|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-297 |
1.66e-174 |
|
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: 484.14 E-value: 1.66e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 14 SCMGLGTMYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASWIPGFKGGESEQLIGRWMKQRGNRQTLFVASKVGFPYG 93
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTEGGVGGESERLIGRWLKDRGNRDDVVIATKVGAGPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 94 N------IPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEAN 167
Cdd:cd19752 81 DpdggpeSPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 168 QAAKNQGWEGFSCIQQFHTYLQPALWADFGNQQILTPEIQEFCSVRK-LSIVAYSPLLAGAYTRNDIPLPEQFRGQNTGH 246
Cdd:cd19752 161 QIARQQGWAEFSAIQQRHSYLRPRPGADFGVQRIVTDELLDYASSRPdLTLLAYSPLLSGAYTRPDRPLPEQYDGPDSDA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1082502195 247 KLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLS 297
Cdd:cd19752 241 RLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-308 |
1.28e-87 |
|
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: 264.46 E-value: 1.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 5 ELGNTRERISCMGLGTMYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASWIPGFKGGESEQLIGRWMKQRGNRQTLFV 84
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAWVPGNAGGESETIIGRWLKSRGKRDRVVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 85 ASKVGFPYGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLG 164
Cdd:cd19081 81 ATKVGFPMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 165 EANQAAKNQGWEGFSCIQQFHTYLqpalwadfgNQQILTPEIQEFCSVRKLSIVAYSPL----LAGAYTRnDIPLPEQFR 240
Cdd:cd19081 161 EALELSRQHGLPRYVSLQPEYNLV---------DRESFEGELLPLCREEGIGVIPYSPLaggfLTGKYRS-EADLPGSTR 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082502195 241 GQNTGHK---------LEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19081 231 RGEAAKRylnerglriLDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-294 |
1.10e-86 |
|
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: 259.37 E-value: 1.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 14 SCMGLGTMYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRGNRQTLFVASKVGFPYG 93
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYG-------DGRSERLLGRWLKGRGNRDDVVIATKGGHPPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 94 NIP--RSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQAAK 171
Cdd:cd06660 74 GDPsrSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 172 NQGWEGFSCIQQFHTYLqpalwadfgNQQILTPEIQEFCSVRKLSIVAYSPLLAGaytrndiplpeqfrgqntghklekl 251
Cdd:cd06660 154 AHGLPGFAAVQPQYSLL---------DRSPMEEELLDWAEENGLPLLAYSPLARG------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1082502195 252 ktvagelgvsANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQ 294
Cdd:cd06660 200 ----------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-310 |
4.33e-78 |
|
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: 240.47 E-value: 4.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGTMYFGT---KTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRg 77
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYG-------PGRSEELLGEALKGR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 78 NRQTLFVASKVGFPYGNIPRS--LKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGA 155
Cdd:COG0667 73 PRDDVVIATKVGRRMGPGPNGrgLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 156 SNFHAWQLGEANQAAKnqGWEGFSCIQ-QFHtylqpaLWadfgNQQILTpEIQEFCSVRKLSIVAYSPL----LAGAYTR 230
Cdd:COG0667 153 SNYSAEQLRRALAIAE--GLPPIVAVQnEYS------LL----DRSAEE-ELLPAARELGVGVLAYSPLagglLTGKYRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 231 NDiPLPEQFRGQNTGH----------KLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVTL 300
Cdd:COG0667 220 GA-TFPEGDRAATNFVqgylternlaLVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLEL 298
|
330
....*....|
gi 1082502195 301 SKKQLEQLAS 310
Cdd:COG0667 299 SAEDLAALDA 308
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-297 |
1.32e-73 |
|
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: 228.21 E-value: 1.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 14 SCMGLGTMYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASWIPGfkgGESEQLIGRWMKQRGNRQTLFVASKVGFPYG 93
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVER---GASERVIGEWLKSRGNRDKVVIATKGGHPDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 94 N---IPRsLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQAA 170
Cdd:cd19082 78 EdmsRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 171 KNQGWEGFSCIQ-QFH-TYLQPALWADFGNqQILTPEIQEFCSVRKLSIVAYSPL----LAGAYTRNDIPLPEQFRGQNT 244
Cdd:cd19082 157 KAHGLPGFAASSpQWSlARPNEPPWPGPTL-VAMDEEMRAWHEENQLPVFAYSSQargfFSKRAAGGAEDDSELRRVYYS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082502195 245 GH---KLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLS 297
Cdd:cd19082 236 EEnfeRLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
4-308 |
1.17e-69 |
|
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: 218.61 E-value: 1.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 4 VELGNTRERISCMGLGTMYFGTKT------DEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRG 77
Cdd:cd19079 3 VRLGNSGLKVSRLCLGCMSFGDPKwrpwvlDEEESRPIIKRALDLGINFFDTANVYS-------GGASEEILGRALKEFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 78 NRQTLFVASKVGFPYGNIP--RSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGA 155
Cdd:cd19079 76 PRDEVVIATKVYFPMGDGPngRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 156 SNFHAWQLGEANQAAKNQGWEGFSCIQQFHTYLQpalwadfgnQQILTpEIQEFCSVRKLSIVAYSPLLAGAYTRNDIPL 235
Cdd:cd19079 156 SSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLY---------REEER-EMIPLCEEEGIGVIPWSPLARGRLARPWGDT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 236 PEQFRGQNTGHKLEKLKT-------------VAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVTLSK 302
Cdd:cd19079 226 TERRRSTTDTAKLKYDYFteadkeivdrveeVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSE 305
|
....*.
gi 1082502195 303 KQLEQL 308
Cdd:cd19079 306 EEIKYL 311
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-310 |
1.45e-69 |
|
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: 218.60 E-value: 1.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGTMYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRgnRQ 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYG-------GGRSEEIIGRWIAGR--RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 81 TLFVASKVGFPYGNIP--RSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNF 158
Cdd:cd19087 72 DIVLATKVFGPMGDDPndRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 159 HAWQLGEANQAAKNQGWEGFSCIQQFHTYLqpalwadfgNQQIlTPEIQEFCSVRKLSIVAYSPL----LAGAYTRNDIP 234
Cdd:cd19087 152 AAWQIAKAQGIAARRGLLRFVSEQPMYNLL---------KRQA-ELEILPAARAYGLGVIPYSPLagglLTGKYGKGKRP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 235 LPEQFRGQNTGH----------KLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVTLSKKQ 304
Cdd:cd19087 222 ESGRLVERARYQarygleeyrdIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPEL 301
|
....*.
gi 1082502195 305 LEQLAS 310
Cdd:cd19087 302 LAEIDE 307
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-308 |
3.10e-69 |
|
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: 217.47 E-value: 3.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 6 LGNTRERISCMGLGTMYFGT----KTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKqrGNRQT 81
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTewgwGADREEARAMFDAYVEAGGNFIDTANNYT-------NGTSERLLGEFIA--GNRDR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 82 LFVASKVGFPY-GNIPRSL---KKEIILSeCEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASN 157
Cdd:cd19080 74 IVLATKYTMNRrPGDPNAGgnhRKNLRRS-VEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 158 FHAWQLGEANQAAKNQGWEGFSCIQQFHTYLQPALWADfgnqqiLTPEIQEFcsvrKLSIVAYSPL----LAGAYTRNDI 233
Cdd:cd19080 153 TPAWVVARANTLAELRGWSPFVALQIEYSLLERTPERE------LLPMARAL----GLGVTPWSPLggglLTGKYQRGEE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 234 PLPEQFRGQNTGHK---------LEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVTLSKKQ 304
Cdd:cd19080 223 GRAGEAKGVTVGFGklternwaiVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQ 302
|
....
gi 1082502195 305 LEQL 308
Cdd:cd19080 303 LARL 306
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-310 |
3.75e-63 |
|
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: 201.39 E-value: 3.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 16 MGLGTMYFGTK---TDEQTSHAILDVYVSHGGSFLDTANKYaswipgfKGGESEQLIGRWMKQR-GNRQTLFVASKVGFP 91
Cdd:pfam00248 1 IGLGTWQLGGGwgpISKEEALEALRAALEAGINFIDTAEVY-------GDGKSEELLGEALKDYpVKRDKVVIATKVPDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 92 YGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLgeanQAAK 171
Cdd:pfam00248 74 DGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQI----EKAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 172 NQGWEGFSCIQ-QFHTYlqpalwadfgnQQILTPEIQEFCSVRKLSIVAYSPL----LAGAYTRNDIPLPEQFRGQNTG- 245
Cdd:pfam00248 150 TKGKIPIVAVQvEYNLL-----------RRRQEEELLEYCKKNGIPLIAYSPLggglLTGKYTRDPDKGPGERRRLLKKg 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 246 -----HKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:pfam00248 219 tplnlEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDE 288
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-308 |
8.19e-61 |
|
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: 196.29 E-value: 8.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGTMYFGTK---------TDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGR 71
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGggffgawggVDQEEADRLVDIALDAGINFFDTADVYS-------EGESEEILGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 72 WMKqrGNRQTLFVASKVGFPYGNIP--RSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGK 149
Cdd:cd19091 74 ALK--GRRDDVLIATKVRGRMGEGPndVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 150 IRFAGASNFHAWQLGEANQAAKNQGWEGFSCIQQFHTylqpALWADFGNqqiltpEIQEFCSVRKLSIVAYSPL----LA 225
Cdd:cd19091 152 VRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYS----LLGRDLEH------ELMPLALDQGVGLLVWSPLagglLS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 226 GAYTRnDIPLPEQFRGQNTG------------HKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENL 293
Cdd:cd19091 222 GKYRR-GQPAPEGSRLRRTGfdfppvdrergyDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNL 300
|
330
....*....|....*
gi 1082502195 294 QSLSVTLSKKQLEQL 308
Cdd:cd19091 301 GAAGLSLTPEEIARL 315
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
11-308 |
3.66e-59 |
|
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: 191.20 E-value: 3.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 11 ERISCMGLGTMYFGT----KTDEQTSHAILDVYVSHGGSFLDTANKYaswipGFkgGESEQLIGRWMKqrGNRQTLFVAS 86
Cdd:cd19084 2 LKVSRIGLGTWAIGGtwwgEVDDQESIEAIKAAIDLGINFFDTAPVY-----GF--GHSEEILGKALK--GRRDDVVIAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 87 KVGFPYGN---IPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQL 163
Cdd:cd19084 73 KCGLRWDGgkgVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 164 GEANQAAKnqgwegFSCIQ-QFHtylqpalwadfgnqqILTPEIQE----FCSVRKLSIVAYSPL----LAGAYTRNDIP 234
Cdd:cd19084 153 EEARKYGP------IVSLQpPYS---------------MLEREIEEellpYCRENGIGVLPYGPLaqglLTGKYKKEPTF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 235 LPE-------QFRGQNTGHKLE---KLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAG-STVSQVEENLQSLSVTLSKK 303
Cdd:cd19084 212 PPDdrrsrfpFFRGENFEKNLEivdKLKEIAEKYGKSLAQLAIAWTLAQ-PGVTSAIVGaKNPEQLEENAGALDWELTEE 290
|
....*
gi 1082502195 304 QLEQL 308
Cdd:cd19084 291 ELKEI 295
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
12-301 |
4.38e-58 |
|
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: 188.57 E-value: 4.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 12 RISCMGLGT-MYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRgNRQTLFVASKVGF 90
Cdd:cd19074 3 KVSELSLGTwLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYA-------AGQAEEVLGKALKGW-PRESYVISTKVFW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 91 PYGNIP--RSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQ 168
Cdd:cd19074 75 PTGPGPndRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 169 AAKNQGWEGFSCIQQFHTYLqpalwadfgnQQILTPEIQEFCSVRKLSIVAYSPL----LAGAYtRNDIPLPEQFRGQNT 244
Cdd:cd19074 155 LARQFGLIPPVVEQPQYNML----------WREIEEEVIPLCEKNGIGLVVWSPLaqglLTGKY-RDGIPPPSRSRATDE 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082502195 245 G--------------HKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVTLS 301
Cdd:cd19074 224 DnrdkkrrlltdenlEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLS 294
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-308 |
4.72e-57 |
|
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: 185.87 E-value: 4.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 13 ISCMGLGTMYFG-----TKTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRgnRQTLFVASK 87
Cdd:cd19085 1 VSRLGLGCWQFGggywwGDQDDEESIATIHAALDAGINFFDTAEAYG-------DGHSEEVLGKALKGR--RDDVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 88 VGfpygniPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEAN 167
Cdd:cd19085 72 VS------PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 168 QAAKnqgwegfscIqqfhTYLQPA---LWadfgnQQILTpEIQEFCSVRKLSIVAYSP----LLAGAYTRN-DIPlPEQF 239
Cdd:cd19085 146 DAGR---------I----DSNQLPynlLW-----RAIEY-EILPFCREHGIGVLAYSPlaqgLLTGKFSSAeDFP-PGDA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 240 RGQNTGHK-----------LEKLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAG-STVSQVEENLQSLSVTLSKKQLEQ 307
Cdd:cd19085 206 RTRLFRHFepgaeeetfeaLEKLKEIADELGVTMAQLALAWVLQQ-PGVTSVIVGaRNPEQLEENAAAVDLELSPSVLER 284
|
.
gi 1082502195 308 L 308
Cdd:cd19085 285 L 285
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
12-310 |
2.66e-49 |
|
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: 166.83 E-value: 2.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 12 RISCMGLGTMYFGTK-------TDEQTSHAILDVYVSHGGSFLDTANKYaswipgfKGGESEQLIGRWMKQRGNRQTLFV 84
Cdd:cd19146 10 RVSPLCLGAMSFGEAwksmmgeCDKETAFKLLDAFYEQGGNFIDTANNY-------QGEESERWVGEWMASRGNRDEMVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 85 ASKVGFPY-------------GNIPRSLKkeiiLSeCEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIR 151
Cdd:cd19146 83 ATKYTTGYrrggpikiksnyqGNHAKSLR----LS-VEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 152 FAGASNFHAWQLGEANQAAKNQGWEGFsCIQQFHtylqpalWA----DFGNqqiltpEIQEFCSVRKLSIVAYSPLLAGA 227
Cdd:cd19146 158 YLGVSDTPAWVVSKANAYARAHGLTQF-VVYQGH-------WSaafrDFER------DILPMCEAEGMALAPWGVLGQGQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 228 Y------------TRNDIPLPEQFRgqNTGHKLEKlktVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQS 295
Cdd:cd19146 224 FrteeefkrrgrsGRKGGPQTEKER--KVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEA 298
|
330
....*....|....*
gi 1082502195 296 LSVTLSKKQLEQLAS 310
Cdd:cd19146 299 LGISLSDEEIQEIED 313
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-309 |
7.89e-47 |
|
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: 160.30 E-value: 7.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGTM-----YFGTKTDEQtSHAILDVYVSHGGSFLDTANKYaswipgfkgGESEQLIGRWMKQ 75
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsafYGPPKPDEE-RFAVLDAAFELGCTFWDTADIY---------GDSEELIGRWFKQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 76 -RGNRQTLFVASKVGF----PYGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKI 150
Cdd:cd19144 71 nPGKREKIFLATKFGIeknvETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 151 RFAGASNFHAWQLGEANQAaknqgwEGFSCIQqfhtyLQPALWAdfgnQQILTPEIQEFCSVRKL--SIVAYSPL----L 224
Cdd:cd19144 151 KHIGLSECSAETLRRAHAV------HPIAAVQ-----IEYSPFS----LDIERPEIGVLDTCRELgvAIVAYSPLgrgfL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 225 AGAYTRNDIPLPEQFR-------GQNTGHKLE---KLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQ 294
Cdd:cd19144 216 TGAIRSPDDFEEGDFRrmaprfqAENFPKNLElvdKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLG 295
|
330
....*....|....*...
gi 1082502195 295 SLSVTLS---KKQLEQLA 309
Cdd:cd19144 296 ALKVKLTeeeEKEIREIA 313
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-310 |
1.22e-46 |
|
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: 159.36 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 3 KVELGNTRERISCMGLGT------MYFGtKTDEQTSHAILDVYVSHGGSFLDTAnkyaswiPGFKGGESEQLIGRWMKQR 76
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTwaigggPWWG-GSDDNESIRTIHAALDLGINLIDTA-------PAYGFGHSEEIVGKAIKGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 77 gnRQTLFVASKVGFPYGN-------------IPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQ 143
Cdd:cd19149 73 --RDKVVLATKCGLRWDReggsfffvrdgvtVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 144 LKKSGKIRFAGASNFHAWQLGEANQAAKnqgwegFSCIQQFHTYLQPALWADfgnqqiLTPeiqeFCSVRKLSIVAYSPL 223
Cdd:cd19149 151 LKRQGKIRAIGASNVSVEQIKEYVKAGQ------LDIIQEKYSMLDRGIEKE------LLP----YCKKNNIAFQAYSPL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 224 ----LAGAYT----------RNDIPL--PEQFRGQNTGhkLEKLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAGS-TV 286
Cdd:cd19149 215 eqglLTGKITpdrefdagdaRSGIPWfsPENREKVLAL--LEKWKPLCEKYGCTLAQLVIAWTLAQ-PGITSALCGArKP 291
|
330 340
....*....|....*....|....
gi 1082502195 287 SQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19149 292 EQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-308 |
3.27e-46 |
|
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: 158.15 E-value: 3.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 2 QKVELGNTRERISCMGLGTM---YFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASwipgfkgGESEQLIGRWMKQRgn 78
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMgmsAFYGPADEEESIATLHRALELGVTFLDTADMYGP-------GTNEELLGKALKDR-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 79 RQTLFVASKVGFPY----GNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAG 154
Cdd:cd19076 72 RDEVVIATKFGIVRdpgsGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 155 ASNFHAWQLGEANQAAKnqgwegFSCIQqfhtyLQPALWAdfgnqqiLTPEIQEFCSVRKLSI--VAYSPL----LAGAY 228
Cdd:cd19076 152 LSEASADTIRRAHAVHP------ITAVQ-----SEYSLWT-------RDIEDEVLPTCRELGIgfVAYSPLgrgfLTGAI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 229 TRNDIPLPEQFRGQN---TGHKL-------EKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSV 298
Cdd:cd19076 214 KSPEDLPEDDFRRNNprfQGENFdknlklvEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDV 293
|
330
....*....|
gi 1082502195 299 TLSKKQLEQL 308
Cdd:cd19076 294 VLTPEELAEI 303
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-308 |
4.50e-46 |
|
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: 157.39 E-value: 4.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 12 RISCMGLGTMYFGTKT-------DEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRGNRQTLFV 84
Cdd:cd19093 1 EVSPLGLGTWQWGDRLwwgygeyGDEDLQAAFDAALEAGVNLFDTAEVYG-------TGRSERLLGRFLKELGDRDEVVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 85 ASKVgFPYgniPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDA-GTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQL 163
Cdd:cd19093 74 ATKF-APL---PWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 164 GEANQAAKNQGWEgFSCIQ-QFHtylqpalwadFGNQQILTPEIQEFCSVRKLSIVAYSPL----LAGAYTrnDIPLPEQ 238
Cdd:cd19093 150 RRAHKALKERGVP-LASNQvEYS----------LLYRDPEQNGLLPACDELGITLIAYSPLaqglLTGKYS--PENPPPG 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082502195 239 FRGQNTGHK--------LEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19093 217 GRRRLFGRKnlekvqplLDALEEIAEKYGKTPAQVALNWLIAK--GVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
3-305 |
7.91e-43 |
|
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: 149.49 E-value: 7.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 3 KVELGNTRERISCMGLGTMYFG-----TKTDEQTSHAILDVYVSHGGSFLDTANKYASwipgfkgGESEQLIGRWMKQRg 77
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTNAVGghnlyPNLDEEEGKDLVREALDNGVNLLDTAFIYGL-------GRSEELVGEVLKEY- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 78 NRQTLFVASKVGFPYG-------NIPRSLKKEIilsecEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKI 150
Cdd:cd19083 73 NRNEVVIATKGAHKFGgdgsvlnNSPEFLRSAV-----EKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 151 RFAGASNFHAWQLGEANQAAKNQGWEG-FSCIQQFHtylqpalwadfgnqqilTPEIQEFCSVRKLSIVAYSPL----LA 225
Cdd:cd19083 148 RAIGVSNFSLEQLKEANKDGYVDVLQGeYNLLQREA-----------------EEDILPYCVENNISFIPYFPLasglLA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 226 GAYT----------RNDIPLPEQFRGQNTGHKLEKLKTVAGELGVSANAVVLVWMMqTPPGIIPLLAGSTVS-QVEENLQ 294
Cdd:cd19083 211 GKYTkdtkfpdndlRNDKPLFKGERFSENLDKVDKLKSIADEKGVTVAHLALAWYL-TRPAIDVVIPGAKRAeQVIDNLK 289
|
330
....*....|.
gi 1082502195 295 SLSVTLSKKQL 305
Cdd:cd19083 290 ALDVTLTEEEI 300
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-306 |
1.61e-41 |
|
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: 146.56 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 13 ISCMGLGTMYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASWIPGFKGGESEQLIGRWMKQRGNRQTLFVASKV---- 88
Cdd:cd19094 1 VSEICLGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPSPETQGRTEEIIGSWLKKKGNRDKVVLATKVagpg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 89 ---GFPYGNIPRsLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPP------------------EEFMEAFYQLKKS 147
Cdd:cd19094 81 egiTWPRGGGTR-LDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLfgggyytepseeedsvsfEEQLEALGELVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 148 GKIRFAGASNFHAWQLGEANQAAKNQGWEGFSCIQQFHTYLqpalwadfgNQqilTPEIQ--EFCSVRKLSIVAYSPL-- 223
Cdd:cd19094 160 GKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLL---------NR---NFEEGlaEACHRENVGLLAYSPLag 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 224 --LAGAYTRNDIPLP-----------EQFRGQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTP---PGIIpllaG-STV 286
Cdd:cd19094 228 gvLTGKYLDGAARPEggrlnlfpgymARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPfvtSTII----GaTTL 303
|
330 340
....*....|....*....|
gi 1082502195 287 SQVEENLQSLSVTLSKKQLE 306
Cdd:cd19094 304 EQLKENIDAFDVPLSDELLA 323
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
12-308 |
7.86e-41 |
|
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: 144.58 E-value: 7.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 12 RISCMGLGTMYFGT-------KTDEQTSHAILDVYVSHGGSFLDTANKYaswipgfKGGESEQLIGRWMKQRGNRQTLFV 84
Cdd:cd19147 9 RVSPLILGAMSIGDawsgfmgSMDKEQAFELLDAFYEAGGNFIDTANNY-------QDEQSETWIGEWMKSRKNRDQIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 85 ASKVGFPY--------------GNIPRSLKKEIilsecEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKI 150
Cdd:cd19147 82 ATKFTTDYkayevgkgkavnycGNHKRSLHVSV-----RDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 151 RFAGASNFHAWQLGEANQAAKNQGWEGFSCIQ--------QFHTYLQP---------ALWADFGNQQILTPEIQEFCSVR 213
Cdd:cd19147 157 LYLGVSDTPAWVVSAANYYATAHGKTPFSVYQgrwnvlnrDFERDIIPmarhfgmalAPWDVLGGGKFQSKKAVEERKKN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 214 KlsivaySPLLAGAYTRNDIPLPEQFRgqntghklEKLKTVAGELGV-SANAVVLVWMMQTPPGIIPLLAGSTVSQVEEN 292
Cdd:cd19147 237 G------EGLRSFVGGTEQTPEEVKIS--------EALEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDN 302
|
330
....*....|....*.
gi 1082502195 293 LQSLSVTLSKKQLEQL 308
Cdd:cd19147 303 IEALSIKLTPEEIEYL 318
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-297 |
3.43e-40 |
|
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: 142.31 E-value: 3.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 18 LGTMYFGT---KTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRwmKQRGNRQTLfVASKVgfpYGN 94
Cdd:cd19075 5 LGTMTFGSqgrFTTAEAAAELLDAFLERGHTEIDTARVYP-------DGTSEELLGE--LGLGERGFK-IDTKA---NPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 95 IPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQAAKNQG 174
Cdd:cd19075 72 VGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 175 WegfsciqqfhtyLQPALWAdfGNQQILT--PEIQEFCSVRKLSI--VAYSPL----LAGAYTRNDIPLPE-QFRGQNTG 245
Cdd:cd19075 152 W------------VLPTVYQ--GMYNAITrqVETELFPCLRKLGIrfYAYSPLaggfLTGKYKYSEDKAGGgRFDPNNAL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082502195 246 HK--------------LEKLKTVAGELGVSANAVVLVWMM-------QTPPGIIplLAGSTVSQVEENLQSLS 297
Cdd:cd19075 218 GKlyrdrywkpsyfeaLEKVEEAAEKEGISLAEAALRWLYhhsaldgEKGDGVI--LGASSLEQLEENLAALE 288
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-308 |
5.72e-38 |
|
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: 135.43 E-value: 5.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 11 ERISCMGLGTMYFG-----TKTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRgNRQTLFVA 85
Cdd:cd19072 2 EEVPVLGLGTWGIGggmskDYSDDKKAIEALRYAIELGINLIDTAEMYG-------GGHAEELVGKAIKGF-DREDLFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 86 SKVGfpygniPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGE 165
Cdd:cd19072 74 TKVS------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 166 ANQAAKNqgwEGFSCIQqfHTYlqpalwadfgnqQILTPEIQ----EFCSVRKLSIVAYSPLLAGAYTRndiplpeqfrg 241
Cdd:cd19072 148 AQSYLKK---GPIVANQ--VEY------------NLFDREEEsgllPYCQKNGIAIIAYSPLEKGKLSN----------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082502195 242 qntGHKLEKLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19072 200 ---AKGSPLLDEIAKKYGKTPAQIALNWLISK-PNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-309 |
4.85e-37 |
|
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: 133.95 E-value: 4.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 13 ISCMGLGT---------MYFGTKTDEQTSHAILDVyVSHGGSFLDTANKYaswipGFkgGESEQLIGRWMKQRGNRqtLF 83
Cdd:cd19102 1 LTTIGLGTwaiggggwgGGWGPQDDRDSIAAIRAA-LDLGINWIDTAAVY-----GL--GHSEEVVGRALKGLRDR--PI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 84 VASKVGFPY---GNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHA 160
Cdd:cd19102 71 VATKCGLLWdeeGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 161 WQLGEanqaaknqgwegfscIQQFH--TYLQPALwadfgnqQILTPEIQE----FCSVRKLSIVAYSP----LLAGAYTR 230
Cdd:cd19102 151 DQMKR---------------CQAIHpiASLQPPY-------SLLRRGIEAeilpFCAEHGIGVIVYSPmqsgLLTGKMTP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 231 NDI-PLPE--------QFRGQNTGHKL---EKLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAGS-TVSQVEENLQSLS 297
Cdd:cd19102 209 ERVaSLPAddwrrrspFFQEPNLARNLalvDALRPIAERHGRTVAQLAIAWVLRR-PEVTSAIVGArRPDQIDETVGAAD 287
|
330
....*....|..
gi 1082502195 298 VTLSKKQLEQLA 309
Cdd:cd19102 288 LRLTPEELAEIE 299
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-301 |
6.09e-36 |
|
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: 129.64 E-value: 6.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 13 ISCMGLGTM------YFGTKTDEQTSHAILDVYVSHGGSFLDTANKYAswiPGFkggeSEQLIGRWMKQRGNRqtLFVAS 86
Cdd:cd19088 1 VSRLGYGAMrltgpgIWGPPADREEAIAVLRRALELGVNFIDTADSYG---PDV----NERLIAEALHPYPDD--VVIAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 87 KVGF---PYGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQL 163
Cdd:cd19088 72 KGGLvrtGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 164 GEANQAAknqgweGFSCIQQFHTylqPALWADFGnqqiltpeIQEFCSVRKLSIVAYSPLLAGAYTRNdiplpeqfrgqn 243
Cdd:cd19088 152 EEARAIV------RIVSVQNRYN---LANRDDEG--------VLDYCEAAGIAFIPWFPLGGGDLAQP------------ 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082502195 244 tghkLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVTLS 301
Cdd:cd19088 203 ----GGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
17-304 |
7.40e-36 |
|
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: 130.37 E-value: 7.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 17 GLGTMYFG--TKTDEQTSHAIlDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMK-QRGNRQTLFVASKVGFPYG 93
Cdd:cd19092 10 VLGCMRLAdwGESAEELLSLI-EAALELGITTFDHADIYG-------GGKCEELFGEALAlNPGLREKIEIQTKCGIRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 94 NIPRSLK-------KEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLgea 166
Cdd:cd19092 82 DDPRPGRikhydtsKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQI--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 167 nqaaknqgwegfsciqqfhTYLQPALwadfgNQQILTPEIQ--------------EFCSVRKLSIVAYSPLLAGAYTRND 232
Cdd:cd19092 159 -------------------ELLQSYL-----DQPLVTNQIElsllhteaiddgtlDYCQLLDITPMAWSPLGGGRLFGGF 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082502195 233 IPLPEQFRgqntghklEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLaGST-VSQVEENLQSLSVTLSKKQ 304
Cdd:cd19092 215 DERFQRLR--------AALEELAEEYGVTIEAIALAWLLRHPARIQPIL-GTTnPERIRSAVKALDIELTREE 278
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
11-308 |
2.28e-35 |
|
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: 128.52 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 11 ERISCMGLGTMYFG-TKTDEQTSHAILDVYVSHGGSFLDTANKYASwipgfkgGESEQLIGRWMkqRGNRQTLFVASKVg 89
Cdd:cd19138 9 TKVPALGQGTWYMGeDPAKRAQEIEALRAGIDLGMTLIDTAEMYGD-------GGSEELVGEAI--RGRRDKVFLVSKV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 90 fpygnIPRSLKKEIILSECEKSLKRLDIETIDLYYVHaYDAGTPPEEFMEAFYQLKKSGKIRFAGASNF------HAWQL 163
Cdd:cd19138 79 -----LPSNASRQGTVRACERSLRRLGTDYLDLYLLH-WRGGVPLAETVAAMEELKKEGKIRAWGVSNFdtddmeELWAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 164 GEANQAAKNQgwegfsciqqfhtylqpALWaDFGNQQI---LTPEIQEfcsvRKLSIVAYSPLLAGaytrndiPLPEQFR 240
Cdd:cd19138 153 PGGGNCAANQ-----------------VLY-NLGSRGIeydLLPWCRE----HGVPVMAYSPLAQG-------GLLRRGL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082502195 241 GQNTghkleKLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19138 204 LENP-----TLKEIAARHGATPAQVALAWVLRD-GNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
12-182 |
4.09e-33 |
|
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: 121.82 E-value: 4.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 12 RISCMGLGTMYFGT----KTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKqrGNRQTLFVASK 87
Cdd:cd19086 2 EVSEIGFGTWGLGGdwwgDVDDAEAIRALRAALDLGINFFDTADVYG-------DGHSERLLGKALK--GRRDKVVIATK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 88 VG---FPYGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVH-AYDAGTPPEEFMEAFYQLKKSGKIRFAGAS-NFHAwq 162
Cdd:cd19086 73 FGnrfDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVSvGDPE-- 150
|
170 180
....*....|....*....|
gi 1082502195 163 lgEANQAAKNqgwEGFSCIQ 182
Cdd:cd19086 151 --EALAALRR---GGIDVVQ 165
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
13-308 |
1.07e-32 |
|
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: 122.35 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 13 ISCMGLGTMYF---GTKTDEQTSHAILDVYVSHGGSFLDTANKYASWIPGfkggESEQLIGRWMKQRG-NRQTLFVASKV 88
Cdd:cd19077 5 VGPIGLGLMGLtwrPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPH----ANLKLLARFFRKYPeYADKVVLSVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 89 GFPYGNIPRSLKKEIILSECEKSLKRLDI-ETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEAN 167
Cdd:cd19077 81 GLDPDTLRPDGSPEAVRKSIENILRALGGtKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 168 QAAKnqgwegFSCIQqfhtyLQPALWAdfgnQQILTPEIQEFCSVRKLSIVAYSPL----LAGAY-TRNDIP------LP 236
Cdd:cd19077 161 AVHP------IAAVE-----VEYSLFS----REIEENGVLETCAELGIPIIAYSPLgrglLTGRIkSLADIPegdfrrHL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082502195 237 EQFRGQNTGHKL---EKLKTVAGELGVSANAVVLVW-MMQTPPGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19077 226 DRFNGENFEKNLklvDALQELAEKKGCTPAQLALAWiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
46-308 |
3.49e-32 |
|
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: 119.68 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 46 FLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVASKVgfpygnIPRSLKKEIILSECEKSLKRLDIETIDLYY 124
Cdd:cd19073 30 HIDTAEIY----------NNEAEVGEAIAESGvPREDLFITTKV------WRDHLRPEDLKKSVDRSLEKLGTDYVDLLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 125 VHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEanqaAKNQGWEGFSCIQ-QFHTYLQPAlwadfgnqqilt 203
Cdd:cd19073 94 IHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE----ALDISPLPIAVNQvEFHPFLYQA------------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 204 pEIQEFCSVRKLSIVAYSPLLAGaytrndiplpEQFRgqntghkLEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAG 283
Cdd:cd19073 158 -ELLEYCRENDIVITAYSPLARG----------EVLR-------DPVIQEIAEKYDKTPAQVALRWLVQK--GIVVIPKA 217
|
250 260
....*....|....*....|....*
gi 1082502195 284 STVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19073 218 SSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
13-310 |
2.70e-31 |
|
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: 118.87 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 13 ISCMGLGTM----YFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASWIpgfkggeSEQLIGRWMKQRgnRQTLFVASKV 88
Cdd:cd19078 4 VSAIGLGCMgmshGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYT-------NEELVGEALKPF--RDQVVIATKF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 89 GF------PYGNIPRSlKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRfagasnfhAWQ 162
Cdd:cd19078 75 GFkidggkPGPLGLDS-RPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIR--------HWG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 163 LGEAnqaaknqgweGFSCIQQFH-----TYLQP--ALWADFGNQQILtPEIQEfcsvrkLSI--VAYSPL----LAGAYT 229
Cdd:cd19078 146 LSEA----------GVETIRRAHavcpvTAVQSeySMMWREPEKEVL-PTLEE------LGIgfVPFSPLgkgfLTGKID 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 230 RNDIPLPEQFRG---QNTGHKLEK-------LKTVAGELGVSANAVVLVWMMQTPPGIIPlLAGST-VSQVEENLQSLSV 298
Cdd:cd19078 209 ENTKFDEGDDRAslpRFTPEALEAnqalvdlLKEFAEEKGATPAQIALAWLLAKKPWIVP-IPGTTkLSRLEENIGAADI 287
|
330
....*....|..
gi 1082502195 299 TLSKKQLEQLAS 310
Cdd:cd19078 288 ELTPEELREIED 299
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
13-308 |
3.03e-31 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 119.57 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 13 ISCMGLGTMYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASWIPGFKGGESEQLIGRWMKQRGNRQTLFVASKVGFPY 92
Cdd:PRK10625 13 VSTLGLGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPRPETQGLTETYIGNWLAKRGSREKLIIASKVSGPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 93 GNIPRS------LKKEIILSECEKSLKRLDIETIDLYYVH--------------AYDAGTPPE---EFMEAFYQLKKSGK 149
Cdd:PRK10625 93 RNNDKGirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgySWTDSAPAVsllETLDALAEQQRAGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 150 IRFAGASNFHAWQLGEANQAAKNQGWEGFSCIQQFHTYLQPALwadfgnqQILTPEIQEFCSVRKLsivAYSPL----LA 225
Cdd:PRK10625 173 IRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSF-------EVGLAEVSQYEGVELL---AYSCLafgtLT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 226 GAYTRNDIP------LPEQF---RGQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSL 296
Cdd:PRK10625 243 GKYLNGAKPagarntLFSRFtrySGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESL 322
|
330
....*....|..
gi 1082502195 297 SVTLSKKQLEQL 308
Cdd:PRK10625 323 HLTLSEEVLAEI 334
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-309 |
5.44e-31 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 119.15 E-value: 5.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGTMYFGTKtDEQTSHAILDVYVSHGGSFLDTANKYaswipgfkgGESEQLIGRWMKQRgnRQ 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPRK-DEEEAEALIRRAIDNGINYIDTARGY---------GDSEEFLGKALKGP--RD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 81 TLFVASKVGfPYGNIPRSLKKEIilsecEKSLKRLDIETIDLYYVHA------YDAGTPPEEFMEAFYQLKKSGKIRFAG 154
Cdd:COG1453 69 KVILATKLP-PWVRDPEDMRKDL-----EESLKRLQTDYIDLYLIHGlnteedLEKVLKPGGALEALEKAKAEGKIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 155 ASnFHAwQLGEANQAAKNQGWEG----FSCIQQFHTYLQPALwadfgnqqiltpeiqEFCSVRKLSIVAYSPLLAGAYTR 230
Cdd:COG1453 143 FS-THG-SLEVIKEAIDTGDFDFvqlqYNYLDQDNQAGEEAL---------------EAAAEKGIGVIIMKPLKGGRLAN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 231 ndipLPEQFrgqntGHKLEKLKTVAgELGVSAnavvlVWmmqTPPGIIPLLAG-STVSQVEENLQSLS--VTLSKKQLEQ 307
Cdd:COG1453 206 ----PPEKL-----VELLCPPLSPA-EWALRF-----LL---SHPEVTTVLSGmSTPEQLDENLKTADnlEPLTEEELAI 267
|
..
gi 1082502195 308 LA 309
Cdd:COG1453 268 LE 269
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-309 |
6.04e-31 |
|
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: 116.43 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 16 MGLGT-MYFGTKTDEQTSHAIldvyvSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVASKVGfpyg 93
Cdd:cd19071 4 IGLGTyKLKPEETAEAVLAAL-----EAGYRHIDTAAAY----------GNEAEVGEAIRESGvPREELFITTKLW---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 94 niPRSLKKEIILSECEKSLKRLDIETIDLYYVH---AYDAGTPPEEFME---AFYQLKKSGKIRFAGASNFHAWQLGEAN 167
Cdd:cd19071 65 --PTDHGYERVREALEESLKDLGLDYLDLYLIHwpvPGKEGGSKEARLEtwrALEELVDEGLVRSIGVSNFNVEHLEELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 168 QAAK-----NQGWegfsciqqFHTYLQPalwadfgnqqiltPEIQEFCSVRKLSIVAYSPLlagayTRNDIPLPEQfrgq 242
Cdd:cd19071 143 AAARikpavNQIE--------LHPYLQQ-------------KELVEFCKEHGIVVQAYSPL-----GRGRRPLLDD---- 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082502195 243 ntghklEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQLA 309
Cdd:cd19071 193 ------PVLKEIAKKYGKTPAQVLLRWALQR--GVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-310 |
2.41e-30 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 115.15 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 11 ERISCMGLGTMYFGtktDEQTSHAI---LDVyvshGGSFLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVAS 86
Cdd:COG0656 3 VEIPALGLGTWQLP---GEEAAAAVrtaLEA----GYRHIDTAAMY----------GNEEGVGEAIAASGvPREELFVTT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 87 KVGfpygniPRSLKKEIILSECEKSLKRLDIETIDLYYVHaYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEA 166
Cdd:COG0656 66 KVW------NDNHGYDDTLAAFEESLERLGLDYLDLYLIH-WPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 167 NQAAK-----NQgwegfscIqQFHTYLQPalwadfgnqqiltPEIQEFCSVRKLSIVAYSPLLAGAYTRNDIplpeqfrg 241
Cdd:COG0656 139 LAETGvkpavNQ-------V-ELHPYLQQ-------------RELLAFCREHGIVVEAYSPLGRGKLLDDPV-------- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082502195 242 qntghklekLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:COG0656 190 ---------LAEIAEKHGKTPAQVVLRWHLQR--GVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDA 247
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
11-278 |
1.23e-29 |
|
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: 114.33 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 11 ERISCMGLGT------MYFGTktDEQTSHAILDVYVSHGGSFLDTANKYaswipGFkgGESEQLIGRWMKQRGNRQTLFV 84
Cdd:cd19148 2 LPVSRIALGTwaiggwMWGGT--DEKEAIETIHKALDLGINLIDTAPVY-----GF--GLSEEIVGKALKEYGKRDRVVI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 85 ASKVGFPYGN---IPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAW 161
Cdd:cd19148 73 ATKVGLEWDEggeVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 162 QLGEANQAAKnqgwegfsciqqFHTyLQPALwadfgnqQILTPEIQE----FCSVRKLSIVAYSP----LLAGAYTRND- 232
Cdd:cd19148 153 QMETFRKVAP------------LHT-VQPPY-------NLFEREIEKdvlpYARKHNIVTLAYGAlcrgLLSGKMTKDTk 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 233 ---------IPlpeQFRGQNTGHKL---EKLKTVAGE-LGVSANAVVLVWMM-QTPPGII 278
Cdd:cd19148 213 fegddlrrtDP---KFQEPRFSQYLaavEELDKLAQErYGKSVIHLAVRWLLdQPGVSIA 269
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-308 |
1.91e-28 |
|
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: 110.35 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 11 ERISCMGLGTMYFGT------KTDEQTSHAiLDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRgNRQTLFV 84
Cdd:cd19137 2 EKIPALGLGTWGIGGfltpdySRDEEMVEL-LKTAIELGYTHIDTAEMYG-------GGHTEELVGKAIKDF-PREDLFI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 85 ASKVgfpygnIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLG 164
Cdd:cd19137 73 VTKV------WPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 165 EANQAAKnqgwEGFSCIQ-QFHTYlqpalwadfgNQQILTPEIQEFCSVRKLSIVAYSPLLAGAYTRNDIplpeqfrgqn 243
Cdd:cd19137 147 EAISKSQ----TPIVCNQvKYNLE----------DRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRT---------- 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082502195 244 tghklekLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19137 203 -------LEEIAKNYGKTIAQIALAWLIQK-PNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-298 |
2.06e-28 |
|
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: 111.53 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGT-MYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRG-N 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYA-------NGQSEEIMGQAIKELGwP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 79 RQTLFVASKVGFPYGNIP---RSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGA 155
Cdd:cd19143 74 RSDYVVSTKIFWGGGGPPpndRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 156 SNFHAWQLGEANQAAKNQGWEGFSCIQQ----FH------TYLqpALWADFGnqqiltpeiqefcsvrkLSIVAYSPL-- 223
Cdd:cd19143 154 SEWSAQQIEEAHEIADRLGLIPPVMEQPqynlFHrervevEYA--PLYEKYG-----------------LGTTTWSPLas 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 224 --LAGAYTrNDIP------LPEQFR--------GQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVS 287
Cdd:cd19143 215 glLTGKYN-NGIPegsrlaLPGYEWlkdrkeelGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVE 293
|
330
....*....|.
gi 1082502195 288 QVEENLQSLSV 298
Cdd:cd19143 294 QLEENLKALEV 304
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-296 |
1.14e-27 |
|
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: 107.67 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGTMYFGTKtDEQTSHAILDvyvsHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRGnRQ 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRE-SPELLRRALD----LGINYFDTAEGYG-------NGNSEEIIGEALKGLR-RD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 81 TLFVASKVGFPygniPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTP---PEEFMEAFYQLKKSGKIRFAGAS- 156
Cdd:cd19105 68 KVFLATKASPR----LDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEErllNEELLEALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 157 --NFHAWqlgeANQAAKNQGWEGFSCiqqfhTYlqpalwaDFGNQQILTPEIQEFCSVRKLSIVAYSPlLAGAYTRNDIP 234
Cdd:cd19105 144 hdNMAEV----LQAAIESGWFDVIMV-----AY-------NFLNQPAELEEALAAAAEKGIGVVAMKT-LAGGYLQPALL 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082502195 235 LPEQFRGQNTGHKLekLKTVAGELGVSanaVVLVWMmqtppgiipllagSTVSQVEENLQSL 296
Cdd:cd19105 207 SVLKAKGFSLPQAA--LKWVLSNPRVD---TVVPGM-------------RNFAELEENLAAA 250
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-162 |
2.44e-27 |
|
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: 106.41 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 3 KVELGNTRERISCMGLGTMYFGTKTDEQTShAILDVYVSHGGSFLDTANKYaswipgfkgGESEQLIGRWMKQRgnRQTL 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRLSQEEAA-AIIRRALDLGINYFDTAPSY---------GDSEEKIGKALKGR--RDKV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 83 FVASKVGFPygnIPRSLKKEIilsecEKSLKRLDIETIDLYYVHA------YDAGTPPEEFMEAFYQLKKSGKIRFAGAS 156
Cdd:cd19100 69 FLATKTGAR---DYEGAKRDL-----ERSLKRLGTDYIDLYQLHAvdteedLDQVFGPGGALEALLEAKEEGKIRFIGIS 140
|
....*.
gi 1082502195 157 NfHAWQ 162
Cdd:cd19100 141 G-HSPE 145
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-308 |
1.06e-26 |
|
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: 106.36 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 3 KVELGNTRERISCMGLGTM----YFGTKTDEQTSHAILDVYVSHGGSFLDTANKYaswipgfkGGES-EQLIGRWMKQrG 77
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMglsgDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIY--------GPNTnEVLLGKALKD-G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 78 NRQTLFVASKVGFPYGNIPRSLKK---EIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAG 154
Cdd:cd19145 73 PREKVQLATKFGIHEIGGSGVEVRgdpAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 155 asnfhawqLGEANQaaknqgwegfSCIQQFHTY-------LQPALWAdfgnqQILTPEIQEFCSVRKLSIVAYSPL---- 223
Cdd:cd19145 153 --------LSEASA----------DTIRRAHAVhpitavqLEWSLWT-----RDIEEEIIPTCRELGIGIVPYSPLgrgf 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 224 ----------LAGAYTRNDIPlpeQFRGQNTGHK---LEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVE 290
Cdd:cd19145 210 fagkakleelLENSDVRKSHP---RFQGENLEKNkvlYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLN 286
|
330
....*....|....*...
gi 1082502195 291 ENLQSLSVTLSKKQLEQL 308
Cdd:cd19145 287 QNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
23-305 |
5.01e-25 |
|
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: 101.95 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 23 FGTKTDEQTSHAILDVYVSHGGSFLDTANKYaswipGFKGGESEQLIGRWMKQ--RGNRQTLFVASKVGF-----PYGNI 95
Cdd:cd19089 22 FGDYTSPEEARELLRTAFDLGITHFDLANNY-----GPPPGSAEENFGRILKRdlRPYRDELVISTKAGYgmwpgPYGDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 96 PrSLKKeiILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQAAKNQGw 175
Cdd:cd19089 97 G-SRKY--LLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 176 egfsciqqfhtylQPALwADFGNQQILTPEIQEFCS--VRKLSI--VAYSPL----LAGAYTRNDIPLPEQFR------- 240
Cdd:cd19089 173 -------------VPLI-IHQPRYSLLDRWAEDGLLevLEEAGIgfIAFSPLaqglLTDKYLNGIPPDSRRAAeskflte 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 241 GQNTGHKLEKLKT---VAGELGVSANAVVLVWMMQTpPGIIPLLAG-STVSQVEENLQSL-SVTLSKKQL 305
Cdd:cd19089 239 EALTPEKLEQLRKlnkIAAKRGQSLAQLALSWVLRD-PRVTSVLIGaSSPSQLEDNVAALkNLDFSEEEL 307
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
17-308 |
8.79e-25 |
|
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: 100.38 E-value: 8.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 17 GLGTMYFGTKTDEQTSHAILDVY--VSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVASKVGFPYG 93
Cdd:cd19120 10 GTGTAWYKSGDDDIQRDLVDSVKlaLKAGFRHIDTAEMY----------GNEKEVGEALKESGvPREDLFITTKVSPGIK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 94 NIPRSLkkeiilsecEKSLKRLDIETIDLYYVH----AYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQA 169
Cdd:cd19120 80 DPREAL---------RKSLAKLGVDYVDLYLIHspffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 170 AK-----NQgwegfscIqQFHTYLQPalwadfgnqqiLTPEIQEFCsvRKLSIV--AYSPLlagaytrndIPLpEQFRGq 242
Cdd:cd19120 151 AKikpavNQ-------I-EFHPYLYP-----------QQPALLEYC--REHGIVvsAYSPL---------SPL-TRDAG- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082502195 243 ntGHKLEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19120 199 --GPLDPVLEKIAEKYGVTPAQVLLRWALQK--GIVVVTTSSKEERMKEYLEAFDFELTEEEVEEI 260
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
23-306 |
1.97e-24 |
|
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: 100.56 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 23 FGTKTDEQTSHAILDVYVSHGGSFLDTANKYaswipGFKGGESEQLIGRWMKQ--RGNRQTLFVASKVGF-----PYGNI 95
Cdd:cd19151 23 FGDVDRYENSRAMLRRAFDLGITHFDLANNY-----GPPPGSAEENFGRILKEdlKPYRDELIISTKAGYtmwpgPYGDW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 96 PrslKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQAAKNQgw 175
Cdd:cd19151 98 G---SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDL-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 176 eGFSCIQQFHTYLQPALWADFGNQQILTPEiqefcsvrKLSIVAYSPLLAGAYTR---NDIPL------PEQF--RGQNT 244
Cdd:cd19151 173 -GTPCLIHQPKYSMFNRWVEEGLLDVLEEE--------GIGCIAFSPLAQGLLTDrylNGIPEdsraakGSSFlkPEQIT 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082502195 245 GHKLEK---LKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVT-LSKKQLE 306
Cdd:cd19151 244 EEKLAKvrrLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNReFSEEELA 309
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-310 |
2.09e-24 |
|
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: 99.26 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 11 ERISCMGLGTM-YFGTKTDEQTSHAiLDVYVSHggsfLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVASKV 88
Cdd:cd19140 6 VRIPALGLGTYpLTGEECTRAVEHA-LELGYRH----IDTAQMY----------GNEAQVGEAIAASGvPRDELFLTTKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 89 GfpygniPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQ 168
Cdd:cd19140 71 W------PDNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 169 AAKnqgwEGFSCIQ-QFHTYLqpalwadfgNQQILTpeiqEFCSVRKLSIVAYSPLLAGAYTRNDIplpeqfrgqntghk 247
Cdd:cd19140 145 LSE----APLFTNQvEYHPYL---------DQRKLL----DAAREHGIALTAYSPLARGEVLKDPV-------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082502195 248 lekLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19140 194 ---LQEIGRKHGKTPAQVALRWLLQQ-EGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-236 |
3.45e-24 |
|
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: 98.46 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 14 SCMGLGTMYFG---TKTDEQTSHAILDVYVSHGGSFLDTANKYaswipgfkgGESEQLIGRWMKQRgNRQTLFVASKVG- 89
Cdd:cd19095 1 SVLGLGTSGIGrvwGVPSEAEAARLLNTALDLGINLIDTAPAY---------GRSEERLGRALAGL-RRDDLFIATKVGt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 90 -FPYGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAwqlgEANQ 168
Cdd:cd19095 71 hGEGGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGE----ELEA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082502195 169 AAKnqgWEGFSCIQQFHTYLQPAlwadfgNQQILtPEIQEfcsvRKLSIVAYSPLLAGAYTRNDIPLP 236
Cdd:cd19095 147 AIA---SGVFDVVQLPYNVLDRE------EEELL-PLAAE----AGLGVIVNRPLANGRLRRRVRRRP 200
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-298 |
2.26e-23 |
|
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: 97.75 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGT-MYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASwipgfkgGESEQLIGRWMKQRGNR 79
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAA-------GKAERTLGNILKSKGWR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 80 QTLFVASKVGFPYGN--IPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASN 157
Cdd:cd19160 76 RSSYVVTTKIYWGGQaeTERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 158 FHAWQLGEANQAAKNQGWEGFSCIQQFHTYLQPAlwadfgNQQILTPEIQEFCSVrklSIVAYSPLLAGAYT-RNDIPLP 236
Cdd:cd19160 156 WSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQRE------KVEMQLPELYHKIGV---GSVTWSPLACGLITgKYDGRVP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 237 EQFR-----------------GQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAG-STVSQVEENLQSLSV 298
Cdd:cd19160 227 DTCRaavkgyqwlkekvqseeGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRS-EGVSSVLLGvSSAEQLIENLGSIQV 305
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-294 |
1.83e-21 |
|
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: 92.38 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 12 RISCMGLGTmYFGTKTDEQTSHA--ILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGR-----WMKQRGNRQTLFV 84
Cdd:cd19099 2 TLSSLGLGT-YRGDSDDETDEEYreALKAALDSGINVIDTAINYR-------GGRSERLIGKalrelIEKGGIKRDEVVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 85 ASKVGFPYGNIPRSLKK---------------------------EIILSECEKSLKRLDIETIDLYYVH---AYDAGTPP 134
Cdd:cd19099 74 VTKAGYIPGDGDEPLRPlkyleeklgrglidvadsaglrhcispAYLEDQIERSLKRLGLDTIDLYLLHnpeEQLLELGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 135 EEFM-------EAFYQLKKSGKIRFAG-ASNF---------HAWQLGEANQAAKNQGWE--GFSCIQ-QFHtYLQPALWA 194
Cdd:cd19099 154 EEFYdrleeafEALEEAVAEGKIRYYGiSTWDgfrappalpGHLSLEKLVAAAEEVGGDnhHFKVIQlPLN-LLEPEALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 195 DFGNQQILTPEIQEFCSVRKLSIVAYSPLLAGAYTRN--DIPLPEQFRGQNTGHKLekLKTVAGELGVSanaVVLVWMmq 272
Cdd:cd19099 233 EKNTVKGEALSLLEAAKELGLGVIASRPLNQGQLLGElrLADLLALPGGATLAQRA--LQFARSTPGVD---SALVGM-- 305
|
330 340
....*....|....*....|..
gi 1082502195 273 tppgiipllagSTVSQVEENLQ 294
Cdd:cd19099 306 -----------RRPEHVDENLA 316
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-298 |
8.35e-21 |
|
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: 90.87 E-value: 8.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGT-MYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASwipgfkgGESEQLIGRWMKQRG-N 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 79 RQTLFVASKVGFP-YGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASN 157
Cdd:cd19159 74 RSSLVITTKLYWGgKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 158 FHAWQLGEANQAAKNQGWEGFSCIQ-QFHTYLQPALwadfgnqQILTPEIQEFCSVRKLSivaYSPLLAGAYT---RNDI 233
Cdd:cd19159 154 WSAMEIMEAYSVARQFNMIPPVCEQaEYHLFQREKV-------EVQLPELYHKIGVGAMT---WSPLACGIISgkyGNGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 234 P-----------------LPEQFRGQNTghKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSL 296
Cdd:cd19159 224 PessraslkcyqwlkeriVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 301
|
..
gi 1082502195 297 SV 298
Cdd:cd19159 302 QV 303
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-297 |
1.62e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 88.74 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 16 MGLGTMYFGT---------KTDEQTSHAILDVYVSHGGSFLDTANKYaswipgfkgGESEQLIGRWMKqrgNRQTLFVAS 86
Cdd:cd19097 3 LALGTAQFGLdygianksgKPSEKEAKKILEYALKAGINTLDTAPAY---------GDSEKVLGKFLK---RLDKFKIIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 87 KVGFPYGNIPRSlkKEIILSECEKSLKRLDIETIDLYYVHAY-DAGTPPEEFMEAFYQLKKSGKIRFAGASnFHAWQlgE 165
Cdd:cd19097 71 KLPPLKEDKKED--EAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVS-VYSPE--E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 166 ANQAAKNQGWEgfsciqqfhtYLQ-PALWADfgnQQILTPEIQEFCSVRKLSIVAYSPLLAGAYTRNDIPLPEQFRGQNT 244
Cdd:cd19097 146 LEKALESFKID----------IIQlPFNILD---QRFLKSGLLAKLKKKGIEIHARSVFLQGLLLMEPDKLPAKFAPAKP 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1082502195 245 ghKLEKLKTVAGELGVSANAVVLVWMMQTpPGIIPLLAG-STVSQVEENLQSLS 297
Cdd:cd19097 213 --LLKKLHELAKKLGLSPLELALGFVLSL-PEIDKIVVGvDSLEQLKEIIAAFK 263
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
17-310 |
1.73e-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: 88.84 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 17 GLGTmyFGTKtDEQTSHAILDVYVSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQRG-----NRQTLFVASKVGfp 91
Cdd:cd19136 5 GLGT--FRLR-GEEEVRQAVDAALKAGYRLIDTASVY----------RNEADIGKALRDLLpkyglSREDIFITSKLA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 92 ygniPRSLKKEIILSECEKSLKRLDIETIDLYYVH-AYDAGTPPE---------EFMEAFYQLKKSGKIRFAGASNFHAW 161
Cdd:cd19136 70 ----PKDQGYEKARAACLGSLERLGTDYLDLYLIHwPGVQGLKPSdprnaelrrESWRALEDLYKEGKLRAIGVSNYTVR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 162 QLGEANQAAK-----NQgwegfsciQQFHTYLQpalwadfgnqqilTPEIQEFCSVRKLSIVAYSPLLAGAYTRNDIPLP 236
Cdd:cd19136 146 HLEELLKYCEvppavNQ--------VEFHPHLV-------------QKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTV 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082502195 237 eqfrgqntghkleklKTVAGELGVSANAVVLVWMMQTPPGIIPLlagSTVSQ-VEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19136 205 ---------------LAIAKKYGRTPAQVLLRWALQQGIGVIPK---STNPErIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
6-296 |
2.37e-20 |
|
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: 89.45 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 6 LGNTRERISCMGLGTMY-FGTKTDEQTSHAILDVYVSHGGSFLDTANkyaswipGFKGGESEQLIGRWMKQRG-NRQTLF 83
Cdd:cd19142 6 LGKSGLRVSNVGLGTWStFSTAISEEQAEEIVTLAYENGINYFDTSD-------AFTSGQAETELGRILKKKGwKRSSYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 84 VASKVGFPYGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQL 163
Cdd:cd19142 79 VSTKIYWSYGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 164 GEANQAAKNqgwegFSCI------QQFHTYLQ-------PALWADFGNQQI--------LTPEIQEFCSVRKLSIVAYSP 222
Cdd:cd19142 159 MEAFSIARQ-----FNCPtpiceqSEYHMFCRekmelymPELYNKVGVGLItwsplslgLDPGISEETRRLVTKLSFKSS 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082502195 223 LLAGAYTRNDIPLpeqfRGQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSL 296
Cdd:cd19142 234 KYKVGSDGNGIHE----ETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSL 303
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
6-298 |
5.35e-20 |
|
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: 88.27 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 6 LGNTRERISCMGLGT-MYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMKQRG-NRQTLF 83
Cdd:cd19141 5 LGKSGLRVSCLGLGTwVTFGSQISDEVAEELVTLAYENGINLFDTAEVYA-------AGKAEIVLGKILKKKGwRRSSYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 84 VASKVGFP-YGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQ 162
Cdd:cd19141 78 ITTKIFWGgKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAME 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 163 LGEANQAAKNQGWEGFSCIQ-QFHTYLQPALwadfgnqQILTPEIQEFCSVrklSIVAYSPLLAGAYT-RNDIPLPEQFR 240
Cdd:cd19141 158 IMEAYSVARQFNLIPPIVEQaEYHLFQREKV-------EMQLPELFHKIGV---GAMTWSPLACGILSgKYDDGVPEYSR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082502195 241 GQNTGH-----------------KLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSV 298
Cdd:cd19141 228 ASLKGYqwlkekilseegrrqqaKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-310 |
7.56e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 88.09 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 2 QKVELGNTRERISCMGLGTMYFG---TKTDEQTSHAILDVYVSHGGSFLDTAnkyaswiPGFKGGESEQLIGRWMKqrGN 78
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGglmGRTTREEQIAAVRRALDLGINFFDTA-------PSYGDGKSEENLGRALK--GL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 79 RQTLFVASKVGFP-------YGNIPRSLkkeiilsecEKSLKRLDIETIDLYYVH--------AYDAGTP-------PEE 136
Cdd:cd19104 72 PAGPYITTKVRLDpddlgdiGGQIERSV---------EKSLKRLKRDSVDLLQLHnrigderdKPVGGTLsttdvlgLGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 137 FMEAFYQLKKSGKIRFAGasnFHAWqlGEANQAAKNQGWEGFSCIQQFHTYLQP-------ALWADFGNQQILtpeiqEF 209
Cdd:cd19104 143 VADAFERLRSEGKIRFIG---ITGL--GNPPAIRELLDSGKFDAVQVYYNLLNPsaaearpRGWSAQDYGGII-----DA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 210 CSVRKLSIVAYSPLLAGAYT------RNDIPLPEQFRGQNTGhKLEKLKTVAGELGVS--ANAVVLVWMMqtpPGIIPLL 281
Cdd:cd19104 213 AAEHGVGVMGIRVLAAGALTtsldrgREAPPTSDSDVAIDFR-RAAAFRALAREWGETlaQLAHRFALSN---PGVSTVL 288
|
330 340 350
....*....|....*....|....*....|.
gi 1082502195 282 AG-STVSQVEENLQSLSV-TLSKKQLEQLAS 310
Cdd:cd19104 289 VGvKNREELEEAVAAEAAgPLPAENLARLEA 319
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
16-295 |
1.04e-19 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 86.84 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 16 MGLGTMYFG---TKTDEQTSHAILDVYVSHGGSFLDTANKYaswipgfkgGESEQLIGRWMKQRGnRQTLFVASKVG-FP 91
Cdd:cd19090 3 LGLGTAGLGgvfGGVDDDEAVATIRAALDLGINYIDTAPAY---------GDSEERLGLALAELP-REPLVLSTKVGrLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 92 YGNIPRSLKKeiILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEF-----MEAFYQLKKSGKIRFAG-ASN--FHAWQL 163
Cdd:cd19090 73 EDTADYSADR--VRRSVEESLERLGRDRIDLLMIHDPERVPWVDILapggaLEALLELKEEGLIKHIGlGGGppDLLRRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 164 GEANQaaknqgwegFSCIQQFHTYlqPALWadfgnQQILTPEIqEFCSVRKLSIVAYSPLLAGAYTRND---IPLPEQFR 240
Cdd:cd19090 151 IETGD---------FDVVLTANRY--TLLD-----QSAADELL-PAAARHGVGVINASPLGMGLLAGRPperVRYTYRWL 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082502195 241 GQNTGHKLEKLKTVAGELGVSANAVVLVWMMQtPPGIIPLLAG-STVSQVEENLQS 295
Cdd:cd19090 214 SPELLDRAKRLYELCDEHGVPLPALALRFLLR-DPRISTVLVGaSSPEELEQNVAA 268
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
23-306 |
2.02e-19 |
|
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: 86.74 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 23 FGTKTDEQTSHAILDVYVSHGGSFLDTANKYaswipGFKGGESEQLIGRWMKQ--RGNRQTLFVASKVGF-----PYGNI 95
Cdd:cd19150 23 FGDDTPLETQRAILRTAFDLGITHFDLANNY-----GPPPGSAEENFGRILREdfAGYRDELIISTKAGYdmwpgPYGEW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 96 PrslKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEAnqAAKNQGW 175
Cdd:cd19150 98 G---SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREA--AAILREL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 176 eGFSCIQQFHTYLQPALWADfgnQQILTPEIQEFcsvrKLSIVAYSPLLAGAYTR---NDIP----------LPEQFRGQ 242
Cdd:cd19150 173 -GTPLLIHQPSYNMLNRWVE---ESGLLDTLQEL----GVGCIAFTPLAQGLLTDkylNGIPegsraskersLSPKMLTE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082502195 243 NTGHKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSL-SVTLSKKQLE 306
Cdd:cd19150 245 ANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALdNLTFSADELA 309
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-309 |
3.23e-19 |
|
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: 84.71 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 13 ISCMGLGTmyFGTKtDEQTSHAILDVyVSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVASKVGFp 91
Cdd:cd19139 1 IPAFGLGT--FRLK-DDVVIDSVRTA-LELGYRHIDTAQIY----------DNEAAVGQAIAESGvPRDELFITTKIWI- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 92 ygnipRSLKKEIILSECEKSLKRLDIETIDLYYVH--AYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQA 169
Cdd:cd19139 66 -----DNLSKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 170 ------AKNQgwegfsciQQFHTYLQpalwadfgnqqilTPEIQEFCSVRKLSIVAYSPLlagAYTR-NDIPLpeqfrgq 242
Cdd:cd19139 141 vgagaiATNQ--------IELSPYLQ-------------NRKLVAHCKQHGIHVTSYMTL---AYGKvLDDPV------- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082502195 243 ntghklekLKTVAGELGVSANAVVLVWMMQTPPGIIPllAGSTVSQVEENLQSLSVTLSKKQLEQLA 309
Cdd:cd19139 190 --------LAAIAERHGATPAQIALAWAMARGYAVIP--SSTKREHLRSNLLALDLTLDADDMAAIA 246
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-310 |
3.76e-19 |
|
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: 85.63 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 12 RISCMGLGTmyFGTKTDEQTshAILDVYVSHGGSFLDTANKYaswipgfkggESEQLIG---RWMKQRG--NRQTLFVAS 86
Cdd:cd19111 3 PMPVIGLGT--YQSPPEEVR--AAVDYALFVGYRHIDTALSY----------QNEKAIGealKWWLKNGklKREEVFITT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 87 KVgFPYGNIPRSLKKEIilsecEKSLKRLDIETIDLYYVH-------------AYDAGTPPEEFMEAFYQLKKSGKIRFA 153
Cdd:cd19111 69 KL-PPVYLEFKDTEKSL-----EKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 154 GASNFHAWQLGEANQAAKNQGwegfSCIQ-QFHTYLQpalwadfgnQQiltpEIQEFCSVRKLSIVAYSPLlaGAYTR-N 231
Cdd:cd19111 143 GLSNFNPRQINKILAYAKVKP----SNLQlECHAYLQ---------QR----ELRKFCNKKNIVVTAYAPL--GSPGRaN 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082502195 232 DIPLPEQFrgqnTGHKLEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19111 204 QSLWPDQP----DLLEDPTVLAIAKELDKTPAQVLLRFVLQR--GTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKT 276
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-297 |
7.52e-19 |
|
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: 84.15 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 14 SCMGLGTMYF----GTKTDEQTSHAILDVYVSHGGSFLDTAnkyaswiPGFKGGESEQLIGRWMKqRGNRQTLFVASKvg 89
Cdd:cd19096 1 SVLGFGTMRLpesdDDSIDEEKAIEMIRYAIDAGINYFDTA-------YGYGGGKSEEILGEALK-EGPREKFYLATK-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 90 FPYGNIPRS--LKKEIilsecEKSLKRLDIETIDLYYVHA-----YDAGTPPEEFMEAFYQLKKSGKIRFAGASnFHAwQ 162
Cdd:cd19096 71 LPPWSVKSAedFRRIL-----EESLKRLGVDYIDFYLLHGlnspeWLEKARKGGLLEFLEKAKKEGLIRHIGFS-FHD-S 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 163 LGEANQAAKNQGWEgfSCIQQFHtYLqpalwaDFGNQQiLTPEIQEFCSvRKLSIVAYSPLLAGaytrndiplpeqFRGQ 242
Cdd:cd19096 144 PELLKEILDSYDFD--FVQLQYN-YL------DQENQA-GRPGIEYAAK-KGMGVIIMEPLKGG------------GLAN 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082502195 243 NTGHKLEKLKtvAGELGVSANAVVLVWmmqTPPGIIPLLAG-STVSQVEENLQSLS 297
Cdd:cd19096 201 NPPEALAILC--GAPLSPAEWALRFLL---SHPEVTTVLSGmSTPEQLDENIAAAD 251
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-308 |
1.98e-18 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 84.27 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGTMY-FGTKTDEQTSHAILDVYVSHGGSFLDTANKYaswipGFKGGESEQLIGRWMKQ--RG 77
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHnFGHVNALESQRAILRKAFDLGITHFDLANNY-----GPPPGSAEENFGRLLREdfAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 78 NRQTLFVASKVGF-----PYGNiprSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRF 152
Cdd:PRK09912 88 YRDELIISTKAGYdmwpgPYGS---GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 153 AGASNFHAWQlgEANQAAKNQGWEGFSCIQQfHTYLQPALWADfgnQQILTPEIQEfcsvRKLSIVAYSP----LLAGAY 228
Cdd:PRK09912 165 VGISSYSPER--TQKMVELLREWKIPLLIHQ-PSYNLLNRWVD---KSGLLDTLQN----NGVGCIAFTPlaqgLLTGKY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 229 TRNdipLPEQFRGQNTGHK----------------LEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEEN 292
Cdd:PRK09912 235 LNG---IPQDSRMHREGNKvrgltpkmlteanlnsLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEEN 311
|
330
....*....|....*..
gi 1082502195 293 LQSLS-VTLSKKQLEQL 308
Cdd:PRK09912 312 VQALNnLTFSTEELAQI 328
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
6-298 |
4.15e-18 |
|
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: 83.21 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 6 LGNTRERISCMGLGT-MYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASwipgfkgGESEQLIGRWMKQRGNRQTLFV 84
Cdd:cd19158 6 LGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGWRRSSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 85 ASKVGFPYGN--IPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQ 162
Cdd:cd19158 79 ITTKIFWGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 163 LGEANQAAKNQGWEGFSCIQ-QFHTYLQPALwadfgnqQILTPEIQEFCSVRKLSivaYSPLLAG-----------AYTR 230
Cdd:cd19158 159 IMEAYSVARQFNLIPPICEQaEYHMFQREKV-------EVQLPELFHKIGVGAMT---WSPLACGivsgkydsgipPYSR 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082502195 231 ---------NDIPLPEQFRGQNTghKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSV 298
Cdd:cd19158 229 aslkgyqwlKDKILSEEGRRQQA--KLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 303
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-309 |
5.90e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 82.38 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 19 GTMYFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASwipgfkgGESEQLIGRWMKQRgNRQTLFVASKvgF-PYGnipR 97
Cdd:cd19103 21 GDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGM-------GASEKILGEFLKRY-PREDYIISTK--FtPQI---A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 98 SLKKEIILSECEKSLKRLDIETIDLYYVH-AYDAgtppEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQAAKNQGWE 176
Cdd:cd19103 88 GQSADPVADMLEGSLARLGTDYIDIYWIHnPADV----ERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAKAGVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 177 gFSCIQQfHTYLQPALWADFGnqqiltpeIQEFCSVRKLSIVAYSPL----LAGAYTRNDiPLPE-QFRGQNTGHKLEKL 251
Cdd:cd19103 164 -LSAVQN-HYSLLYRSSEEAG--------ILDYCKENGITFFAYMVLeqgaLSGKYDTKH-PLPEgSGRAETYNPLLPQL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082502195 252 -------KTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSK---KQLEQLA 309
Cdd:cd19103 233 eeltavmAEIGAKHGASIAQVAIAWAIAK--GTTPIIGVTKPHHVEDAARAASITLTDdeiKELEQLA 298
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
3-310 |
1.92e-15 |
|
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: 74.73 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 3 KVELGNTRErISCMGLGTmyFGTKTDEQTSHAIlDVYVSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQT 81
Cdd:cd19157 1 TVTLNNGVK-MPWLGLGV--FKVEEGSEVVNAV-KTALKNGYRSIDTAAIY----------GNEEGVGKGIKESGiPREE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 82 LFVASKV-----GFpygniprslkkEIILSECEKSLKRLDIETIDLYYVHaYDAGTPPEEFMEAFYQLKKSGKIRFAGAS 156
Cdd:cd19157 67 LFITSKVwnadqGY-----------DSTLKAFEASLERLGLDYLDLYLIH-WPVKGKYKETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 157 NFHAWQLGEANQAAK-----NQgwegfsciQQFHTYLqpalwadfgNQQiltpEIQEFCSVRKLSIVAYSPLLAGAYTRN 231
Cdd:cd19157 135 NFQVHHLEDLLADAEivpmvNQ--------VEFHPRL---------TQK----ELRDYCKKQGIQLEAWSPLMQGQLLDN 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082502195 232 DIplpeqfrgqntghklekLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19157 194 PV-----------------LKEIAEKYNKSVAQVILRWDLQN--GVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDA 253
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
12-310 |
1.95e-14 |
|
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: 72.44 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 12 RISCMGLGTMyfgtKTDEQTSHAILDVYVSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQ-----RGNRQTLFVAS 86
Cdd:cd19154 11 KMPLIGLGTW----QSKGAEGITAVRTALKAGYRLIDTAFLY----------QNEEAIGEALAElleegVVKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 87 KVGFPYgniprsLKKEIILSECEKSLKRLDIETIDLYYVHA-------------------YDAGTPPEEFMEAFYQLKKS 147
Cdd:cd19154 77 KLWTHE------HAPEDVEEALRESLKKLQLEYVDLYLIHApaafkddegesgtmengmsIHDAVDVEDVWRGMEKVYDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 148 GKIRFAGASNFHAWQLGEANQAAK----NQGWEgfsCiqqfHTYLQpalwadfgnqqilTPEIQEFCSVRKLSIVAYSPL 223
Cdd:cd19154 151 GLTKAIGVSNFNNDQIQRILDNARvkphNNQVE---C----HLYFP-------------QKELVEFCKKHNISVTSYATL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 224 laGAYTRNDIPLPEQFRGQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKK 303
Cdd:cd19154 211 --GSPGRANFTKSTGVSPAPNLLQDPIVKAIAEKHGKTPAQVLLRYLLQR--GIAVIPKSATPSRIKENFNIFDFSLSEE 286
|
....*..
gi 1082502195 304 QLEQLAS 310
Cdd:cd19154 287 DMATLEE 293
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-310 |
5.89e-14 |
|
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: 70.43 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 4 VELGNTRErISCMGLGTMYFGTKTDEQTSHAILDVYVSHggsfLDTANKYASwipgfkggesEQLIGRWMKQRG-NRQTL 82
Cdd:cd19135 5 VRLSNGVE-MPILGLGTSHSGGYSHEAVVYALKECGYRH----IDTAKRYGC----------EELLGKAIKESGvPREDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 83 FVASKVgFP--YGNipRSLKKEiilseCEKSLKRLDIETIDLYYVHAYDAGTPP-------EEFMEAFYQLKKSGKIRFA 153
Cdd:cd19135 70 FLTTKL-WPsdYGY--ESTKQA-----FEASLKRLGVDYLDLYLLHWPDCPSSGknvketrAETWRALEELYDEGLCRAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 154 GASNF---HAWQLGE-------ANQAaknqgwegfsciqQFHTYLQPAlwadfgnqqiltpEIQEFCSVRKLSIVAYSPL 223
Cdd:cd19135 142 GVSNFlieHLEQLLEdcsvvphVNQV-------------EFHPFQNPV-------------ELIEYCRDNNIVFEGYCPL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 224 LAGAytrndiPLPEqfrgqntghklEKLKTVAGELGVSANAVVLVWMMQTPPGIIPllaGST-VSQVEENLQSLSVTLSK 302
Cdd:cd19135 196 AKGK------ALEE-----------PTVTELAKKYQKTPAQILIRWSIQNGVVTIP---KSTkEERIKENCQVFDFSLSE 255
|
....*...
gi 1082502195 303 KQLEQLAS 310
Cdd:cd19135 256 EDMATLDS 263
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-309 |
6.31e-14 |
|
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: 70.38 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTmyFGTKTDEQTsHAILDVyVSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVAS 86
Cdd:cd19132 2 NDGTQIPAIGFGT--YPLKGDEGV-EAVVAA-LQAGYRLLDTAFNY----------ENEGAVGEAVRRSGvPREELFVTT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 87 KvgfpygnIP-RSLKKEIILSECEKSLKRLDIETIDLY-----------YVHAYdagtppeefmEAFYQLKKSGKIRFAG 154
Cdd:cd19132 68 K-------LPgRHHGYEEALRTIEESLYRLGLDYVDLYlihwpnpsrdlYVEAW----------QALIEAREEGLVRSIG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 155 ASNFHAWQLGEANQA-----AKNQgwegfscIQqfhtyLQPALwadfgNQQiltpEIQEFCsvRKLSIV--AYSPLlaga 227
Cdd:cd19132 131 VSNFLPEHLDRLIDEtgvtpAVNQ-------IE-----LHPYF-----PQA----EQRAYH--REHGIVtqSWSPL---- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 228 yTRNDIPLPEQfrgqntghkleKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQ 307
Cdd:cd19132 184 -GRGSGLLDEP-----------VIKAIAEKHGKTPAQVVLRWHVQL--GVVPIPKSANPERQRENLAIFDFELSDEDMAA 249
|
..
gi 1082502195 308 LA 309
Cdd:cd19132 250 IA 251
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
4-308 |
2.77e-13 |
|
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: 68.23 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 4 VELGNTrERISCMGLGT--MYFGTKTDEQTSHAILDVYVShggsfLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQ 80
Cdd:cd19126 1 VTLNNG-TRMPWLGLGVfqTPDGDETERAVQTALENGYRS-----IDTAAIY----------KNEEGVGEAIRESGvPRE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 81 TLFVASKVGfpygniPRSLKKEIILSECEKSLKRLDIETIDLYYVHaydagTP-PEEFME---AFYQLKKSGKIRFAGAS 156
Cdd:cd19126 65 ELFVTTKLW------NDDQRARRTEDAFQESLDRLGLDYVDLYLIH-----WPgKDKFIDtwkALEKLYASGKVKAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 157 NFHAWQLGEANQAAK-----NQgwegfsciQQFHTYLQpalwadfgnqqilTPEIQEFCSVRKLSIVAYSPLLAGAYTRN 231
Cdd:cd19126 134 NFQEHHLEELLAHADvvpavNQ--------VEFHPYLT-------------QKELRGYCKSKGIVVEAWSPLGQGGLLSN 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082502195 232 diplpeqfrgqntghklEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19126 193 -----------------PVLAAIGEKYGKSAAQVVLRWDIQH--GVVTIPKSVHASRIKENADIFDFELSEDDMTAI 250
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-154 |
2.82e-13 |
|
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: 68.73 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 1 MQKVELGNTRERISCMGLGTMYFGT---KTDEQTSHAILDVYVSHGGSFLDTAnkyaswiPGFKGGESEQLIGRWMKQrG 77
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGvfgPVDEEEAIRTVHEALDSGINYIDTA-------PWYGQGRSETVLGKALKG-I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 78 NRQTLFVASKVGfPYG-NIPRSL--KKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPP----EEFMEAFYQLKKSGKI 150
Cdd:cd19163 73 PRDSYYLATKVG-RYGlDPDKMFdfSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLdqilNETLPALQKLKEEGKV 151
|
....
gi 1082502195 151 RFAG 154
Cdd:cd19163 152 RFIG 155
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-309 |
4.11e-13 |
|
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: 68.21 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTmyFGTKTDEQTshAILDVYVSHGGSFLDTANKYaswipgfkGGESE--QLIGRWMKQRGN--RQTLF 83
Cdd:cd19118 2 NTGNKIPAIGLGT--WQAEPGEVG--AAVKIALKAGYRHLDLAKVY--------QNQHEvgQALKELLKEEPGvkREDLF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 84 VASKVgfpYGNiprSLKKEIILSECEKSLKRLDIETIDLYYVH---AYDAGTPPEEFM---------------------E 139
Cdd:cd19118 70 ITSKL---WNN---SHRPEYVEPALDDTLKELGLDYLDLYLIHwpvAFKPTGDLNPLTavptnggevdldlsvslvdtwK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 140 AFYQLKKSGKIRFAGASNFHAWQLGEANQAaknqgwegfsciqqfhTYLQPALwadfgNQ-----QILTPEIQEFCSVRK 214
Cdd:cd19118 144 AMVELKKTGKVKSIGVSNFSIDHLQAIIEE----------------TGVVPAV-----NQieahpLLLQDELVDYCKSKN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 215 LSIVAYSPLlaGAYTRNDIPLpeqfrgqnTGHklEKLKTVAGELGVSANAVVLVWMMQTPPGIIPllAGSTVSQVEENLQ 294
Cdd:cd19118 203 IHITAYSPL--GNNLAGLPLL--------VQH--PEVKAIAAKLGKTPAQVLIAWGIQRGHSVIP--KSVTPSRIRSNFE 268
|
330
....*....|....*
gi 1082502195 295 slSVTLSKKQLEQLA 309
Cdd:cd19118 269 --QVELSDDEFNAVT 281
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
8-310 |
6.16e-13 |
|
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: 67.94 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTMyfgTKTDEQTSHAIlDVYVSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQ-----RGNRQTL 82
Cdd:cd19155 7 NNGEKMPVVGLGTW---QSSPEEIETAV-DTALEAGYRHIDTAYVY----------RNEAAIGNVLKKwidsgKVKREEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 83 FVASKVGfPYGNIPRSLKKEIilsecEKSLKRLDIETIDLYYVHA---------YDAGTPPEEFMEAFYQ---------- 143
Cdd:cd19155 73 FIVTKLP-PGGNRREKVEKFL-----LKSLEKLQLDYVDLYLIHFpvgslskedDSGKLDPTGEHKQDYTtdlldiwkam 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 144 --LKKSGKIRFAGASNFHAWQLGEANQAAKNQGwegfSCIQ-QFHTYLQpalwadfgnQQiltpEIQEFCSVRKLSIVAY 220
Cdd:cd19155 147 eaQVDQGLTRSIGLSNFNREQMARILKNARIKP----ANLQvELHVYLQ---------QK----DLVDFCSTHSITVTAY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 221 SPL----LAGAY-TRNDIP--LPEQFrgqntghKLEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENL 293
Cdd:cd19155 210 APLgspgAAHFSpGTGSPSgsSPDLL-------QDPVVKAIAERHGKSPAQVLLRWLMQR--GVVVIPKSTNAARIKENF 280
|
330
....*....|....*..
gi 1082502195 294 QSLSVTLSKKQLEQLAS 310
Cdd:cd19155 281 QVFDFELTEADMAKLSS 297
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-310 |
7.79e-13 |
|
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: 67.21 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTmyFGTKTDEQTSHAILDVyVSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVAS 86
Cdd:cd19133 4 NNGVEMPILGFGV--FQIPDPEECERAVLEA-IKAGYRLIDTAAAY----------GNEEAVGRAIKKSGiPREELFITT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 87 KV---GFPYGNIPRSLkkeiilsecEKSLKRLDIETIDLYYVH--------AYDAgtppeefMEAFYqlkKSGKIRFAGA 155
Cdd:cd19133 71 KLwiqDAGYEKAKKAF---------ERSLKRLGLDYLDLYLIHqpfgdvygAWRA-------MEELY---KEGKIRAIGV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 156 SNFHAWQLGEANQAAK-----NQgwegfsciQQFHTYlqpalwadfgNQQIltpEIQEFCSVRKLSIVAYSPLLAGaytR 230
Cdd:cd19133 132 SNFYPDRLVDLILHNEvkpavNQ--------IETHPF----------NQQI---EAVEFLKKYGVQIEAWGPFAEG---R 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 231 NDIplpeqFrgQNtghklEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19133 188 NNL-----F--EN-----PVLTEIAEKYGKSVAQVILRWLIQR--GIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAA 253
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-310 |
9.12e-13 |
|
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: 67.37 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTMYFGTKtdeQTSHAIlDVYVSHGGSFLDTANKYaswipgfkGGESEqlIGRWMKQRG-----NRQTL 82
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPG---VVGNAV-KTAIKEGYRHIDCAAIY--------GNEKE--IGKALKKLFedgvvKREDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 83 FVASKVGFPYgniprsLKKEIILSECEKSLKRLDIETIDLYYVH------AYDAGTPPEEFME--------AFYQLKKSG 148
Cdd:cd19125 72 FITSKLWCTD------HAPEDVPPALEKTLKDLQLDYLDLYLIHwpvrlkKGAHMPEPEEVLPpdipstwkAMEKLVDSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 149 KIRFAGASNFHAWQLGEANQAAKnqgwegfsciqqfhtyLQPALwadfgNQQILTP-----EIQEFCSVRKLSIVAYSPL 223
Cdd:cd19125 146 KVRAIGVSNFSVKKLEDLLAVAR----------------VPPAV-----NQVECHPgwqqdKLHEFCKSKGIHLSAYSPL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 224 LAGAYTRNDIPLPEqfrgqntghkLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPllAGSTVSQVEENLQSLSVTLSKK 303
Cdd:cd19125 205 GSPGTTWVKKNVLK----------DPIVTKVAEKLGKTPAQVALRWGLQRGTSVLP--KSTNEERIKENIDVFDWSIPEE 272
|
....*..
gi 1082502195 304 QLEQLAS 310
Cdd:cd19125 273 DFAKFSS 279
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
3-310 |
3.32e-12 |
|
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: 65.77 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 3 KVELGNTRErISCMGLGTmyFGTKTDEQTSHAI---LDVYVSHggsfLDTANKYaswipgfkggESEQLIGRWMK---QR 76
Cdd:cd19116 2 TIKLNDGNE-IPAIALGT--WKLKDDEGVRQAVkhaIEAGYRH----IDTAYLY----------GNEAEVGEAIRekiAE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 77 GN--RQTLFVASKVgfpYGNIPRslkKEIILSECEKSLKRLDIETIDLYYVH---AYDAGTPPEE----------FME-- 139
Cdd:cd19116 65 GVvkREDLFITTKL---WNSYHE---REQVEPALRESLKRLGLDYVDLYLIHwpvAFKENNDSESngdgslsdidYLEtw 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 140 -AFYQLKKSGKIRFAGASNFHAWQ----LGEAN-QAAKNQgwegfscIQQFHTYLQPALWAdfgnqqiltpeiqeFCSVR 213
Cdd:cd19116 139 rGMEDLVKLGLTRSIGVSNFNSEQinrlLSNCNiKPAVNQ-------IEVHPTLTQEKLVA--------------YCQSN 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 214 KLSIVAYSPLlagaytrnDIPLPEQFRGQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENL 293
Cdd:cd19116 198 GIVVMAYSPF--------GRLVPRGQTNPPPRLDDPTLVAIAKKYGKTTAQIVLRYLIDR--GVVPIPKSSNKKRIKENI 267
|
330
....*....|....*..
gi 1082502195 294 QSLSVTLSKKQLEQLAS 310
Cdd:cd19116 268 DIFDFQLTPEEVAALNS 284
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
47-279 |
8.34e-12 |
|
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: 64.08 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 47 LDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVASKV-----GFpygniprslkkEIILSECEKSLKRLDIETI 120
Cdd:cd19156 40 IDTAAIY----------KNEEGVGQGIRESGvPREEVFVTTKLwnsdqGY-----------ESTLAAFEESLEKLGLDYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 121 DLYYVHAYDAGTPPEEFmEAFYQLKKSGKIRFAGASNFHAWQLGEANQAAK-----NQgwegfsciqqfhTYLQPALwad 195
Cdd:cd19156 99 DLYLIHWPVKGKFKDTW-KAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKvapmvNQ------------IELHPLL--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 196 fgNQQILtpeiQEFCSVRKLSIVAYSPLlagaytrndiplpeqfrGQntGHKLEK--LKTVAGELGVSANAVVLVWMMQT 273
Cdd:cd19156 163 --TQEPL----RKFCKEKNIAVEAWSPL-----------------GQ--GKLLSNpvLKAIGKKYGKSAAQVIIRWDIQH 217
|
....*.
gi 1082502195 274 PPGIIP 279
Cdd:cd19156 218 GIITIP 223
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-310 |
1.77e-11 |
|
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: 63.58 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTMyfgtKTDEQTSHAILDVYVSHGGSFLDTANKYaswipgfkGGESE--QLIGRWMKQRG-NRQTLFV 84
Cdd:cd19123 7 SNGDLIPALGLGTW----KSKPGEVGQAVKQALEAGYRHIDCAAIY--------GNEAEigAALAEVFKEGKvKREDLWI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 85 ASKVgfpYGNiprSLKKEIILSECEKSLKRLDIETIDLYYVH---AYDAGT---------------PPEEFMEAFYQLKK 146
Cdd:cd19123 75 TSKL---WNN---SHAPEDVLPALEKTLADLQLDYLDLYLMHwpvALKKGVgfpesgedllslspiPLEDTWRAMEELVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 147 SGKIRFAGASNFHAWQL----GEANQA-AKNQgwegfsciQQFHTYLQpalwadfgnqqilTPEIQEFCSVRKLSIVAYS 221
Cdd:cd19123 149 KGLCRHIGVSNFSVKKLedllATARIKpAVNQ--------VELHPYLQ-------------QPELLAFCRDNGIHLTAYS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 222 PLlaGAYTRndiplPEQFRGQNTGHKLEK--LKTVAGELGVSANAVVLVWMMQTPPGIIPllagSTVS--QVEENLQSLS 297
Cdd:cd19123 208 PL--GSGDR-----PAAMKAEGEPVLLEDpvINKIAEKHGASPAQVLIAWAIQRGTVVIP----KSVNpeRIQQNLEAAE 276
|
330
....*....|...
gi 1082502195 298 VTLSKKQLEQLAS 310
Cdd:cd19123 277 VELDASDMATIAA 289
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
47-310 |
2.06e-11 |
|
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: 63.16 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 47 LDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVASKVGFPYGNIPRSLKKeiilseCEKSLKRLDIETIDLYYV 125
Cdd:cd19131 40 IDTAAIY----------GNEEGVGKAIRASGvPREELFITTKLWNSDQGYDSTLRA------FDESLRKLGLDYVDLYLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 126 H----AYDagtppeEFME---AFYQLKKSGKIRFAGASNFHAWQLGEANQAaknqgwegfsciqqfhTYLQPALwadfgN 198
Cdd:cd19131 104 HwpvpAQD------KYVEtwkALIELKKEGRVKSIGVSNFTIEHLQRLIDE----------------TGVVPVV-----N 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 199 QQILTP-----EIQEFCSVRKLSIVAYSPLlagaytrndiplpeqfrGQNTGHKLEKLKTVAGELGVSANAVVLVWMMQT 273
Cdd:cd19131 157 QIELHPrfqqrELRAFHAKHGIQTESWSPL-----------------GQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQN 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 1082502195 274 PPGIIPllAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19131 220 GLVVIP--KSVTPSRIAENFDVFDFELDADDMQAIAG 254
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
66-310 |
4.43e-11 |
|
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: 62.40 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 66 EQLIGRWMKQRG------NRQTLFVASKVGfpygNIPRslKKEIILSECEKSLKRLDIETIDLYYVH---AYDAG----- 131
Cdd:cd19106 46 EQEVGEALKEKVgpgkavPREDLFVTSKLW----NTKH--HPEDVEPALRKTLKDLQLDYLDLYLIHwpyAFERGdnpfp 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 132 -----------TPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQAAKNQGwegfSCIQ-QFHTYLqpalwadfgNQ 199
Cdd:cd19106 120 knpdgtirydsTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVARIKP----AVLQvECHPYL---------AQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 200 QiltpEIQEFCSVRKLSIVAYSPLlaG----AYTRNDIPLPeqfrgqntghkLE--KLKTVAGELGVSANAVVLVWMMQT 273
Cdd:cd19106 187 N----ELIAHCKARGLVVTAYSPL--GspdrPWAKPDEPVL-----------LEepKVKALAKKYNKSPAQILLRWQVQR 249
|
250 260 270
....*....|....*....|....*....|....*..
gi 1082502195 274 ppGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19106 250 --GVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDA 284
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-309 |
7.93e-11 |
|
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: 61.38 E-value: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 15 CMGLGTMYFGTKTDEQTSHAILDVYVSHggsfLDTANKYASwipgfkggesEQLIGRWMKQ-----RGNRQTLFVASKVG 89
Cdd:cd19128 3 RLGFGTYKITESESKEAVKNAIKAGYRH----IDCAYYYGN----------EAFIGIAFSEifkdgGVKREDLFITSKLW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 90 fpygniPRSLKKEIILSECEKSLKRLDIETIDLYYVH-------------------AYDAGTPPEEFMEAFYQLKKSGKI 150
Cdd:cd19128 69 ------PTMHQPENVKEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 151 RFAGASNFHAWQLGEANQAAKnqgwegfscIQQFHTYLQPALWadFGNQQILtpeiqEFCSVRKLSIVAYSPlLAGAYTr 230
Cdd:cd19128 143 KNIGVSNYSTKLLTDLLNYCK---------IKPFMNQIECHPY--FQNDKLI-----KFCIENNIHVTAYRP-LGGSYG- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 231 ndiplpeqfRGQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTPPG---IIPllAGSTVSQVEENLQSLSVTLSKKQLEQ 307
Cdd:cd19128 205 ---------DGNLTFLNDSELKALATKYNTTPPQVIIAWHLQKWPKnysVIP--KSANKSRCQQNFDINDLALTKEDMDA 273
|
..
gi 1082502195 308 LA 309
Cdd:cd19128 274 IN 275
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-300 |
8.55e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 61.46 E-value: 8.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 24 GTKTDEQTSHAILDVYVSHGGSFLDTANKYaswipgfkgGESEQLIGR----WMKQRGNRQTLFVASK-VGFPYgniPRS 98
Cdd:cd19101 17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIY---------GPAEELIGEfrkrLRRERDAADDVQIHTKwVPDPG---ELT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 99 LKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPP-EEFMEAFYQLKKSGKIRFAGASNFHAWQLGEANQA----AKNQ 173
Cdd:cd19101 85 MTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPGyLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAgvpiVSNQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 174 gwEGFSCIQQfhtylQPAlwadfgnqqiltPEIQEFCSVRKLSIVAYSPLLAGAYTRN--DIPLPEQFRGQNTGHK---- 247
Cdd:cd19101 165 --VQYSLLDR-----RPE------------NGMAALCEDHGIKLLAYGTLAGGLLSEKylGVPEPTGPALETRSLQkykl 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 248 --------------LEKLKTVAGELGVSANAVVLVWMMQTP--PGIIpllAGSTVS-QVEENLQSLSVTL 300
Cdd:cd19101 226 midewggwdlfqelLRTLKAIADKHGVSIANVAVRWVLDQPgvAGVI---VGARNSeHIDDNVRAFSFRL 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
79-310 |
1.77e-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: 60.74 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 79 RQTLFVASKVGFPygniprSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPE----------------EFM---E 139
Cdd:cd19110 61 REDLFIVSKLWCT------CHKKSLVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEpdlpldrsgmvipsdtDFLdtwE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 140 AFYQLKKSGKIRFAGASNFHAWQL-------GEANQAAKNQgwegFSCiqqfHTYLqpalwadfgNQQILTpeiqEFCSV 212
Cdd:cd19110 135 AMEDLVIEGLVKNIGVSNFNHEQLerllnkpGLRVKPVTNQ----IEC----HPYL---------TQKKLI----SFCQS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 213 RKLSIVAYSPLLAGAytrNDIPLPEQfrgqntghklEKLKTVAGELGVSANAVVLVWMMQTPPGIIPllAGSTVSQVEEN 292
Cdd:cd19110 194 RNVSVTAYRPLGGSC---EGVDLIDD----------PVIQRIAKKHGKSPAQILIRFQIQRNVIVIP--KSVTPSRIKEN 258
|
250
....*....|....*...
gi 1082502195 293 LQSLSVTLSKKQLEQLAS 310
Cdd:cd19110 259 IQVFDFELTEHDMDNLLS 276
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-310 |
6.48e-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: 59.28 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 29 EQTSHAILDVYVSHGGSFLDTANKYaswipgfkgGESEQLIGRWMKQRG-NRQTLFVASKVGFPYG---NI---PRSLKk 101
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSY---------GRAEEFLGSWLRSRNiAPDAVFVGSKWGYTYTadwQVdaaVHEVK- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 102 eiilsecEKSLKRLD---IET-------IDLYYVHA--YDAGT-PPEEFMEAFYQLKKSG-KIRFAGASNFHAWQLGEAN 167
Cdd:cd19098 104 -------DHSLARLLkqwEETrsllgkhLDLYQIHSatLESGVlEDADVLAALAELKAEGvKIGLSLSGPQQAETLRRAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 168 QAAKNqGWEGFSCIQqfhtylqpALWadfgnqQILTP---EIQEFCSVRKLSIVAYSPLLAGAYT-RNDIPlpeQFRGqn 243
Cdd:cd19098 177 EIEID-GARLFDSVQ--------ATW------NLLEQsagEALEEAHEAGMGVIVKEALANGRLTdRNPSP---ELAP-- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082502195 244 tghKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19098 237 ---LMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAALAD 300
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
47-310 |
1.13e-09 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 58.11 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 47 LDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVASKVGFpygnipRSLKKEIILSECEKSLKRLDIETIDLYYV 125
Cdd:PRK11172 33 IDTAQIY----------DNEAAVGQAIAESGvPRDELFITTKIWI------DNLAKDKLIPSLKESLQKLRTDYVDLTLI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 126 H--AYDAGTPPEEFMEAFYQLKKSGKIRFAGASNFHAWQLGEA------NQAAKNQgwegfsciQQFHTYLQpalwadfg 197
Cdd:PRK11172 97 HwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAiaavgaENIATNQ--------IELSPYLQ-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 198 NQQILtpeiqEFCSVRKLSIVAYSPLlagAYtrndiplpeqfrgqntGHKL--EKLKTVAGELGVSANAVVLVWMMQTPP 275
Cdd:PRK11172 161 NRKVV-----AFAKEHGIHVTSYMTL---AY----------------GKVLkdPVIARIAAKHNATPAQVILAWAMQLGY 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 1082502195 276 GIIPllaGST-VSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:PRK11172 217 SVIP---SSTkRENLASNLLAQDLQLDAEDMAAIAA 249
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-310 |
1.18e-08 |
|
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: 55.20 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTMyfgTKTDEQTSHAILdVYVSHGGSFLDTANKYaswipgfkGGESEqlIGRWMKQRG-NRQTLFVAS 86
Cdd:cd19117 9 NTGAEIPAVGLGTW---QSKPNEVAKAVE-AALKAGYRHIDTAAIY--------GNEEE--VGQGIKDSGvPREEIFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 87 KVGFPYGNIPrslkkeiilSEC-EKSLKRLDIETIDLYYVH---------------------AYDAGTPPEEFMEAFYQL 144
Cdd:cd19117 75 KLWCTWHRRV---------EEAlDQSLKKLGLDYVDLYLMHwpvpldpdgndflfkkddgtkDHEPDWDFIKTWELMQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 145 KKSGKIRFAGASNFHAWQLGE--ANQAAK-----NQgwegfsciQQFHTYLQpalwadfgnqqilTPEIQEFCSVRKLSI 217
Cdd:cd19117 146 PATGKVKAIGVSNFSIKNLEKllASPSAKivpavNQ--------IELHPLLP-------------QPKLVDFCKSKGIHA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 218 VAYSPLlaGAytrNDIPLpeqfrgqntgHKLEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLs 297
Cdd:cd19117 205 TAYSPL--GS---TNAPL----------LKEPVIIKIAKKHGKTPAQVIISWGLQR--GYSVLPKSVTPSRIESNFKLF- 266
|
330
....*....|...
gi 1082502195 298 vTLSKKQLEQLAS 310
Cdd:cd19117 267 -TLSDEEFKEIDE 278
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
12-308 |
1.43e-08 |
|
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: 54.72 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 12 RISCMGLGTmyFGTKTDEqTSHAILDVyVSHGGSFLDTANKYaswipgfkGGESEqlIGRWMKQRG-NRQTLFVASKV-- 88
Cdd:cd19127 8 EMPALGLGV--FQTPPEE-TADAVATA-LADGYRLIDTAAAY--------GNERE--VGEGIRRSGvDRSDIFVTTKLwi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 89 -GFPYGNIPRSLkkeiilsecEKSLKRLDIETIDLYYVHaYDAGTPPEEFMEAFYQLKK---SGKIRFAGASNFHAWQLG 164
Cdd:cd19127 74 sDYGYDKALRGF---------DASLRRLGLDYVDLYLLH-WPVPNDFDRTIQAYKALEKllaEGRVRAIGVSNFTPEHLE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 165 EANQA-----AKNQgwegfsciQQFHTYL-QPALwadfgnqqiltpeiQEFCsvRKLSIV--AYSPLlaGAYTRNDIPLP 236
Cdd:cd19127 144 RLIDAttvvpAVNQ--------VELHPYFsQKDL--------------RAFH--RRLGIVtqAWSPI--GGVMRYGASGP 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082502195 237 EQfrgqnTGHKLEK--LKTVAGELGVSANAVVLVWMMQTPPGIIPllagSTVS--QVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19127 198 TG-----PGDVLQDptITGLAEKYGKTPAQIVLRWHLQNGVSAIP----KSVHpeRIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
18-301 |
1.67e-08 |
|
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: 54.92 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 18 LGTMYfgTKTDEQTSHAILDVYVSHGGSFLDTANKYaswipGFkgGESEQLIGRWMKqRGNRQTLFVASKVG-------- 89
Cdd:cd19152 10 LGNLY--EAVSDEEAKATLVAAWDLGIRYFDTAPWY-----GA--GLSEERLGAALR-ELGREDYVISTKVGrllvplqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 90 -------FPYGNIPRSLKKEI----ILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFMEAFYQ-----------LKKS 147
Cdd:cd19152 80 veptfepGFWNPLPFDAVFDYsydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQaikgafraleeLREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 148 GKIRFAGA-SNFhaWQLgeANQAAKNQGWEGFSCIQQFHTYLQPALwadfgnqQILTPEIQEfcsvRKLSIVAYSPLLAG 226
Cdd:cd19152 160 GVIKAIGLgVND--WEV--ILRILEEADLDWVMLAGRYTLLDHSAA-------RELLPECEK----RGVKVVNAGPFNSG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 227 --------AYTRNDIPLPEQFRgqntghKLEKLKTVAGELGVSANAVVLVWMMQtPPGIIPLLAG-STVSQVEENLQSLS 297
Cdd:cd19152 225 flaggdnfDYYEYGPAPPELIA------RRDRIEALCEQHGVSLAAAALQFALA-PPAVASVAPGaSSPERVEENVALLA 297
|
....
gi 1082502195 298 VTLS 301
Cdd:cd19152 298 TEIP 301
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
15-306 |
3.31e-08 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 53.82 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 15 CMGLGTMYFGTKTDEQTSH--AILDVYVSHGGSFLDTANKYaswipgfkgGESEQLIGRWMKQRGN---RQTLFVASKVG 89
Cdd:cd19164 17 IFGAATFSYQYTTDPESIPpvDIVRRALELGIRAFDTSPYY---------GPSEIILGRALKALRDefpRDTYFIITKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 90 ------FPYG--NIPRSLkkeiilsecEKSLKRLDIETIDLYYVHayDAG-TPPEEFMEA---FYQLKKSGKIRFAGASN 157
Cdd:cd19164 88 rygpddFDYSpeWIRASV---------ERSLRRLHTDYLDLVYLH--DVEfVADEEVLEAlkeLFKLKDEGKIRNVGISG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 158 FHAWQLGEANQAAKNQGWEGFSCIQQF-HTYLQPALWADFgnqqilTPEIQEFCSVRklSIVAYSPLLAGAYTRNDIPL- 235
Cdd:cd19164 157 YPLPVLLRLAELARTTAGRPLDAVLSYcHYTLQNTTLLAY------IPKFLAAAGVK--VVLNASPLSMGLLRSQGPPEw 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082502195 236 ---PEQFRgqNTGHKLEKLktvAGELGVSANAVVLVWMMQTPPGIIPLLAG-STVSQVEENLQSLSVTLSKKQLE 306
Cdd:cd19164 229 hpaSPELR--AAAAKAAEY---CQAKGTDLADVALRYALREWGGEGPTVVGcSNVDELEEAVEAYWSVLAGASEE 298
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
79-309 |
4.45e-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: 53.60 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 79 RQTLFVASKVGFPYGNiPRSLKKEIilsecEKSLKRLDIETIDLYYVH--------AYDAGTPP-------EEFME---- 139
Cdd:cd19113 68 REELFLTSKLWNNFHD-PKNVETAL-----NKTLSDLKLDYVDLFLIHfpiafkfvPIEEKYPPgfycgdgDNFVYedvp 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 140 ------AFYQLKKSGKIRFAGASNFHAWQLGEANQAAKNQGwegfSCIQ-QFHTYLQpalwadfgnqqilTPEIQEFCSV 212
Cdd:cd19113 142 ildtwkALEKLVDAGKIKSIGVSNFPGALILDLLRGATIKP----AVLQiEHHPYLQ-------------QPKLIEYAQK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 213 RKLSIVAYSPLLAGAYTRNDIPlpeqfRGQNTGHKLEK--LKTVAGELGVSANAVVLVWMMQTPPGIIPllAGSTVSQVE 290
Cdd:cd19113 205 AGITITAYSSFGPQSFVELNQG-----RALNTPTLFEHdtIKSIAAKHNKTPAQVLLRWATQRGIAVIP--KSNLPERLL 277
|
250
....*....|....*....
gi 1082502195 291 ENLQSLSVTLSKKQLEQLA 309
Cdd:cd19113 278 QNLSVNDFDLTKEDFEEIA 296
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
28-310 |
5.45e-08 |
|
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: 52.99 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 28 DEQTSHAI---LDVYVSHggsfLDTANKYASwipgfkggesEQLIGRWMKQRG-NRQTLFVASKVGfpygniPRSLKKEI 103
Cdd:cd19130 22 PADTQRAVataLEVGYRH----IDTAAIYGN----------EEGVGAAIAASGiPRDELFVTTKLW------NDRHDGDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 104 ILSECEKSLKRLDIETIDLYYVH--AYDAGTPPEEFmEAFYQLKKSGKIRFAGASNFHAWQLGEANQaaknqgwegfsci 181
Cdd:cd19130 82 PAAAFAESLAKLGLDQVDLYLVHwpTPAAGNYVHTW-EAMIELRAAGRTRSIGVSNFLPPHLERIVA------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 182 qqfHTYLQPALwadfgNQQILTP-----EIQEFCSVRKLSIVAYSPLlagaytrndiplpeqfrGQNTGHKLEKLKTVAG 256
Cdd:cd19130 148 ---ATGVVPAV-----NQIELHPayqqrTIRDWAQAHDVKIEAWSPL-----------------GQGKLLGDPPVGAIAA 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1082502195 257 ELGVSANAVVLVWMMQTPPGIIPllAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19130 203 AHGKTPAQIVLRWHLQKGHVVFP--KSVRRERMEDNLDVFDFDLTDTEIAAIDA 254
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
16-308 |
9.14e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 52.28 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 16 MGLGTM------YFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASWIpgfkggeSEQLIgrwmkqrgnRQTLF------ 83
Cdd:PRK10376 20 LGYGAMqlagpgVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHV-------TNQLI---------REALHpypddl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 84 -VASKVGF---PYGNIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPP-----EEFMEAFYQLKKSGKIRFAG 154
Cdd:PRK10376 84 tIVTKVGArrgEDGSWLPAFSPAELRRAVHDNLRNLGLDVLDVVNLRLMGDGHGPaegsiEEPLTVLAELQRQGLVRHIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 155 ASNFHAWQLGEANQAAKnqgwegFSCIQQFHTYLQ---PALWADFGNQQIltpeiqefcsvrklSIVAYSPLlaGAYTrn 231
Cdd:PRK10376 164 LSNVTPTQVAEARKIAE------IVCVQNHYNLAHradDALIDALARDGI--------------AYVPFFPL--GGFT-- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082502195 232 diPLpeqfrgQNTGhklekLKTVAGELGVSANAVVLVWMMQTPPGIIpLLAG-STVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:PRK10376 220 --PL------QSST-----LSDVAASLGATPMQVALAWLLQRSPNIL-LIPGtSSVAHLRENLAAAELVLSEEVLAEL 283
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
17-309 |
1.18e-07 |
|
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: 51.89 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 17 GLGTMYFGTkTDEQTSHAILDVyVSHGGSFLDTANKYaswipgfkggESEQLIGRWMKQ---RG---NRQTLFVASKVgf 90
Cdd:cd19124 9 GMGTASDPP-SPEDIKAAVLEA-IEVGYRHFDTAAAY----------GTEEALGEALAEalrLGlvkSRDELFVTSKL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 91 pygnIPRSLKKEIILSECEKSLKRLDIETIDLYYVH--------AYDAGTPPEEFM--------EAFYQLKKSGKIRFAG 154
Cdd:cd19124 75 ----WCSDAHPDLVLPALKKSLRNLQLEYVDLYLIHwpvslkpgKFSFPIEEEDFLpfdikgvwEAMEECQRLGLTKAIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 155 ASNFHAWQLGE----------ANQAAKNQGWegfsciQQfhtylqpalwadfgnqqiltPEIQEFCSVRKLSIVAYSPLL 224
Cdd:cd19124 151 VSNFSCKKLQEllsfatippaVNQVEMNPAW------QQ--------------------KKLREFCKANGIHVTAYSPLG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 225 AGAYtrndiplpeqFRGQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQSLSVTLSKKQ 304
Cdd:cd19124 205 APGT----------KWGSNAVMESDVLKEIAAAKGKTVAQVSLRWVYEQ--GVSLVVKSFNKERMKQNLDIFDWELTEED 272
|
....*
gi 1082502195 305 LEQLA 309
Cdd:cd19124 273 LEKIS 277
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
102-310 |
1.53e-07 |
|
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: 52.10 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 102 EIILSECEKSLKRLDIETIDLYYVH-----------------------AYDAGTPPEEFMEAFYQLKKSGKIRFAGASNF 158
Cdd:cd19112 83 GHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWHAMEKLVSAGLVRSIGISNY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 159 HAWQLGEANQAAKnqgwegfsciqqfhtyLQPALwadfgNQQILTPEIQ-----EFCSVRKLSIVAYSPLLAGAYTRndi 233
Cdd:cd19112 163 DIFLTRDCLAYSK----------------IKPAV-----NQIETHPYFQrdslvKFCQKHGISVTAHTPLGGAAANA--- 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082502195 234 plpEQFrgqNTGHKLEK--LKTVAGELGVSANAVVLVWMMQTPPGIIPllAGSTVSQVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19112 219 ---EWF---GSVSPLDDpvLKDLAKKYGKSAAQIVLRWGIQRNTAVIP--KSSKPERLKENIDVFDFQLSKEDMKLIKS 289
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-299 |
2.66e-07 |
|
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: 50.99 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTMYFGT-KTDEQTSHAIldvyvSHGGSFLDTANKYaswipgfkGGESEqlIGRWMKQRGN----RQTL 82
Cdd:cd19121 7 NTGASIPAVGLGTWQAKAgEVKAAVAHAL-----KIGYRHIDGALCY--------QNEDE--VGEGIKEAIAggvkREDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 83 FVASKVGFPYGNIPRslkkeiilsEC-EKSLKRLDIETIDLYYVH----AYDAGTPPE---------------------E 136
Cdd:cd19121 72 FVTTKLWSTYHRRVE---------LClDRSLKSLGLDYVDLYLVHwpvlLNPNGNHDLfptlpdgsrdldwdwnhvdtwK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 137 FMEAFYqlkKSGKIRFAGASNF----------HAWQLGEANQAaknqgwegfsciqQFHTYLQpalwadfgnQQiltpEI 206
Cdd:cd19121 143 QMEKVL---KTGKTKAIGVSNYsipyleellkHATVVPAVNQV-------------ENHPYLP---------QQ----EL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 207 QEFCSVRKLSIVAYSPL-LAGAytrndiPLpeqfrgqntgHKLEKLKTVAGELGVSANAVVLVWmmQTPPGIIPLLAGST 285
Cdd:cd19121 194 VDFCKEKGILIEAYSPLgSTGS------PL----------ISDEPVVEIAKKHNVGPGTVLISY--QVARGAVVLPKSVT 255
|
330
....*....|....
gi 1082502195 286 VSQVEENLQSLSVT 299
Cdd:cd19121 256 PDRIKSNLEIIDLD 269
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
16-297 |
4.41e-07 |
|
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: 50.44 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 16 MGLGTMYFG--TKTDEQTSHAILDVYVSHGGSFLDTANKYAswipgfkGGESEQLIGRWMkQRGNRQTLFVASKVG---- 89
Cdd:cd19162 3 LGLGAASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYG-------LGLSERRLGAAL-ARHPRAEYVVSTKVGrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 90 ---------------FPYGNIPRSLkkeiilsecEKSLKRLDIETIDLYYVHayDAGTPPEEFM----EAFYQLKKSGKI 150
Cdd:cd19162 75 pgaagrpagadrrfdFSADGIRRSI---------EASLERLGLDRLDLVFLH--DPDRHLLQALtdafPALEELRAEGVV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 151 RFAGASnfhAWQLGEANQAAKNQGWEGFsCIQQFHTYLQPAlwadfgnqqiLTPEIQEFCSVRKLSIVAYSPL----LAG 226
Cdd:cd19162 144 GAIGVG---VTDWAALLRAARRADVDVV-MVAGRYTLLDRR----------AATELLPLCAAKGVAVVAAGVFnsgiLAT 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082502195 227 AYTRNDI----PLPEQFRGQntghkLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPLLAGSTVSQVEENLQSLS 297
Cdd:cd19162 210 DDPAGDRydyrPATPEVLAR-----ARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLR 279
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
79-310 |
6.54e-07 |
|
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: 50.11 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 79 RQTLFVASKVgfpygnIPRSLKKEIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFM-------------------E 139
Cdd:cd19107 61 REDLFIVSKL------WCTFHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFpldesgnvipsdttfldtwE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 140 AFYQLKKSGKIRFAGASNFHAWQL-------GEANQAAKNQgwegFSCiqqfHTYLqpalwadfgNQQILTpeiqEFCSV 212
Cdd:cd19107 135 AMEELVDEGLVKAIGVSNFNHLQIerilnkpGLKYKPAVNQ----IEC----HPYL---------TQEKLI----QYCQS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 213 RKLSIVAYSPLlaGAYTR-----NDIPLPEQfrgqntghklEKLKTVAGELGVSANAVVLVWMMQTPPGIIPllAGSTVS 287
Cdd:cd19107 194 KGIVVTAYSPL--GSPDRpwakpEDPSLLED----------PKIKEIAAKHNKTTAQVLIRFPIQRNLVVIP--KSVTPE 259
|
250 260
....*....|....*....|...
gi 1082502195 288 QVEENLQSLSVTLSKKQLEQLAS 310
Cdd:cd19107 260 RIAENFKVFDFELSSEDMATILS 282
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-310 |
7.11e-07 |
|
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: 49.86 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 11 ERISCMGLGTMYFGTKTDEQTSHAILDVyvshGGSFLDTANKYASwipgfkggesEQLIGRWMKQRGN-----RQTLFVA 85
Cdd:cd19114 2 DKMPLVGFGTAKIKANETEEVIYNAIKV----GYRLIDGALLYGN----------EAEVGRGIRKAIQeglvkREDLFIV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 86 SKVgfpYGNIPRslkKEIILSECEKSLKRLDIETIDLYYVH-----------------AYDAGTPPEEF-----MEAFYQ 143
Cdd:cd19114 68 TKL---WNNFHG---KDHVREAFDRQLKDYGLDYIDLYLIHfpipaayvdpaenypflWKDKELKKFPLeqspmQECWRE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 144 LKK---SGKIRFAGASNFHAWQLGEANQAAKNQGwegfSCIQ-QFHTYLQPALWADFGNQQiltpeiqefcsvrKLSIVA 219
Cdd:cd19114 142 MEKlvdAGLVRNIGIANFNVQLILDLLTYAKIKP----AVLQiEHHPYLQQKRLIDWAKKQ-------------GIQITA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 220 YSPLLAGAYTRndipLPEQFRGQNTGHKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPllAGSTVSQVEENLQSLSVT 299
Cdd:cd19114 205 YSSFGNAVYTK----VTKHLKHFTNLLEHPVVKKLADKHKRDTGQVLLRWAVQRNITVIP--KSVNVERMKTNLDITSYK 278
|
330
....*....|.
gi 1082502195 300 LSKKQLEQLAS 310
Cdd:cd19114 279 LDEEDMEALYE 289
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
5-156 |
8.81e-07 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 49.78 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 5 ELGNTRERISCMGLGTMYFGT---KTDEQTSHAILDVYVSHGGSFLDTAnkyaswiPGFKGGESEQLIGRWMKQRG-NRQ 80
Cdd:PLN02587 3 ELGSTGLKVSSVGFGASPLGSvfgPVSEEDAIASVREAFRLGINFFDTS-------PYYGGTLSEKVLGKALKALGiPRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 81 TLFVASKVG-------FPYGNIPRSLkkeiilsecEKSLKRLDIETIDLYYVHAYDAGTPPE---EFMEAFYQLKKSGKI 150
Cdd:PLN02587 76 KYVVSTKCGrygegfdFSAERVTKSV---------DESLARLQLDYVDILHCHDIEFGSLDQivnETIPALQKLKESGKV 146
|
....*.
gi 1082502195 151 RFAGAS 156
Cdd:PLN02587 147 RFIGIT 152
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-299 |
1.97e-06 |
|
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: 48.39 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTmyFGTKTDEQTSHAILDVYVSHGGSFLDTANKYASwipgfkGGESEQLIGRWMKQRGN--RQTLFVA 85
Cdd:cd19122 4 NNGVKIPAVGFGT--FANEGAKGETYAAVTKALDVGYRHLDCAWFYLN------EDEVGDAVRDFLKENPSvkREDLFIC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 86 SKVgfpYGNIPRSlkkEIILSECEKSLKRLDIETIDLYYVH------AYDAGTP-----------------PEEFMEAFY 142
Cdd:cd19122 76 TKV---WNHLHEP---EDVKWSIDNSLKNLKLDYIDLFLVHwpiaaeKNDQRSPklgpdgkyvilkdltenPEPTWRAME 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 143 QLKKSGKIRFAGASNFHAWQLGEANQAAKnqgwegfsciqqfhtyLQPALwadfgNQQILTP-----EIQEFCSVRKLSI 217
Cdd:cd19122 150 EIYESGKAKAIGVSNWTIPGLKKLLSFAK----------------VKPHV-----NQIEIHPflpneELVDYCFSNDILP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 218 VAYSPLlagaYTRNDIPlpeqfrgqNTGHKLEK---LKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEENLQ 294
Cdd:cd19122 209 EAYSPL----GSQNQVP--------STGERVSEnptLNEVAEKGGYSLAQVLIAWGLRR--GYVVLPKSSTPSRIESNFK 274
|
....*
gi 1082502195 295 SLSVT 299
Cdd:cd19122 275 SIELS 279
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
102-308 |
5.03e-06 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 47.10 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 102 EIILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEFM-------------------EAFYQLKKSGKIRFAGASNFHAWQ 162
Cdd:cd19109 82 ELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYprdengkwlyhktnlcatwEALEACKDAGLVKSIGVSNFNRRQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 163 L-------GEANQAAKNQgwegFSCiqqfHTYLqpalwadfgNQqiltPEIQEFCSVRKLSIVAYSPL-LAGAYTRNDIP 234
Cdd:cd19109 162 LelilnkpGLKHKPVSNQ----VEC----HPYF---------TQ----PKLLEFCQQHDIVIVAYSPLgTCRDPIWVNVS 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082502195 235 LPEQFrgqntghKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPllAGSTVSQVEENLQSLSVTLSKKQLEQL 308
Cdd:cd19109 221 SPPLL-------EDPLLNSIGKKYNKTAAQVVLRFNIQRGVVVIP--KSFNPERIKENFQIFDFSLTEEEMKDI 285
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-308 |
7.70e-06 |
|
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: 46.72 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTMYFGTK---TDEQTSHAILDVYvSHggsfLDTANKYaswipgfkggESEQLIGRWMKQ-----RGNR 79
Cdd:cd19119 7 NTGASIPALGLGTASPHEDraeVKEAVEAAIKEGY-RH----IDTAYAY----------ETEDFVGEAIKRaiddgSIKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 80 QTLFVASKVgFP--YGNIPRSLkkeiilsecEKSLKRLDIETIDLYYVH--------AYDAGTPpeefmeaFYQLKKSGK 149
Cdd:cd19119 72 EELFITTKV-WPtfYDEVERSL---------DESLKALGLDYVDLLLVHwpvcfekdSDDSGKP-------FTPVNDDGK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 150 IRFAGASNF-HAWQLGEA---NQAAKNQGWEGFS------CIQQFHTylQPALwadfgNQQILTP-----EIQEFCSVRK 214
Cdd:cd19119 135 TRYAASGDHiTTYKQLEKiylDGRAKAIGVSNYSivylerLIKECKV--VPAV-----NQVELHPhlpqmDLRDFCFKHG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 215 LSIVAYSPLlagaytrndiplpeqfrGQNTG--HKLEKLKTVAGELGVSANAVVLVWMMQTPPGIIPllagSTVSQVEEN 292
Cdd:cd19119 208 ILVTAYSPL-----------------GSHGApnLKNPLVKKIAEKYNVSTGDILISYHVRQGVIVLP----KSLKPVRIV 266
|
330
....*....|....*.
gi 1082502195 293 LQSLSVTLSKKQLEQL 308
Cdd:cd19119 267 SNGKIVSLTKEDLQKL 282
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-292 |
1.12e-05 |
|
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: 46.30 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 8 NTRERISCMGLGTMYFGTKTDEQTSHAILDVYVSHggsfLDTANKYaswipgfkggESEQLIGRWMKQ---RGN--RQTL 82
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRH----FDCAERY----------RNEAEVGEAMQEvfkAGKirREDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 83 FVASKVgfpYGNIPRSlkkEIILSECEKSLKRLDIETIDLYYVHA--------------------YDAGTPPEEFMEAFY 142
Cdd:cd19129 67 FVTTKL---WNTNHRP---ERVKPAFEASLKRLQLDYLDLYLIHTpfafqpgdeqdprdangnviYDDGVTLLDTWRAME 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 143 QLKKSGKIRFAGASNFHAWQLGEANQAAKNQGwegfSCIQ-QFHTYLQPalWadfgnqqiltpEIQEFCSVRKLSIVAYS 221
Cdd:cd19129 141 RLVDEGRCKAIGLSDVSLEKLREIFEAARIKP----AVVQvESHPYLPE--W-----------ELLDFCKNHGIVLQAFA 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082502195 222 PLlagaytrndiplpeqfrgqntGHKLEK-------LKTVAGELGVSANAVVLVWMMQTppGIIPLLAGSTVSQVEEN 292
Cdd:cd19129 204 PL---------------------GHGMEPklledpvITAIARRVNKTPAQVLLAWAIQR--GTALLTTSKTPSRIREN 258
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
15-148 |
1.86e-04 |
|
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: 42.31 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 15 CMGLGTMYfgTKTDEQTSHAILDVYVSHGGSFLDTANKYaswipGFkgGESEQLIGRWMKQRGnRQTLFVASKVG----- 89
Cdd:cd19161 7 TAGLGNLY--TAVSNADADATLDAAWDSGIRYFDTAPMY-----GH--GLAEHRLGDFLREKP-RDEFVLSTKVGrllkp 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082502195 90 ------FPYGNIPRSLKKEI--------ILSECEKSLKRLDIETIDLYYVHAYDAGTPPEEF-MEAFYQLKKSG 148
Cdd:cd19161 77 aregsvPDPNGFVDPLPFEIvydysydgIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKeRHHFAQLMSGG 150
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
27-159 |
8.24e-04 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 40.44 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 27 TDEQTSHAI---LDVyvshGGSFLDTANKYaswipgfkggESEQLIGRWMKQRG-NRQTLFVASKVGFPYGNIPRSlkke 102
Cdd:PRK11565 26 SNEEVITAIhkaLEV----GYRSIDTAAIY----------KNEEGVGKALKEASvAREELFITTKLWNDDHKRPRE---- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082502195 103 iilsECEKSLKRLDIETIDLYYVHAYDAgtPPEEFMEAFYQ---LKKSGKIRFAGASNFH 159
Cdd:PRK11565 88 ----ALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGmieLQKEGLIKSIGVCNFQ 141
|
|
| |
