQ-------------NRKVVAFAKEHGIHVTSYMTL---AY---GKVLKD-----------PVIARIAAKHNATPAQV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001929468 267 VYYWLMNRKPNAIPliAATTDEQFKEALGSLELELS-EDMLR 307
Cdd:PRK11172 207 ILAWAMQLGYSVIP--SSTKRENLASNLLAQDLQLDaEDMAA 246
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
66-314 |
1.62e-12 |
|
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: 66.74 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 66 SEKMIGKWLKERNN-----REDVIIASKVgfpypgteYGTSKKQIKEECHKSLERLGTDYIDLYYAH------------T 128
Cdd:cd19112 49 NEKEVGEALAEAFKtglvkREDLFITTKL--------WNSDHGHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgtT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 129 D-----------DFNTPLEETLEAFNELITEGKVRAIGASNFKawrLERARQIAKqnhwqsysaiqqrYSYLRPksgwdf 197
Cdd:cd19112 121 GsalgedgvldiDVTISLETTWHAMEKLVSAGLVRSIGISNYD---IFLTRDCLA-------------YSKIKP------ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 198 gdqvAANQ----------DLFEFVEDTGISLVAYSPLLQGAytnPNKEF---KEQYQGPdtdkrlaVLDEIAAETGATRN 264
Cdd:cd19112 179 ----AVNQiethpyfqrdSLVKFCQKHGISVTAHTPLGGAA---ANAEWfgsVSPLDDP-------VLKDLAKKYGKSAA 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 265 QLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELS-EDM---------LRAMTEAKF 314
Cdd:cd19112 245 QIVLRWGIQRNTAVIP--KSSKPERLKENIDVFDFQLSkEDMkliksldrkYRTNQPAKF 302
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
67-309 |
1.75e-12 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 66.39 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 67 EKMIGKWLKE-----RNNREDVIIASKVgfpYPgteYGTSKKQIKEECHKSLERLGTDYIDLYYAH-------------- 127
Cdd:cd19128 40 EAFIGIAFSEifkdgGVKREDLFITSKL---WP---TMHQPENVKEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdpr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 128 -----TDDFNTPLEETLEAFNELITEGKVRAIGASNFkawrlerarqiakqnhwqSYSAIQQRYSYLRPKSgwdFGDQVA 202
Cdd:cd19128 114 ddnqiQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNY------------------STKLLTDLLNYCKIKP---FMNQIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 203 A-----NQDLFEFVEDTGISLVAYSPLLqGAYTNPNKEfkeqyqgPDTDKRlavLDEIAAETGATRNQLVYYWLMNRKPN 277
Cdd:cd19128 173 ChpyfqNDKLIKFCIENNIHVTAYRPLG-GSYGDGNLT-------FLNDSE---LKALATKYNTTPPQVIIAWHLQKWPK 241
|
250 260 270
....*....|....*....|....*....|...
gi 1001929468 278 AIPLIA-ATTDEQFKEALGSLELELSEDMLRAM 309
Cdd:cd19128 242 NYSVIPkSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
48-311 |
7.03e-12 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 64.60 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 48 DTANMYshwisdqtqggESEKMIGKWLKER------NNREDVIIASK--VGFPYPGteygtskkQIKEECHKSLERLGTD 119
Cdd:cd19124 38 DTAAAY-----------GTEEALGEALAEAlrlglvKSRDELFVTSKlwCSDAHPD--------LVLPALKKSLRNLQLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 120 YIDLYYAH--------------TDDFNTPL--EETLEAFNELITEGKVRAIGASNFKAWRLERARQIAKqnhwqsysaiq 183
Cdd:cd19124 99 YVDLYLIHwpvslkpgkfsfpiEEEDFLPFdiKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFAT----------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 184 qrysyLRPksgwdfgdqvAANQ----------DLFEFVEDTGISLVAYSPLlqGAYTNPnkefkeqyQGPDTDKRLAVLD 253
Cdd:cd19124 168 -----IPP----------AVNQvemnpawqqkKLREFCKANGIHVTAYSPL--GAPGTK--------WGSNAVMESDVLK 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001929468 254 EIAAETGATRNQLVYYWLMNRkpnAIPLIAATTDEQ-FKEALGSLELELSEDMLRAMTE 311
Cdd:cd19124 223 EIAAAKGKTVAQVSLRWVYEQ---GVSLVVKSFNKErMKQNLDIFDWELTEEDLEKISE 278
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
40-292 |
9.27e-12 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 64.40 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKE-----RNNREDVIIASKVgfpypgteYGTSKK--QIKEECHKS 112
Cdd:cd19129 29 LEAGFRHFDCAERY-----------RNEAEVGEAMQEvfkagKIRREDLFVTTKL--------WNTNHRpeRVKPAFEAS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 113 LERLGTDYIDLYYAHTD--------------------DFNTPLEETLEAFNELITEGKVRAIGASNFKawrLERARQIAK 172
Cdd:cd19129 90 LKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVS---LEKLREIFE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 173 QNHWQSYSAIQQRYSYLrPKSgwdfgdqvaanqDLFEFVEDTGISLVAYSPLLQGAYTNPnkefkeqYQGPdtdkrlaVL 252
Cdd:cd19129 167 AARIKPAVVQVESHPYL-PEW------------ELLDFCKNHGIVLQAFAPLGHGMEPKL-------LEDP-------VI 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1001929468 253 DEIAAETGATRNQLVYYWLMNRkpNAIPLIAATTDEQFKE 292
Cdd:cd19129 220 TAIARRVNKTPAQVLLAWAIQR--GTALLTTSKTPSRIRE 257
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-232 |
6.43e-11 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 61.78 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 9 TGLQVSQMGLGCLYFGARDSKEKsfrrMDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERNN----REDVI 84
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAA----VAHALKIGYRHIDGALCY-----------QNEDEVGEGIKEAIAggvkREDLF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 85 IASKVgfpypgteYGTSKKQIKEECHKSLERLGTDYIDLYYAH-----TDDFNTPLEETLE-----------------AF 142
Cdd:cd19121 73 VTTKL--------WSTYHRRVELCLDRSLKSLGLDYVDLYLVHwpvllNPNGNHDLFPTLPdgsrdldwdwnhvdtwkQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 143 NELITEGKVRAIGASNFKAWRLErarQIAKqnHWQSYSAIQQ--RYSYLrPKsgwdfgdqvaanQDLFEFVEDTGISLVA 220
Cdd:cd19121 145 EKVLKTGKTKAIGVSNYSIPYLE---ELLK--HATVVPAVNQveNHPYL-PQ------------QELVDFCKEKGILIEA 206
|
250
....*....|..
gi 1001929468 221 YSPLlqGAYTNP 232
Cdd:cd19121 207 YSPL--GSTGSP 216
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
18-257 |
1.06e-10 |
|
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: 61.47 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 18 LGCLYFGARDSKEKSFRRMDqyLAAGGNFLDTANMYShwisdqtqGGESEKMIGKWLKERNnREDVIIASKVG------- 90
Cdd:cd19152 10 LGNLYEAVSDEEAKATLVAA--WDLGIRYFDTAPWYG--------AGLSEERLGAALRELG-REDYVISTKVGrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 91 -------FPYPGT-----EYGTSKKQIKEECHKSLERLGTDYIDLYYAHTDDFNTPLEETLEAFNELIT----------- 147
Cdd:cd19152 79 eveptfePGFWNPlpfdaVFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKgafraleelre 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 148 EGKVRAIGASnFKAWR-LERARQIAKQNhwqsYSAIQQRYSYLrpksgwdfgDQVAAnQDLFEFVEDTGISLVAYSPLLQ 226
Cdd:cd19152 159 EGVIKAIGLG-VNDWEvILRILEEADLD----WVMLAGRYTLL---------DHSAA-RELLPECEKRGVKVVNAGPFNS 223
|
250 260 270
....*....|....*....|....*....|.
gi 1001929468 227 GAYTNPNKEFKEQYQGPDTDKrLAVLDEIAA 257
Cdd:cd19152 224 GFLAGGDNFDYYEYGPAPPEL-IARRDRIEA 253
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-309 |
1.16e-10 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 60.69 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLYFGARDSKeksfRRMDQYLAAGGNFLDTANMYSHwisdqtQGGESEKMIGKWLKernnREDVIIASKV 89
Cdd:cd19130 7 GNSIPQLGYGVFKVPPADTQ----RAVATALEVGYRHIDTAAIYGN------EEGVGAAIAASGIP----RDELFVTTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 90 GFPYPGTEygtskkQIKEECHKSLERLGTDYIDLYYAH-----TDDFntplEETLEAFNELITEGKVRAIGASNFKAWRL 164
Cdd:cd19130 73 WNDRHDGD------EPAAAFAESLAKLGLDQVDLYLVHwptpaAGNY----VHTWEAMIELRAAGRTRSIGVSNFLPPHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 165 ERARQ----IAKQNHWQSYSAIQQRYSYlrpksgwdfgdqvaanqdlfEFVEDTGISLVAYSPLLQGA-YTNPnkefkeq 239
Cdd:cd19130 143 ERIVAatgvVPAVNQIELHPAYQQRTIR--------------------DWAQAHDVKIEAWSPLGQGKlLGDP------- 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 240 yqgpdtdkrlaVLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELSEDMLRAM 309
Cdd:cd19130 196 -----------PVGAIAAAHGKTPAQIVLRWHLQKGHVVFP--KSVRRERMEDNLDVFDFDLTDTEIAAI 252
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
80-305 |
1.35e-10 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 61.13 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 80 REDVIIASKVgfpypgteYGTSKKQ--IKEECHKSLERLGTDYIDLYYAH------TDDFNTPLEE-------------T 138
Cdd:cd19110 61 REDLFIVSKL--------WCTCHKKslVKTACTRSLKALKLNYLDLYLIHwpmgfkPGEPDLPLDRsgmvipsdtdfldT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 139 LEAFNELITEGKVRAIGASNFKAWRLERArqIAKQN-HWQSYSAIQQRYSYLRPKsgwdfgdqvaanqDLFEFVEDTGIS 217
Cdd:cd19110 133 WEAMEDLVIEGLVKNIGVSNFNHEQLERL--LNKPGlRVKPVTNQIECHPYLTQK-------------KLISFCQSRNVS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 218 LVAYSPLlqgaytNPNKEFKEQYQGPdtdkrlaVLDEIAAETGATRNQLVYYWLMNRkpNAIPLIAATTDEQFKEALGSL 297
Cdd:cd19110 198 VTAYRPL------GGSCEGVDLIDDP-------VIQRIAKKHGKSPAQILIRFQIQR--NVIVIPKSVTPSRIKENIQVF 262
|
....*....
gi 1001929468 298 ELELSE-DM 305
Cdd:cd19110 263 DFELTEhDM 271
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
40-311 |
3.08e-10 |
|
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: 59.73 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 40 LAAGGNFLDTANMYShwisDQTQGGESekmIGKWLKERNN--REDVIIASKVgfpypgteYGTSKKQ--IKEECHKSLER 115
Cdd:cd19118 30 LKAGYRHLDLAKVYQ----NQHEVGQA---LKELLKEEPGvkREDLFITSKL--------WNNSHRPeyVEPALDDTLKE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 116 LGTDYIDLYYAH--------TD----------------DFNTPLEETLEAFNELITEGKVRAIGASNFKAWRLErarqia 171
Cdd:cd19118 95 LGLDYLDLYLIHwpvafkptGDlnpltavptnggevdlDLSVSLVDTWKAMVELKKTGKVKSIGVSNFSIDHLQ------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 172 kqnhwqsysAIQQRYSyLRPKSgwdfgDQVAA-----NQDLFEFVEDTGISLVAYSPL---LQGA---YTNPnkefkeqy 240
Cdd:cd19118 169 ---------AIIEETG-VVPAV-----NQIEAhplllQDELVDYCKSKNIHITAYSPLgnnLAGLpllVQHP-------- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001929468 241 qgpdtdkrlaVLDEIAAETGATRNQLVYYWLMNRKPNAIP--LIAATTDEQFKealgslELELSEDMLRAMTE 311
Cdd:cd19118 226 ----------EVKAIAAKLGKTPAQVLIAWGIQRGHSVIPksVTPSRIRSNFE------QVELSDDEFNAVTA 282
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-311 |
3.12e-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: 381324 [Multi-domain] Cd Length: 318 Bit Score: 60.05 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 29 KEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqgGESEKMIGKWLKERN-NREDVIIASKVGFPYpgteygTSKKQIKE 107
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSY----------GRAEEFLGSWLRSRNiAPDAVFVGSKWGYTY------TADWQVDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 108 ECHK---------------SLERLGtDYIDLYYAHTDDFNTPL---EETLEAFNELITEGkvRAIGASNF---KAWRLER 166
Cdd:cd19098 98 AVHEvkdhslarllkqweeTRSLLG-KHLDLYQIHSATLESGVledADVLAALAELKAEG--VKIGLSLSgpqQAETLRR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 167 ARQIAKQNHwQSYSAIQQRYSYLRPKSGwdfgdqvaanqDLFEFVEDTGISLVAYSPLLQGAYTNPNkefkeqyQGPDTD 246
Cdd:cd19098 175 ALEIEIDGA-RLFDSVQATWNLLEQSAG-----------EALEEAHEAGMGVIVKEALANGRLTDRN-------PSPELA 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001929468 247 KRLAVLDEIAAETGATRNQLVYYWLMNRKPNAIPLIAATTDEQFKEALGSLELELSEDMLRAMTE 311
Cdd:cd19098 236 PLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAALAD 300
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
42-260 |
2.60e-09 |
|
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: 57.34 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 42 AGGNFLDTANMYSHwisdqtqgGESEKMIGKWLKErNNREDVIIASKVG-----------FPYPG--------TEYGTSK 102
Cdd:cd19161 32 SGIRYFDTAPMYGH--------GLAEHRLGDFLRE-KPRDEFVLSTKVGrllkparegsvPDPNGfvdplpfeIVYDYSY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 103 KQIKEECHKSLERLGTDYIDL-------YYAHTDD-----FNTPLEETLEAFNELITEGKVRAIGASnfkawrlerarqi 170
Cdd:cd19161 103 DGIMRSFEDSLQRLGLNRIDIlyvhdigVYTHGDRkerhhFAQLMSGGFKALEELKKAGVIKAFGLG------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 171 akQNHWQSYSA-----------IQQRYSYLrpksgwdfgDQVAAnQDLFEFVEDTGISLVAYSPLLQGAY-TNPNKEFKE 238
Cdd:cd19161 170 --VNEVQICLEaldeadldcflLAGRYSLL---------DQSAE-EEFLPRCEQRGTSLVIGGVFNSGILaTGTKSGAKF 237
|
250 260
....*....|....*....|....
gi 1001929468 239 QYQGPDTD--KRLAVLDEIAAETG 260
Cdd:cd19161 238 NYGDAPAEiiSRVMEIEKICDAYN 261
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
80-311 |
5.65e-09 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 56.27 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 80 REDVIIASKVgfpypgteYGT--SKKQIKEECHKSLERLGTDYIDLYYAHtddF-------------------------- 131
Cdd:cd19115 70 REDLFIVSKL--------WNTfhDGERVEPICRKQLADWGIDYFDLFLIH---Fpialkyvdpavryppgwfydgkkvef 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 132 -NTPLEETLEAFNELITEGKVRAIGASNFKA------WRLERARQIAKQNHWQSYsaIQQrysylrpksgwdfgdqvaan 204
Cdd:cd19115 139 sNAPIQETWTAMEKLVDKGLARSIGVSNFSAqllmdlLRYARIRPATLQIEHHPY--LTQ-------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 205 QDLFEFVEDTGISLVAYSPLlqgaytNPnKEFKEqYQGPDTDKRLAVLDE-----IAAETGATRNQLVYYWLMNRKPNAI 279
Cdd:cd19115 197 PRLVKYAQKEGIAVTAYSSF------GP-QSFLE-LDLPGAKDTPPLFEHdviksIAEKHGKTPAQVLLRWATQRGIAVI 268
|
250 260 270
....*....|....*....|....*....|..
gi 1001929468 280 PliAATTDEQFKEALGSLELELSEDMLRAMTE 311
Cdd:cd19115 269 P--KSNNPKRLAQNLDVTGFDLEAEEIKAISA 298
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
28-309 |
6.91e-09 |
|
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: 55.63 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 28 SKEKSFRRMDQYLAAGGNFLDTANMYSHwisdqtqggesEKMIGKWL-KERNNREDVIIASKVGFPypgtEYGTSKKQik 106
Cdd:cd19134 22 SDDEAERSVSAALEAGYRLIDTAAAYGN-----------EAAVGRAIaASGIPRGELFVTTKLATP----DQGFTASQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 107 EECHKSLERLGTDYIDLYYAHtddFNTPLEET-LEAFNELIT---EGKVRAIGASNFKAWRLERARQIAKQNhwqsySAI 182
Cdd:cd19134 85 AACRASLERLGLDYVDLYLIH---WPAGREGKyVDSWGGLMKlreEGLARSIGVSNFTAEHLENLIDLTFFT-----PAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 183 QQrySYLRPKsgwdfgdqvaANQD-LFEFVEDTGISLVAYSPLLQG-AYTNPnkefkeqyqgpdtdkrlAVLdEIAAETG 260
Cdd:cd19134 157 NQ--IELHPL----------LNQAeLRKVNAQHGIVTQAYSPLGVGrLLDNP-----------------AVT-AIAAAHG 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1001929468 261 ATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALGSLELELSEDMLRAM 309
Cdd:cd19134 207 RTPAQVLLRWSLQLGNVVIS--RSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
15-166 |
1.06e-08 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 55.08 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 15 QMGLGCLyfgaRDSKEKSFRRMDQYLAAGGNFLDTANMYshwisdqtqggESEKMIGKWLKERN-NREDVIIASKVgfpy 93
Cdd:PRK11565 17 QLGLGVW----QASNEEVITAIHKALEVGYRSIDTAAIY-----------KNEEGVGKALKEASvAREELFITTKL---- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001929468 94 pgteYGTSKKQIKEECHKSLERLGTDYIDLYYAHtddFNTPLEET-LEAFNELIT---EGKVRAIGASNFKAWRLER 166
Cdd:PRK11565 78 ----WNDDHKRPREALEESLKKLQLDYVDLYLMH---WPVPAIDHyVEAWKGMIElqkEGLIKSIGVCNFQIHHLQR 147
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
80-311 |
2.31e-08 |
|
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: 54.37 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 80 REDVIIASKVGFPYpgteygTSKKQIKEECHKSLERLGTDYIDLYYAH----------------------TDDF---NTP 134
Cdd:cd19113 68 REELFLTSKLWNNF------HDPKNVETALNKTLSDLKLDYVDLFLIHfpiafkfvpieekyppgfycgdGDNFvyeDVP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 135 LEETLEAFNELITEGKVRAIGASNFKAWRLE---RARQIAKqnhwqsySAIQ-QRYSYL-RPKsgwdfgdqvaanqdLFE 209
Cdd:cd19113 142 ILDTWKALEKLVDAGKIKSIGVSNFPGALILdllRGATIKP-------AVLQiEHHPYLqQPK--------------LIE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 210 FVEDTGISLVAYSP--------LLQGAYTNPNKEFKEQyqgpdtdkrlaVLDEIAAETGATRNQLVYYWLMNRKPNAIPl 281
Cdd:cd19113 201 YAQKAGITITAYSSfgpqsfveLNQGRALNTPTLFEHD-----------TIKSIAAKHNKTPAQVLLRWATQRGIAVIP- 268
|
250 260 270
....*....|....*....|....*....|
gi 1001929468 282 iAATTDEQFKEALGSLELELSEDMLRAMTE 311
Cdd:cd19113 269 -KSNLPERLLQNLSVNDFDLTKEDFEEIAK 297
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-240 |
4.42e-08 |
|
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: 53.66 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 9 TGLQVSQMGLGClyfgARDSKEKSFRRMDQYLA--AGGNFLDTANMYshwisdqtqggESEKMIGKWLKE-----RNNRE 81
Cdd:cd19119 8 TGASIPALGLGT----ASPHEDRAEVKEAVEAAikEGYRHIDTAYAY-----------ETEDFVGEAIKRaiddgSIKRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 82 DVIIASKVgfpYPgteygTSKKQIKEECHKSLERLGTDYIDL--------YYAHTDDFNTPLE----------------- 136
Cdd:cd19119 73 ELFITTKV---WP-----TFYDEVERSLDESLKALGLDYVDLllvhwpvcFEKDSDDSGKPFTpvnddgktryaasgdhi 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 137 ETLEAFNELITEGKVRAIGASNFKAWRLER----ARQIAKQNHWQSYSAIQQRysylrpksgwdfgdqvaanqDLFEFVE 212
Cdd:cd19119 145 TTYKQLEKIYLDGRAKAIGVSNYSIVYLERlikeCKVVPAVNQVELHPHLPQM--------------------DLRDFCF 204
|
250 260 270
....*....|....*....|....*....|....
gi 1001929468 213 DTGISLVAYSPLlqGAYTNPN------KEFKEQY 240
Cdd:cd19119 205 KHGILVTAYSPL--GSHGAPNlknplvKKIAEKY 236
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-313 |
7.42e-08 |
|
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: 52.95 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 10 GLQVSQMGLGCLYFGARDSKEKSFrrmdQYLAAGGNFLDTANMYshwisdqtqGGESEkmIGKWLKERNN-----REDVI 84
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIY----NAIKVGYRLIDGALLY---------GNEAE--VGRGIRKAIQeglvkREDLF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 85 IASKVGFPYPGteygtsKKQIKEECHKSLERLGTDYIDLYYAH----------------------TDDF---NTPLEETL 139
Cdd:cd19114 66 IVTKLWNNFHG------KDHVREAFDRQLKDYGLDYIDLYLIHfpipaayvdpaenypflwkdkeLKKFpleQSPMQECW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 140 EAFNELITEGKVRAIGASNFKAWRLERARQIAKQNHwqsySAIQ-QRYSYLRPKSgwdfgdqvaanqdLFEFVEDTGISL 218
Cdd:cd19114 140 REMEKLVDAGLVRNIGIANFNVQLILDLLTYAKIKP----AVLQiEHHPYLQQKR-------------LIDWAKKQGIQI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001929468 219 VAYSPLLQGAY---TNPNKEFKEQYQGPdtdkrlaVLDEIAAETGATRNQLVYYWLMNRKPNAIPliAATTDEQFKEALG 295
Cdd:cd19114 203 TAYSSFGNAVYtkvTKHLKHFTNLLEHP-------VVKKLADKHKRDTGQVLLRWAVQRNITVIP--KSVNVERMKTNLD 273
|
330
....*....|....*...
gi 1001929468 296 SLELELSEDMLRAMTEAK 313
Cdd:cd19114 274 ITSYKLDEEDMEALYELE 291
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
111-166 |
2.08e-03 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 39.14 E-value: 2.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001929468 111 KSLERLGTDYIDLYYAHT--------DDFntPLEE-------------TLEAFNELITEGKVRAIGASNFKAWRLER 166
Cdd:cd19108 96 KSLKKLQLDYVDLYLIHFpvalkpgeELF--PKDEngklifdtvdlcaTWEAMEKCKDAGLAKSIGVSNFNRRQLEM 170
|
|
| |
