|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-304 |
0e+00 |
|
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: 519.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAFWNEGCSGGESELLLGQWLKDRGNREHIVLATKVGAQPT 93
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTEGGVGGESERLIGRWLKDRGNRDDVVIATKVGAGPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 94 IPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHTWRVEKAR 173
Cdd:cd19752 81 DPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 174 NISKSHHWASYSCIQQRYTYLRPKPGADFGVQISANDELLNYCQTHDDFSLLAYSPLLNGSYTRSDAPLQKQYESEDAQA 253
Cdd:cd19752 161 QIARQQGWAEFSAIQQRHSYLRPRPGADFGVQRIVTDELLDYASSRPDLTLLAYSPLLSGAYTRPDRPLPEQYDGPDSDA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1133861166 254 RLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLN 304
Cdd:cd19752 241 RLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-315 |
2.36e-111 |
|
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: 325.32 E-value: 2.36e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGCLNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAFWNEGCSGGESELLLGQWLKDRGNREHIVLA 85
Cdd:cd19081 2 LGRTGLSVSPLCLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAWVPGNAGGESETIIGRWLKSRGKRDRVVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 86 TKVGAQPTIPGggfesmEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHH 165
Cdd:cd19081 82 TKVGFPMGPNG------PGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 166 TWRVEKARNISKSHHWASYSCIQQRYTYLRPKPgadfgvqisANDELLNYCQTHdDFSLLAYSPL----LNGSYtRSDAP 241
Cdd:cd19081 156 AWRLQEALELSRQHGLPRYVSLQPEYNLVDRES---------FEGELLPLCREE-GIGVIPYSPLaggfLTGKY-RSEAD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 242 LQK---------QYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19081 225 LPGstrrgeaakRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEV 304
|
...
gi 1133861166 313 HRL 315
Cdd:cd19081 305 ARL 307
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-315 |
7.86e-101 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 298.63 E-value: 7.86e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCLNFG---SRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcSGGESELLLGQWLKDRg 77
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGgpwGGVDEAEAIAILDAALDAGINFFDTADVY-------GPGRSEELLGEALKGR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 78 NREHIVLATKVGaqptIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVR 157
Cdd:COG0667 73 PRDDVVIATKVG----RRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 158 ALGCSNHHTWRVEKARNISKshHWASYSCIQQRYTYLRPKPGadfgvqisanDELLNYCQTHdDFSLLAYSPL----LNG 233
Cdd:COG0667 149 YIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRSAE----------EELLPAAREL-GVGVLAYSPLagglLTG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 234 SYT---------RSDAPLQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLN 304
Cdd:COG0667 216 KYRrgatfpegdRAATNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAAD 295
|
330
....*....|.
gi 1133861166 305 IRLTQDQLHRL 315
Cdd:COG0667 296 LELSAEDLAAL 306
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-301 |
6.36e-97 |
|
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: 285.95 E-value: 6.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAFWnegcsggESELLLGQWLKDRGNREHIVLATKVGAqpt 93
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDG-------RSERLLGRWLKGRGNRDDVVIATKGGH--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 94 iPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHTWRVEKAR 173
Cdd:cd06660 71 -PPGGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 174 NISKSHHWASYSCIQQRYTYLRPKPgadfgvqisANDELLNYCQTHdDFSLLAYSPLLNGsytrsdaplqkqyesedaqa 253
Cdd:cd06660 150 AYAKAHGLPGFAAVQPQYSLLDRSP---------MEEELLDWAEEN-GLPLLAYSPLARG-------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1133861166 254 rlrvlsevaqetggtLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLD 301
Cdd:cd06660 200 ---------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
6-315 |
9.55e-91 |
|
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: 272.92 E-value: 9.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGCLNFGSRT------DKETSYRLLDQYVDAGGSFLDTSNNYafwnegcSGGESELLLGQWLKDRGNR 79
Cdd:cd19079 5 LGNSGLKVSRLCLGCMSFGDPKwrpwvlDEEESRPIIKRALDLGINFFDTANVY-------SGGASEEILGRALKEFAPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 80 EHIVLATKVGAqptiPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRAL 159
Cdd:cd19079 78 DEVVIATKVYF----PMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 160 GCSNHHTWRVEKARNISKSHHWASYSCIQQRYTYL-----RpkpgadfgvqisandELLNYCQTHdDFSLLAYSPL---- 230
Cdd:cd19079 154 GASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLyreeeR---------------EMIPLCEEE-GIGVIPWSPLargr 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 231 LNGSY---------TRSDAPLQKQYESE-DAQARLRVLsEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENL 300
Cdd:cd19079 218 LARPWgdtterrrsTTDTAKLKYDYFTEaDKEIVDRVE-EVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAV 296
|
330
....*....|....*
gi 1133861166 301 DSLNIRLTQDQLHRL 315
Cdd:cd19079 297 AALDIKLSEEEIKYL 311
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-315 |
1.88e-89 |
|
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: 269.44 E-value: 1.88e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCLNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRgnRE 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYG-------GGRSEEIIGRWIAGR--RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATKVGaQPTIPGggfESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALG 160
Cdd:cd19087 72 DIVLATKVF-GPMGDD---PNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 161 CSNHHTWRVEKARNISKSHHWASYSCIQQRYTYlrpkpgadfgVQISANDELLNYCQTHdDFSLLAYSPL----LNGSYT 236
Cdd:cd19087 148 VSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNL----------LKRQAELEILPAARAY-GLGVIPYSPLagglLTGKYG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 237 RSDAPLQ-KQYESEDAQAR---------LRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIR 306
Cdd:cd19087 217 KGKRPESgRLVERARYQARygleeyrdiAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEIT 296
|
....*....
gi 1133861166 307 LTQDQLHRL 315
Cdd:cd19087 297 LTPELLAEI 305
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
5-315 |
2.17e-88 |
|
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: 266.78 E-value: 2.17e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 5 LLGNTGIQVSALGLGCLNFGSR----TDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKdrGNRE 80
Cdd:cd19080 2 LLGRSGLRVSPLALGTMTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYT-------NGTSERLLGEFIA--GNRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATK--VGAQPTIPGGGfesmeGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRA 158
Cdd:cd19080 73 RIVLATKytMNRRPGDPNAG-----GNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 159 LGCSNHHTWRVEKARNISKSHHWASYSCIQQRYTYlrpkpgadfgVQISANDELLNYCQTHdDFSLLAYSPL----LNGS 234
Cdd:cd19080 148 VGISDTPAWVVARANTLAELRGWSPFVALQIEYSL----------LERTPERELLPMARAL-GLGVTPWSPLggglLTGK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 235 YTRS---------DAPLQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNI 305
Cdd:cd19080 217 YQRGeegrageakGVTVGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL 296
|
330
....*....|
gi 1133861166 306 RLTQDQLHRL 315
Cdd:cd19080 297 TLSPEQLARL 306
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-304 |
4.19e-85 |
|
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: 257.87 E-value: 4.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAFWNEGcsgGESELLLGQWLKDRGNREHIVLATKvGAQPt 93
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVER---GASERVIGEWLKSRGNRDKVVIATK-GGHP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 94 ipggGFESMEG--LSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHTWRVEK 171
Cdd:cd19082 76 ----DLEDMSRsrLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 172 ARNISKSHHWASYSCIQQRYTYLRPKPGADFGVQ-ISANDELLNYCQTHdDFSLLAYSPLLNGSYTR-------SDAPLQ 243
Cdd:cd19082 152 ANAYAKAHGLPGFAASSPQWSLARPNEPPWPGPTlVAMDEEMRAWHEEN-QLPVFAYSSQARGFFSKraaggaeDDSELR 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133861166 244 KQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLN 304
Cdd:cd19082 231 RVYYSEENFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-315 |
2.47e-83 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 254.46 E-value: 2.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCLNFGSR---------TDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcSGGESELLLGQ 71
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGggffgawggVDQEEADRLVDIALDAGINFFDTADVY-------SEGESEEILGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 72 WLKDRgnREHIVLATKVGAQPtipGGGFESMeGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLV 151
Cdd:cd19091 74 ALKGR--RDDVLIATKVRGRM---GEGPNDV-GLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 152 RAGKVRALGCSNHHTWRVEKARNISKSHHWASYSCIQQRYTYLrpkpGADFgvqisaNDELLNYCQtHDDFSLLAYSPL- 230
Cdd:cd19091 148 RQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLL----GRDL------EHELMPLAL-DQGVGLLVWSPLa 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 231 ---LNGSYTRsDAPLQK------------QYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQ 295
Cdd:cd19091 217 gglLSGKYRR-GQPAPEgsrlrrtgfdfpPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQ 295
|
330 340
....*....|....*....|
gi 1133861166 296 LQENLDSLNIRLTQDQLHRL 315
Cdd:cd19091 296 LEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-315 |
5.98e-70 |
|
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: 219.32 E-value: 5.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNFGS----RTDKETSYRLLDQYVDAGGSFLDTSNNYAFwnegcsgGESELLLGQWLKDRgnREHIVLA 85
Cdd:cd19084 1 DLKVSRIGLGTWAIGGtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGF-------GHSEEILGKALKGR--RDDVVIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 86 TKVGAQPTIPGGGFESmegLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHH 165
Cdd:cd19084 72 TKCGLRWDGGKGVTKD---LSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 166 TWRVEKARNISKshhwasYSCIQQRYTYLRPKpgadfgvqisANDELLNYCQTHdDFSLLAYSPL----LNGSYT----- 236
Cdd:cd19084 149 VEQLEEARKYGP------IVSLQPPYSMLERE----------IEEELLPYCREN-GIGVLPYGPLaqglLTGKYKkeptf 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 237 -----RSDAPLQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLTQDQ 311
Cdd:cd19084 212 ppddrRSRFPFFRGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEE 291
|
....
gi 1133861166 312 LHRL 315
Cdd:cd19084 292 LKEI 295
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-315 |
2.04e-69 |
|
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: 217.95 E-value: 2.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 16 LGLGCLNFGS---RTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDR-GNREHIVLATKVgaq 91
Cdd:pfam00248 1 IGLGTWQLGGgwgPISKEEALEALRAALEAGINFIDTAEVYG-------DGKSEELLGEALKDYpVKRDKVVIATKV--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 92 ptiPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHTWRVEK 171
Cdd:pfam00248 71 ---PDGDGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 172 ArnisKSHHWASYSCIQQRYTYLRPKPgadfgvqisaNDELLNYCQtHDDFSLLAYSPLLNGSYT-RSDAPLQKQYESED 250
Cdd:pfam00248 148 A----LTKGKIPIVAVQVEYNLLRRRQ----------EEELLEYCK-KNGIPLIAYSPLGGGLLTgKYTRDPDKGPGERR 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133861166 251 ---------AQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:pfam00248 213 rllkkgtplNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-310 |
1.16e-67 |
|
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: 213.61 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGC-LNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRgNREHIVLATKV 88
Cdd:cd19074 1 GLKVSELSLGTwLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYA-------AGQAEEVLGKALKGW-PRESYVISTKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 89 GAqptiPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNhhtW- 167
Cdd:cd19074 73 FW----PTGPGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSE---Ws 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 168 --RVEKARNISKSHHWASYSCIQQRYTYLRPKPgadfgvqisaNDELLNYCQTHdDFSLLAYSPL----LNGSY------ 235
Cdd:cd19074 146 aeQIAEAHDLARQFGLIPPVVEQPQYNMLWREI----------EEEVIPLCEKN-GIGLVVWSPLaqglLTGKYrdgipp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 236 -TRSDAPLQK------QYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLT 308
Cdd:cd19074 215 pSRSRATDEDnrdkkrRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLS 294
|
..
gi 1133861166 309 QD 310
Cdd:cd19074 295 PE 296
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-310 |
5.78e-66 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 210.11 E-value: 5.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 13 VSALGLGCLNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAFWNEGCSGGESELLLGQWLKDRGNREHIVLATKV---G 89
Cdd:cd19094 1 VSEICLGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPSPETQGRTEEIIGSWLKKKGNRDKVVLATKVagpG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 90 AQPTIPGGGFEsmeGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPL------------------EETMEAFDRLV 151
Cdd:cd19094 81 EGITWPRGGGT---RLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLfgggyytepseeedsvsfEEQLEALGELV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 152 RAGKVRALGCSNHHTWRVEKARNISKSHHWASYSCIQQRYTYL-RpkpgadfgvqisANDELLNYCQTHDDFSLLAYSPL 230
Cdd:cd19094 158 KAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLnR------------NFEEGLAEACHRENVGLLAYSPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 231 ----LNGSYTRSDAPL-----------QKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQ 295
Cdd:cd19094 226 aggvLTGKYLDGAARPeggrlnlfpgyMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQ 305
|
330
....*....|....*
gi 1133861166 296 LQENLDSLNIRLTQD 310
Cdd:cd19094 306 LKENIDAFDVPLSDE 320
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
6-312 |
3.85e-60 |
|
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: 194.80 E-value: 3.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGCLNFG-----SRTDKETSYRLLDQYVDAGGSFLDTSNNYAFwnegcsgGESELLLGQWLKDRgnRE 80
Cdd:cd19149 4 LGKSGIEASVIGLGTWAIGggpwwGGSDDNESIRTIHAALDLGINLIDTAPAYGF-------GHSEEIVGKAIKGR--RD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATKVGAQPTIPGGGFESMEG-------LSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRA 153
Cdd:cd19149 75 KVVLATKCGLRWDREGGSFFFVRDgvtvyknLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 154 GKVRALGCSNHHTWRVEKARNIskshhwASYSCIQQRYTYLRPKpgadfgvqisANDELLNYCQTHdDFSLLAYSPL--- 230
Cdd:cd19149 155 GKIRAIGASNVSVEQIKEYVKA------GQLDIIQEKYSMLDRG----------IEKELLPYCKKN-NIAFQAYSPLeqg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 231 -LNGSYT----------RSDAPLQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQEN 299
Cdd:cd19149 218 lLTGKITpdrefdagdaRSGIPWFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEEN 297
|
330
....*....|...
gi 1133861166 300 LDSLNIRLTQDQL 312
Cdd:cd19149 298 AKAGDIRLSAEDI 310
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-318 |
9.27e-58 |
|
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: 188.79 E-value: 9.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNFGSR-------TDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcSGGESELLLGQWLKDRGNREHI 82
Cdd:cd19146 8 GVRVSPLCLGAMSFGEAwksmmgeCDKETAFKLLDAFYEQGGNFIDTANNY-------QGEESERWVGEWMASRGNRDEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 83 VLATK--VGAQPTIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALG 160
Cdd:cd19146 81 VLATKytTGYRRGGPIKIKSNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 161 CSNHHTWRVEKARNISKSHHWASYSCIQQRYTylrpkpgadfgvqISAND---ELLNYCQtHDDFSLLAYSPLLNGSYtR 237
Cdd:cd19146 161 VSDTPAWVVSKANAYARAHGLTQFVVYQGHWS-------------AAFRDferDILPMCE-AEGMALAPWGVLGQGQF-R 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 238 SDAplqkQYESEDAQAR------------LRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNI 305
Cdd:cd19146 226 TEE----EFKRRGRSGRkggpqtekerkvSEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI 301
|
330
....*....|...
gi 1133861166 306 RLTQDQLHRLHTA 318
Cdd:cd19146 302 SLSDEEIQEIEDA 314
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-315 |
5.77e-57 |
|
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: 186.27 E-value: 5.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 2 QQLLLGNTGIQVSALGLGCL---NFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAFwnegcsgGESELLLGQWLKDRgn 78
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMgmsAFYGPADEEESIATLHRALELGVTFLDTADMYGP-------GTNEELLGKALKDR-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 79 REHIVLATKVGAQpTIPGGGFESMEGlSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRA 158
Cdd:cd19076 72 RDEVVIATKFGIV-RDPGSGFRGVDG-RPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 159 LGCSNhhtwrvEKARNISKSHHWASYSCIQQRYT-YLRpkpGADFGVqISANDELlnycqthdDFSLLAYSPL----LNG 233
Cdd:cd19076 150 IGLSE------ASADTIRRAHAVHPITAVQSEYSlWTR---DIEDEV-LPTCREL--------GIGFVAYSPLgrgfLTG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 234 SYTRSDAPLQKQY---------ESEDAQARL-RVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSL 303
Cdd:cd19076 212 AIKSPEDLPEDDFrrnnprfqgENFDKNLKLvEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGAL 291
|
330
....*....|..
gi 1133861166 304 NIRLTQDQLHRL 315
Cdd:cd19076 292 DVVLTPEELAEI 303
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-315 |
2.71e-55 |
|
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: 180.50 E-value: 2.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNFGSRTDKETSYR-----LLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRgNREHIVL 84
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSDDkkaieALRYAIELGINLIDTAEMYG-------GGHAEELVGKAIKGF-DREDLFI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 85 ATKVgaqptipgggfeSMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNH 164
Cdd:cd19072 73 TTKV------------SPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 165 HTWRVEKARNISKSHHWASyscIQQRYTYLRPkpgadfgvqiSANDELLNYCQTHdDFSLLAYSPLLNGSYTRSDaplqk 244
Cdd:cd19072 141 SLEELEEAQSYLKKGPIVA---NQVEYNLFDR----------EEESGLLPYCQKN-GIAIIAYSPLEKGKLSNAK----- 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133861166 245 qyesedaqaRLRVLSEVAQETGGTLNQIVLAWLLqSTPTTLSIIAASKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19072 202 ---------GSPLLDEIAKKYGKTPAQIALNWLI-SKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-319 |
1.54e-54 |
|
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: 179.70 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 13 VSALGLGCLNFG-----SRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRgnREHIVLATK 87
Cdd:cd19085 1 VSRLGLGCWQFGggywwGDQDDEESIATIHAALDAGINFFDTAEAYG-------DGHSEEVLGKALKGR--RDDVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 88 VGAQPtipgggfesmegLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHTW 167
Cdd:cd19085 72 VSPDN------------LTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 168 RVEKARNISKshhwasYSCIQQRYTYLrpkpgadfgvQISANDELLNYCQTHdDFSLLAYSP----LLNGSYT------- 236
Cdd:cd19085 140 QLEEALDAGR------IDSNQLPYNLL----------WRAIEYEILPFCREH-GIGVLAYSPlaqgLLTGKFSsaedfpp 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 237 ---RSDAPL--QKQYESEdAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLTQDQ 311
Cdd:cd19085 203 gdaRTRLFRhfEPGAEEE-TFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSV 281
|
....*...
gi 1133861166 312 LHRLHTAG 319
Cdd:cd19085 282 LERLDEIS 289
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-315 |
8.65e-54 |
|
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: 178.56 E-value: 8.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGC-LNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRG-N 78
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYA-------NGQSEEIMGQAIKELGwP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 79 REHIVLATKV--GAqptipGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKV 156
Cdd:cd19143 74 RSDYVVSTKIfwGG-----GGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 157 RALGCSNhhtWR---VEKARNISKSHHWASYSCIQQRYTYL-RPKpgadFGVQISANDELLNYCQThdDFSLLAySPLLN 232
Cdd:cd19143 149 FYWGTSE---WSaqqIEEAHEIADRLGLIPPVMEQPQYNLFhRER----VEVEYAPLYEKYGLGTT--TWSPLA-SGLLT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 233 GSY-------TRSDAP------LQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQEN 299
Cdd:cd19143 219 GKYnngipegSRLALPgyewlkDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEEN 298
|
330
....*....|....*...
gi 1133861166 300 LDSLNI--RLTQDQLHRL 315
Cdd:cd19143 299 LKALEVlpKLTPEVMEKI 316
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-302 |
4.04e-50 |
|
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: 166.50 E-value: 4.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 11 IQVSALGLGCLNFGSRT----DKETSYRLLDQYVDAGGSFLDTSNNYafwnegcSGGESELLLGQWLKDRgnREHIVLAT 86
Cdd:cd19086 1 LEVSEIGFGTWGLGGDWwgdvDDAEAIRALRAALDLGINFFDTADVY-------GDGHSERLLGKALKGR--RDKVVIAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 87 KVGaqpTIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHI-DDVNTPLEETMEAFDRLVRAGKVRALGCSnhh 165
Cdd:cd19086 72 KFG---NRFDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNpPDEVLDNDELFEALEKLKQEGKIRAYGVS--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 166 TWRVEKARNISKShhwASYSCIQQRYTYLRPKPGadfgvqisanDELLNYCQTHdDFSLLAYSPLLNGSYTrsdaplqkq 245
Cdd:cd19086 146 VGDPEEALAALRR---GGIDVVQVIYNLLDQRPE----------EELFPLAEEH-GVGVIARVPLASGLLT--------- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1133861166 246 yesedaqarlrvlsevaqetgGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDS 302
Cdd:cd19086 203 ---------------------GKLAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-318 |
1.25e-48 |
|
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: 164.33 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCL----NFGSRTDKETSYRLLDQYVDAGGSFLDTSNNY-AFWNEgcsggeseLLLGQWLKdrGNREHIVL 84
Cdd:cd19078 1 GLEVSAIGLGCMgmshGYGPPPDKEEMIELIRKAVELGITFFDTAEVYgPYTNE--------ELVGEALK--PFRDQVVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 85 ATKVGaqPTIPGGGFESMEGLSRKA-IEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSN 163
Cdd:cd19078 71 ATKFG--FKIDGGKPGPLGLDSRPEhIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 164 hhtwrvEKARNISKSHHWASYSCIQQRYTYLRPKPgadfgvqisaNDELLNYCQtHDDFSLLAYSPL----LNGSYT--- 236
Cdd:cd19078 149 ------AGVETIRRAHAVCPVTAVQSEYSMMWREP----------EKEVLPTLE-ELGIGFVPFSPLgkgfLTGKIDent 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 237 -------RSDAPlQKQYESEDA-QARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLT 308
Cdd:cd19078 212 kfdegddRASLP-RFTPEALEAnQALVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELT 290
|
330
....*....|
gi 1133861166 309 QDQLHRLHTA 318
Cdd:cd19078 291 PEELREIEDA 300
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
6-312 |
6.10e-48 |
|
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: 162.97 E-value: 6.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGC-----LNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAFwnegcsgGESELLLGQWLKDRgNRE 80
Cdd:cd19083 4 LGKSDIDVNPIGLGTnavggHNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGL-------GRSEELVGEVLKEY-NRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATKvGAqptIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALG 160
Cdd:cd19083 76 EVVIATK-GA---HKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 161 CSNHhtwrveKARNISKSHHWASYSCIQQRYTYLrpkpgadfgvQISANDELLNYCQTHdDFSLLAYSPL----LNGSYT 236
Cdd:cd19083 152 VSNF------SLEQLKEANKDGYVDVLQGEYNLL----------QREAEEDILPYCVEN-NISFIPYFPLasglLAGKYT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 237 R----SDAPLQKQ---YESEDAQARLRV---LSEVAQETGGTLNQIVLAWLLqSTPTTLSIIA-ASKPEQLQENLDSLNI 305
Cdd:cd19083 215 KdtkfPDNDLRNDkplFKGERFSENLDKvdkLKSIADEKGVTVAHLALAWYL-TRPAIDVVIPgAKRAEQVIDNLKALDV 293
|
....*..
gi 1133861166 306 RLTQDQL 312
Cdd:cd19083 294 TLTEEEI 300
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
6-312 |
2.29e-47 |
|
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: 161.27 E-value: 2.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSA--LGLGClNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwneGCSGGESELLLGQWLKD--RGNREH 81
Cdd:cd19089 4 CGRSGLHLPAisLGLWH-NFGDYTSPEEARELLRTAFDLGITHFDLANNY-----GPPPGSAEENFGRILKRdlRPYRDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 82 IVLATKVGAQpTIPG--GGfesmeGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRAL 159
Cdd:cd19089 78 LVISTKAGYG-MWPGpyGD-----GGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 160 GCSNHHTWRVEKARNISKSHHwASYSCIQQRYTYLRPKPgadfgvqisaNDELLNYCQtHDDFSLLAYSPL--------- 230
Cdd:cd19089 152 GISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDRWA----------EDGLLEVLE-EAGIGFIAFSPLaqglltdky 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 231 LNG-----SYTRSDAPLQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSL-N 304
Cdd:cd19089 220 LNGippdsRRAAESKFLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALkN 299
|
....*...
gi 1133861166 305 IRLTQDQL 312
Cdd:cd19089 300 LDFSEEEL 307
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-312 |
1.17e-46 |
|
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: 159.92 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCLNF----GSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsgGESELLLGQWLK-D 75
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLsafyGPPKPDEERFAVLDAAFELGCTFWDTADIY---------GDSEELIGRWFKqN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 76 RGNREHIVLATKVGAQPTIPGGGFeSMEGlSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGK 155
Cdd:cd19144 72 PGKREKIFLATKFGIEKNVETGEY-SVDG-SPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 156 VRALGCSNhhtwrvEKARNISKSHHWASYSCIQQRYTylrPkpgadFGVQISAND-ELLNYCQtHDDFSLLAYSPL---- 230
Cdd:cd19144 150 IKHIGLSE------CSAETLRRAHAVHPIAAVQIEYS---P-----FSLDIERPEiGVLDTCR-ELGVAIVAYSPLgrgf 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 231 LNGSYT----------RSDAPlqkQYESEDAQARLRV---LSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQ 297
Cdd:cd19144 215 LTGAIRspddfeegdfRRMAP---RFQAENFPKNLELvdkIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLE 291
|
330
....*....|....*
gi 1133861166 298 ENLDSLNIRLTQDQL 312
Cdd:cd19144 292 ENLGALKVKLTEEEE 306
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-318 |
1.93e-46 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 158.78 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCLNFGS--RTDKETSyRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDR-G 77
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEwdLSPAEAA-ALIEAALELGITTFDHADIYG-------GYTCEALFGEALKLSpS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 78 NREHIVLATKVGAQPtiPGGGFESMEG---LSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDvntPL---EETMEAFDRLV 151
Cdd:COG4989 73 LREKIELQTKCGIRL--PSEARDNRVKhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPD---PLmdpEEVAEAFDELK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 152 RAGKVRALGCSNHHTWRVEkarniskshhwasysCIQqryTYLRPKPGADfGVQISA------NDELLNYCQTHdDFSLL 225
Cdd:COG4989 148 ASGKVRHFGVSNFTPSQFE---------------LLQ---SALDQPLVTN-QIELSLlhtdafDDGTLDYCQLN-GITPM 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 226 AYSPLLNGSYTRSDaplqkqyeSEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNI 305
Cdd:COG4989 208 AWSPLAGGRLFGGF--------DEQFPRLRAALDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDI 279
|
330
....*....|...
gi 1133861166 306 RLTQDQLHRLHTA 318
Cdd:COG4989 280 ELTREEWYELYEA 292
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
10-315 |
2.59e-46 |
|
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: 159.22 E-value: 2.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNFGS-------RTDKETSYRLLDQYVDAGGSFLDTSNNYAfwNEgcsggESELLLGQWLKDRGNREHI 82
Cdd:cd19147 7 GIRVSPLILGAMSIGDawsgfmgSMDKEQAFELLDAFYEAGGNFIDTANNYQ--DE-----QSETWIGEWMKSRKNRDQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 83 VLATKVGAQPT---IPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRAL 159
Cdd:cd19147 80 VIATKFTTDYKayeVGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 160 GCSNHHTWRVEKARNISKSHHWASYSCIQQRYTYLRpkpgADFgvqisaNDELLNYCQtHDDFSLLAYSPLLNGSYTRSD 239
Cdd:cd19147 160 GVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLN----RDF------ERDIIPMAR-HFGMALAPWDVLGGGKFQSKK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 240 APLQKQYESE--------DAQARLRV-----LSEVAQETG-GTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNI 305
Cdd:cd19147 229 AVEERKKNGEglrsfvggTEQTPEEVkiseaLEKVAEEHGtESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSI 308
|
330
....*....|
gi 1133861166 306 RLTQDQLHRL 315
Cdd:cd19147 309 KLTPEEIEYL 318
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-303 |
1.81e-45 |
|
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: 156.18 E-value: 1.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 18 LGCLNFG---SRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcSGGESELLLGQwlKDRGNREhIVLATKvgAQPTI 94
Cdd:cd19075 5 LGTMTFGsqgRFTTAEAAAELLDAFLERGHTEIDTARVY-------PDGTSEELLGE--LGLGERG-FKIDTK--ANPGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 95 PGGgfesmegLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHTWRVEKARN 174
Cdd:cd19075 73 GGG-------LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 175 ISKSHHWASYSCIQQRYTYL-RpkpgadfgvqiSANDELLNYCQTHdDFSLLAYSPL----LNGSYTRSDAPL------- 242
Cdd:cd19075 146 ICKENGWVLPTVYQGMYNAItR-----------QVETELFPCLRKL-GIRFYAYSPLaggfLTGKYKYSEDKAgggrfdp 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133861166 243 --------QKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPttLS-------IIAASKPEQLQENLDSL 303
Cdd:cd19075 214 nnalgklyRDRYWKPSYFEALEKVEEAAEKEGISLAEAALRWLYHHSA--LDgekgdgvILGASSLEQLEENLAAL 287
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-315 |
2.92e-45 |
|
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: 155.46 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 12 QVSALGLGCLNFGSRT-------DKETSYRLLDQYVDAGGSFLDTSNNYafwnegcSGGESELLLGQWLKDRGNREHIVL 84
Cdd:cd19093 1 EVSPLGLGTWQWGDRLwwgygeyGDEDLQAAFDAALEAGVNLFDTAEVY-------GTGRSERLLGRFLKELGDRDEVVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 85 ATKVGAQPTipgggfesmeGLSRKAIEQAIDGSLRRLGTDYVDLY----YAHiddVNTPLEETMEAFDRLVRAGKVRALG 160
Cdd:cd19093 74 ATKFAPLPW----------RLTRRSVVKALKASLERLGLDSIDLYqlhwPGP---WYSQIEALMDGLADAVEEGLVRAVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 161 CSNHHTWRVEKARNISKSHHwASYSCIQQRYTYLRPKPgadfgvqisANDELLNYCQTHdDFSLLAYSPL----LNGSYT 236
Cdd:cd19093 141 VSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRDP---------EQNGLLPACDEL-GITLIAYSPLaqglLTGKYS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 237 RSDAP--------LQKQYesEDAQARLRVLSEVAQETGGTLNQIVLAWLLQStpTTLSIIAASKPEQLQENLDSLNIRLT 308
Cdd:cd19093 210 PENPPpggrrrlfGRKNL--EKVQPLLDALEEIAEKYGKTPAQVALNWLIAK--GVVPIPGAKNAEQAEENAGALGWRLS 285
|
....*..
gi 1133861166 309 QDQLHRL 315
Cdd:cd19093 286 EEEVAEL 292
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-318 |
3.24e-44 |
|
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: 152.71 E-value: 3.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLNFG-SRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLK-DRGNREHIVLA 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLAdWGESAEELLSLIEAALELGITTFDHADIYG-------GGKCEELFGEALAlNPGLREKIEIQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 86 TKVGAQPTIPGGGFESME-GLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDvntPL---EETMEAFDRLVRAGKVRALGC 161
Cdd:cd19092 74 TKCGIRLGDDPRPGRIKHyDTSKEHILASVEGSLKRLGTDYLDLLLLHRPD---PLmdpEEVAEAFDELVKSGKVRYFGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 162 SNHHTWRVEkarniskshhwasyscIQQRYTylrPKPGADFGVQISA------NDELLNYCQTHdDFSLLAYSPLLNGSY 235
Cdd:cd19092 151 SNFTPSQIE----------------LLQSYL---DQPLVTNQIELSLlhteaiDDGTLDYCQLL-DITPMAWSPLGGGRL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 236 TRSDAPLQKqyesedaqaRLR-VLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLTQDQLHR 314
Cdd:cd19092 211 FGGFDERFQ---------RLRaALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREEWYE 281
|
....
gi 1133861166 315 LHTA 318
Cdd:cd19092 282 IYEA 285
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-312 |
1.40e-43 |
|
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: 151.79 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 7 GNTGIQVSALGLGCL-NFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwneGCSGGESELLLGQWLKD--RGNREHIV 83
Cdd:cd19151 6 GRSGLKLPAISLGLWhNFGDVDRYENSRAMLRRAFDLGITHFDLANNY-----GPPPGSAEENFGRILKEdlKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVGaQPTIPG--GGFESmeglsRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGC 161
Cdd:cd19151 81 ISTKAG-YTMWPGpyGDWGS-----KKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 162 SNHHTWRVEKARNISKSH------HWASYSCIQQrytylrpkpgadfgvqiSANDELLNYCQtHDDFSLLAYSPLLNGSY 235
Cdd:cd19151 155 SNYPPEEAREAAAILKDLgtpcliHQPKYSMFNR-----------------WVEEGLLDVLE-EEGIGCIAFSPLAQGLL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 236 T--------------RSDAPLQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLD 301
Cdd:cd19151 217 TdrylngipedsraaKGSSFLKPEQITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVG 296
|
330
....*....|..
gi 1133861166 302 SL-NIRLTQDQL 312
Cdd:cd19151 297 ALdNREFSEEEL 308
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-317 |
2.04e-43 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 152.32 E-value: 2.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCLNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAFWNEGCSGGESELLLGQWLKDRGNRE 80
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPRPETQGLTETYIGNWLAKRGSRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATKVGAQPTIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLY----------------YAHIDDVNT-PLEET 143
Cdd:PRK10625 81 KLIIASKVSGPSRNNDKGIRPNQALDRKNIREALHDSLKRLQTDYLDLYqvhwpqrptncfgklgYSWTDSAPAvSLLET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 144 MEAFDRLVRAGKVRALGCSNHHTWRVEKARNISKSHHWASYSCIQQRYTYLrpkpGADFGVQISANDEllnycqtHDDFS 223
Cdd:PRK10625 161 LDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLL----NRSFEVGLAEVSQ-------YEGVE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 224 LLAYSPL----LNGSYTRSDAPLQK---------QYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAA 290
Cdd:PRK10625 230 LLAYSCLafgtLTGKYLNGAKPAGArntlfsrftRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330 340 350
....*....|....*....|....*....|...
gi 1133861166 291 SKPEQLQENLDSLNIRLTQDQL------HRLHT 317
Cdd:PRK10625 310 TTMEQLKTNIESLHLTLSEEVLaeieavHQVYT 342
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-318 |
4.81e-43 |
|
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: 150.13 E-value: 4.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 40 VDAGGSFLDTSNNYAFwnegcsgGESELLLGQWLKDRgnREHIVLATKVGAQPTIPGGGFESmegLSRKAIEQAIDGSLR 119
Cdd:cd19102 36 LDLGINWIDTAAVYGL-------GHSEEVVGRALKGL--RDRPIVATKCGLLWDEEGRIRRS---LKPASIRAECEASLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 120 RLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNhhtWRVEKARNISKSHHWASyscIQQRYTYLRPkpg 199
Cdd:cd19102 104 RLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSN---FSVDQMKRCQAIHPIAS---LQPPYSLLRR--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 200 adfgvQISAndELLNYCQTHdDFSLLAYSP----LLNGSYTR-SDAPL----QKQYESEDAQARLR-------VLSEVAQ 263
Cdd:cd19102 175 -----GIEA--EILPFCAEH-GIGVIVYSPmqsgLLTGKMTPeRVASLpaddWRRRSPFFQEPNLArnlalvdALRPIAE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1133861166 264 ETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLTQDQLHRLHTA 318
Cdd:cd19102 247 RHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-308 |
6.36e-41 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 143.13 E-value: 6.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 13 VSALGLGCLNF------GSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRGNRehIVLAT 86
Cdd:cd19088 1 VSRLGYGAMRLtgpgiwGPPADREEAIAVLRRALELGVNFIDTADSYG-------PDVNERLIAEALHPYPDD--VVIAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 87 KVGAqpTIPGGGFESMEGlSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHT 166
Cdd:cd19088 72 KGGL--VRTGPGWWGPDG-SPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 167 WRVEKARNIskshhwASYSCIQQRYTYLRPKPgadfgvqisanDELLNYCqTHDDFSLLAYSPLlngsytRSDAPLQkqy 246
Cdd:cd19088 149 AQIEEARAI------VRIVSVQNRYNLANRDD-----------EGVLDYC-EAAGIAFIPWFPL------GGGDLAQ--- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133861166 247 esedaqaRLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLT 308
Cdd:cd19088 202 -------PGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-315 |
1.71e-39 |
|
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: 139.69 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 9 TGIQVSALGLGCLNFG-SRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRgnREHIVLATK 87
Cdd:cd19138 7 DGTKVPALGQGTWYMGeDPAKRAQEIEALRAGIDLGMTLIDTAEMYG-------DGGSEELVGEAIRGR--RDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 88 VgaQPTipgggfesmeGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDvNTPLEETMEAFDRLVRAGKVRALGCSNHHTW 167
Cdd:cd19138 78 V--LPS----------NASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 168 RVEKARNISKSHHWAsysCIQQRYTYlrPKPGADFgvqisandELLNYCQTHdDFSLLAYSPLLNGSYTRSDAPLQKqye 247
Cdd:cd19138 145 DMEELWAVPGGGNCA---ANQVLYNL--GSRGIEY--------DLLPWCREH-GVPVMAYSPLAQGGLLRRGLLENP--- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133861166 248 sedaqarlrVLSEVAQETGGTLNQIVLAWLLQStPTTLSIIAASKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19138 208 ---------TLKEIAARHGATPAQVALAWVLRD-GNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
10-318 |
4.16e-39 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 138.26 E-value: 4.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGClnfgSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwNEGcsggeselLLGQWLKDRG-NREHIVLATKV 88
Cdd:COG0656 2 GVEIPALGLGT----WQLPGEEAAAAVRTALEAGYRHIDTAAMYG--NEE--------GVGEAIAASGvPREELFVTTKV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 89 GAqptipgggfesmEGLSRKAIEQAIDGSLRRLGTDYVDLYYAH--IDDvntPLEETMEAFDRLVRAGKVRALGCSNHHT 166
Cdd:COG0656 68 WN------------DNHGYDDTLAAFEESLERLGLDYLDLYLIHwpGPG---PYVETWRALEELYEEGLIRAIGVSNFDP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 167 WRVEKARNISkshhwasysciqqrytylrpkpgadfGVQISAN----------DELLNYCQTHdDFSLLAYSPLlngsyt 236
Cdd:COG0656 133 EHLEELLAET--------------------------GVKPAVNqvelhpylqqRELLAFCREH-GIVVEAYSPL------ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 237 rsdaplqkqyesedAQARL---RVLSEVAQETGGTLNQIVLAWLLQstpttLSIIA---ASKPEQLQENLDSLNIRLTQD 310
Cdd:COG0656 180 --------------GRGKLlddPVLAEIAEKHGKTPAQVVLRWHLQ-----RGVVVipkSVTPERIRENLDAFDFELSDE 240
|
....*...
gi 1133861166 311 QLHRLHTA 318
Cdd:COG0656 241 DMAAIDAL 248
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-315 |
5.97e-39 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 140.51 E-value: 5.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCL-NFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwneGCSGGESELLLGQWLKD--RG 77
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWhNFGHVNALESQRAILRKAFDLGITHFDLANNY-----GPPPGSAEENFGRLLREdfAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 78 NREHIVLATKVGAQpTIPGggfESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVR 157
Cdd:PRK09912 88 YRDELIISTKAGYD-MWPG---PYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 158 ALGCSNHHTWRVEKARNIskSHHWASYSCIQQrytylrpkPGADFGVQISANDELLNYCQThDDFSLLAYSP----LLNG 233
Cdd:PRK09912 164 YVGISSYSPERTQKMVEL--LREWKIPLLIHQ--------PSYNLLNRWVDKSGLLDTLQN-NGVGCIAFTPlaqgLLTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 234 SYTrSDAPLQKQYESEDAQAR--------------LRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQEN 299
Cdd:PRK09912 233 KYL-NGIPQDSRMHREGNKVRgltpkmlteanlnsLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEEN 311
|
330
....*....|....*..
gi 1133861166 300 LDSL-NIRLTQDQLHRL 315
Cdd:PRK09912 312 VQALnNLTFSTEELAQI 328
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-313 |
1.59e-38 |
|
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: 138.21 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNFGSR----TDKETSYRLLDQYVDAGGSFLDTSNNYAFwnegcsgGESELLLGQWLKDRGNREHIVLA 85
Cdd:cd19148 1 DLPVSRIALGTWAIGGWmwggTDEKEAIETIHKALDLGINLIDTAPVYGF-------GLSEEIVGKALKEYGKRDRVVIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 86 TKVGAQpTIPGGGFesMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHH 165
Cdd:cd19148 74 TKVGLE-WDEGGEV--VRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 166 TWRVEKARNISKSHhwasysCIQQRYTYLRPKpgadfgvqisANDELLNYCQTHdDFSLLAYSP----LLNGSYT----- 236
Cdd:cd19148 151 PEQMETFRKVAPLH------TVQPPYNLFERE----------IEKDVLPYARKH-NIVTLAYGAlcrgLLSGKMTkdtkf 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 237 ------RSDAPLQKQYESEDAQARLRvLSEVAQETGGT-LNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLTQ 309
Cdd:cd19148 214 egddlrRTDPKFQEPRFSQYLAAVEE-LDKLAQERYGKsVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLND 292
|
....
gi 1133861166 310 DQLH 313
Cdd:cd19148 293 EDMK 296
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
7-312 |
1.98e-38 |
|
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: 137.97 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 7 GNTGIQVSALGLGCL-NFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwneGCSGGESELLLGQWLKD--RGNREHIV 83
Cdd:cd19150 6 GKSGLKLPALSLGLWhNFGDDTPLETQRAILRTAFDLGITHFDLANNY-----GPPPGSAEENFGRILREdfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVGAQpTIPGggfESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSN 163
Cdd:cd19150 81 ISTKAGYD-MWPG---PYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 164 HHTWRVEKARNISKSH------HWASYSCIqQRYTylrpkpgadfgvqisANDELLNycqTHDDFSL--LAYSPL----- 230
Cdd:cd19150 157 YSPERTREAAAILRELgtplliHQPSYNML-NRWV---------------EESGLLD---TLQELGVgcIAFTPLaqgll 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 231 ----LNG----SYTRSDAPLQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDS 302
Cdd:cd19150 218 tdkyLNGipegSRASKERSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGA 297
|
330
....*....|.
gi 1133861166 303 L-NIRLTQDQL 312
Cdd:cd19150 298 LdNLTFSADEL 308
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-315 |
5.43e-38 |
|
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: 135.78 E-value: 5.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNFGSR-----TDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRgNREHIVL 84
Cdd:cd19137 1 GEKIPALGLGTWGIGGFltpdySRDEEMVELLKTAIELGYTHIDTAEMYG-------GGHTEELVGKAIKDF-PREDLFI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 85 ATKVgaQPTipgggfesmeGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNH 164
Cdd:cd19137 73 VTKV--WPT----------NLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 165 HTWRVEKARNISKShhwaSYSCIQQRYTYLRPKPgadfgvqisANDELLNYCQtHDDFSLLAYSPLLNGsytrsdaplqk 244
Cdd:cd19137 141 NRRLLEEAISKSQT----PIVCNQVKYNLEDRDP---------ERDGLLEYCQ-KNGITVVAYSPLRRG----------- 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133861166 245 qyesedAQARLRVLSEVAQETGGTLNQIVLAWLLQStPTTLSIIAASKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19137 196 ------LEKTNRTLEEIAKNYGKTIAQIALAWLIQK-PNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-302 |
3.94e-36 |
|
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: 130.43 E-value: 3.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNFG----SRTDKETSyRLLDQYVDAGGSFLDTSNNYafwnegcsgGESELLLGQWLKDRgNREHIVLATKVG 89
Cdd:cd19095 1 SVLGLGTSGIGrvwgVPSEAEAA-RLLNTALDLGINLIDTAPAY---------GRSEERLGRALAGL-RRDDLFIATKVG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 90 AqptiPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSnHHTWRV 169
Cdd:cd19095 70 T----HGEGGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVS-GDGEEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 170 EKARnisKSHHwasYSCIQQRYTYLRPkpgadfgvqisANDELLNYCQTHdDFSLLAYSPLLNGSYTRSDAPLqkqYESE 249
Cdd:cd19095 145 EAAI---ASGV---FDVVQLPYNVLDR-----------EEEELLPLAAEA-GLGVIVNRPLANGRLRRRVRRR---PLYA 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1133861166 250 DAQARLRVLSEVAQETGGtlnQIVLAWLLQSTPTTLSIIAASKPEQLQENLDS 302
Cdd:cd19095 204 DYARRPEFAAEIGGATWA---QAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
6-310 |
8.88e-36 |
|
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: 131.03 E-value: 8.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGC-LNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRG-NREHIV 83
Cdd:cd19141 5 LGKSGLRVSCLGLGTwVTFGSQISDEVAEELVTLAYENGINLFDTAEVYA-------AGKAEIVLGKILKKKGwRRSSYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVgaqptIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSN 163
Cdd:cd19141 78 ITTKI-----FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 164 HHTWRVEKARNISKSHHWASYSCIQQRYTYL-RPKpgadFGVQISandELLNYCQThddfSLLAYSPL----LNGSYTR- 237
Cdd:cd19141 153 WSAMEIMEAYSVARQFNLIPPIVEQAEYHLFqREK----VEMQLP---ELFHKIGV----GAMTWSPLacgiLSGKYDDg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 238 ----SDAPLqKQYE-------SEDA---QARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSL 303
Cdd:cd19141 222 vpeySRASL-KGYQwlkekilSEEGrrqQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAI 300
|
....*....
gi 1133861166 304 NIR--LTQD 310
Cdd:cd19141 301 QVLpkLTPN 309
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-165 |
1.21e-35 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 128.75 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGCLNFGSRTDKETSyRLLDQYVDAGGSFLDTSNNYafwnegcsgGESELLLGQWLKDRgnREHIVLA 85
Cdd:cd19100 4 LGRTGLKVSRLGFGGGPLGRLSQEEAA-AIIRRALDLGINYFDTAPSY---------GDSEEKIGKALKGR--RDKVFLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 86 TKVGAQptipgggfesmeglSRKAIEQAIDGSLRRLGTDYVDLYYAH----IDDVNTPLEE--TMEAFDRLVRAGKVRAL 159
Cdd:cd19100 72 TKTGAR--------------DYEGAKRDLERSLKRLGTDYIDLYQLHavdtEEDLDQVFGPggALEALLEAKEEGKIRFI 137
|
....*.
gi 1133861166 160 GCSNHH 165
Cdd:cd19100 138 GISGHS 143
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
6-315 |
9.69e-35 |
|
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: 128.32 E-value: 9.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGCLNF----GSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsGGES-ELLLGQWLKDrGNRE 80
Cdd:cd19145 5 LGSQGLEVSAQGLGCMGLsgdyGAPKPEEEGIALIHHAFNSGVTFLDTSDIY--------GPNTnEVLLGKALKD-GPRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATKVGaqptIPGGGFESMEGLSRKA-IEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRAL 159
Cdd:cd19145 76 KVQLATKFG----IHEIGGSGVEVRGDPAyVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 160 GCSNhhtwrvEKARNISKSHHWASYSCIQQRYT-YLRpkpgadfgvqiSANDELLNYCQTHdDFSLLAYSPL-------- 230
Cdd:cd19145 152 GLSE------ASADTIRRAHAVHPITAVQLEWSlWTR-----------DIEEEIIPTCREL-GIGIVPYSPLgrgffagk 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 231 ------LNGSYTRSDAPLQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLN 304
Cdd:cd19145 214 akleelLENSDVRKSHPRFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALS 293
|
330
....*....|.
gi 1133861166 305 IRLTQDQLHRL 315
Cdd:cd19145 294 VKLTKEDLKEI 304
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-315 |
4.98e-34 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 127.63 E-value: 4.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCLNFgSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsgGESELLLGQWLKdrGNRE 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRL-PRKDEEEAEALIRRAIDNGINYIDTARGY---------GDSEEFLGKALK--GPRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATKVgaQPTIPgggfesmeglSRKAIEQAIDGSLRRLGTDYVDLYYAH-IDDVNTpLEET------MEAFDRLVRA 153
Cdd:COG1453 69 KVILATKL--PPWVR----------DPEDMRKDLEESLKRLQTDYIDLYLIHgLNTEED-LEKVlkpggaLEALEKAKAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 154 GKVRALGCSNHHtwRVEKARNISKSHHWasySCIQQRYTYLrpkpgaDFGVQisANDELLNYCQTHdDFSLLAYSPLLNG 233
Cdd:COG1453 136 GKIRHIGFSTHG--SLEVIKEAIDTGDF---DFVQLQYNYL------DQDNQ--AGEEALEAAAEK-GIGVIIMKPLKGG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 234 SYTRsdaplqkqyESEDAQARLRVLSEVAQetggtLNqivLAWLLQSTPTTLSIIAASKPEQLQENLDSLN--IRLTQDQ 311
Cdd:COG1453 202 RLAN---------PPEKLVELLCPPLSPAE-----WA---LRFLLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEE 264
|
....
gi 1133861166 312 LHRL 315
Cdd:COG1453 265 LAIL 268
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-315 |
6.97e-34 |
|
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: 124.31 E-value: 6.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 15 ALGLGclNFGSRTDkeTSYRLLDQYVDAGGSFLDTSnnYAFWNEGcsggeselLLGQWLKDRG-NREHIVLATKVgaqpt 93
Cdd:cd19073 3 ALGLG--TWQLRGD--DCANAVKEALELGYRHIDTA--EIYNNEA--------EVGEAIAESGvPREDLFITTKV----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 94 ipgggfeSMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHTWRVEKAR 173
Cdd:cd19073 64 -------WRDHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 174 NISKshhwASYSCIQQRY-TYLRPKpgadfgvqisandELLNYCQTHdDFSLLAYSPLLNGSYtrsdaplqkqyesedaq 252
Cdd:cd19073 137 DISP----LPIAVNQVEFhPFLYQA-------------ELLEYCREN-DIVITAYSPLARGEV----------------- 181
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133861166 253 ARLRVLSEVAQETGGTLNQIVLAWLLQStpTTLSIIAASKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19073 182 LRDPVIQEIAEKYDKTPAQVALRWLVQK--GIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-303 |
3.38e-33 |
|
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: 122.69 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCLNFGSRtdketSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRGnRE 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRE-----SPELLRRALDLGINYFDTAEGYG-------NGNSEEIIGEALKGLR-RD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATKVGAQptipgggfesMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHidDVNTP-----LEETMEAFDRLVRAGK 155
Cdd:cd19105 68 KVFLATKASPR----------LDKKDKAELLKSVEESLKRLQTDYIDIYQLH--GVDTPeerllNEELLEALEKLKKEGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 156 VRALGCSNHHTwRVEKARNISKSHHWasySCIQQRYTYLRPKPGAdfgvqisanDELLNYCQTHdDFSLLAYSPLLNGSY 235
Cdd:cd19105 136 VRFIGFSTHDN-MAEVLQAAIESGWF---DVIMVAYNFLNQPAEL---------EEALAAAAEK-GIGVVAMKTLAGGYL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133861166 236 TRSDAPlqkqyesedaqarlrvlseVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSL 303
Cdd:cd19105 202 QPALLS-------------------VLKAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
6-305 |
8.27e-33 |
|
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: 123.61 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGC-LNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRG-NREHIV 83
Cdd:cd19159 6 LGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVgaqptIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSN 163
Cdd:cd19159 79 ITTKL-----YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 164 HHTWRVEKARNISKSHHWASYSCIQQRY-TYLRPKpgadFGVQISandELLNYCQThddfSLLAYSPL----LNGSY--- 235
Cdd:cd19159 154 WSAMEIMEAYSVARQFNMIPPVCEQAEYhLFQREK----VEVQLP---ELYHKIGV----GAMTWSPLacgiISGKYgng 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 236 ----TRSDAP----LQKQYESEDA---QARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLN 304
Cdd:cd19159 223 vpesSRASLKcyqwLKERIVSEEGrkqQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 302
|
.
gi 1133861166 305 I 305
Cdd:cd19159 303 V 303
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-315 |
1.35e-32 |
|
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: 121.05 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 15 ALGLGClnfgSRTDKETSYRLLDQYVDAGGSFLDTSNNYafWNEGCsggesellLGQWLKDRG-NREHIVLATKVgaqpt 93
Cdd:cd19071 3 LIGLGT----YKLKPEETAEAVLAALEAGYRHIDTAAAY--GNEAE--------VGEAIRESGvPREELFITTKL----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 94 ipgggfeSMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAH------IDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHtw 167
Cdd:cd19071 64 -------WPTDHGYERVREALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFN-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 168 rvekarniskSHHwasyscIQQRYTYLRPKPGAdfgVQI-----SANDELLNYCQTHDdFSLLAYSPLLNGSYTRSDAPl 242
Cdd:cd19071 135 ----------VEH------LEELLAAARIKPAV---NQIelhpyLQQKELVEFCKEHG-IVVQAYSPLGRGRRPLLDDP- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133861166 243 qkqyesedaqarlrVLSEVAQETGGTLNQIVLAWLLQS--TPTTLSiiaaSKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19071 194 --------------VLKEIAKKYGKTPAQVLLRWALQRgvVVIPKS----SNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
6-315 |
2.03e-31 |
|
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: 119.80 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGC-LNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRG-NREHIV 83
Cdd:cd19158 6 LGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVgaqptIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSN 163
Cdd:cd19158 79 ITTKI-----FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 164 HHTWRVEKARNISKSHHWASYSCIQQRY-TYLRPKpgadFGVQISandELLNYCQThddfSLLAYSPL----LNGSYTRS 238
Cdd:cd19158 154 WSSMEIMEAYSVARQFNLIPPICEQAEYhMFQREK----VEVQLP---ELFHKIGV----GAMTWSPLacgiVSGKYDSG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 239 DAP-----------LQKQYESEDA---QARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLN 304
Cdd:cd19158 223 IPPysraslkgyqwLKDKILSEEGrrqQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQ 302
|
330
....*....|...
gi 1133861166 305 I--RLTQDQLHRL 315
Cdd:cd19158 303 VlpKLSSSIVHEI 315
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-313 |
3.81e-31 |
|
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: 118.42 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNTGIQVSALGLGCLNFGS---RTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcSGGESELLLGQWLKDrG 77
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGvfgPVDEEEAIRTVHEALDSGINYIDTAPWY-------GQGRSETVLGKALKG-I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 78 NREHIVLATKVGAQPTIPGGGFEsmegLSRKAIEQAIDGSLRRLGTDYVDLYYAH----IDDVNTPLEETMEAFDRLVRA 153
Cdd:cd19163 73 PRDSYYLATKVGRYGLDPDKMFD----FSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 154 GKVRALGCSnhhtwrvekARNISKSHHWASYSciqqrytylrpkpgadfGVQIsanDELLNYCQ-THDDFSLLAYSPLL- 231
Cdd:cd19163 149 GKVRFIGIT---------GYPLDVLKEVLERS-----------------PVKI---DTVLSYCHyTLNDTSLLELLPFFk 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 232 -------NGSYTR----SDAPLQKQYE-SEDAQARLRVLSEVAQETGGTLNQIVLAWLLQST--PTTLsiIAASKPEQLQ 297
Cdd:cd19163 200 ekgvgviNASPLSmgllTERGPPDWHPaSPEIKEACAKAAAYCKSRGVDISKLALQFALSNPdiATTL--VGTASPENLR 277
|
330
....*....|....*.
gi 1133861166 298 ENLDSLNIRLTQDQLH 313
Cdd:cd19163 278 KNLEAAEEPLDAHLLA 293
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
6-305 |
9.02e-31 |
|
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: 118.16 E-value: 9.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGC-LNFGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRG-NREHIV 83
Cdd:cd19160 8 LGKSGLRVSCLGLGTwVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYA-------AGKAERTLGNILKSKGwRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVgaqptIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSN 163
Cdd:cd19160 81 VTTKI-----YWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 164 HHTWRVEKARNISKSHHWASYSCIQQRY-TYLRPKpgadfgVQISANDELLNYCQTHDDFSLLAYSpLLNGSYT-----R 237
Cdd:cd19160 156 WSAMEIMEAYSVARQFNLIPPVCEQAEYhLFQREK------VEMQLPELYHKIGVGSVTWSPLACG-LITGKYDgrvpdT 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133861166 238 SDAP------LQKQYESEDA---QARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNI 305
Cdd:cd19160 229 CRAAvkgyqwLKEKVQSEEGkkqQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQV 305
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-304 |
1.37e-28 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 111.11 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNFGSR---TDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsgGESELLLGQWLKdRGNREHIVLATKVGA 90
Cdd:cd19090 1 SALGLGTAGLGGVfggVDDDEAVATIRAALDLGINYIDTAPAY---------GDSEERLGLALA-ELPREPLVLSTKVGR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 91 QPTiPGGGFesmeglSRKAIEQAIDGSLRRLGTDYVDLYYAH-IDDVNTPLE----ETMEAFDRLVRAGKVRA--LGCSN 163
Cdd:cd19090 71 LPE-DTADY------SADRVRRSVEESLERLGRDRIDLLMIHdPERVPWVDIlapgGALEALLELKEEGLIKHigLGGGP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 164 HHTWR--VEKARniskshhwasYSCI--QQRYTYLRPkpgadfgvqiSANDELLNYCQTHdDFSLLAYSPLLNGSYTRSD 239
Cdd:cd19090 144 PDLLRraIETGD----------FDVVltANRYTLLDQ----------SAADELLPAAARH-GVGVINASPLGMGLLAGRP 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133861166 240 APLQK---QYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLN 304
Cdd:cd19090 203 PERVRytyRWLSPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-317 |
2.74e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 111.20 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGCLNFGS---RTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcSGGESELLLGQWLKdrGNREHI 82
Cdd:cd19104 5 FGRTGLKVSELTFGGGGIGGlmgRTTREEQIAAVRRALDLGINFFDTAPSY-------GDGKSEENLGRALK--GLPAGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 83 VLATKVGaqptIPGGGFESMEGlsrkAIEQAIDGSLRRLGTDYVDLYYAH----------------IDDVNTPlEETMEA 146
Cdd:cd19104 76 YITTKVR----LDPDDLGDIGG----QIERSVEKSLKRLKRDSVDLLQLHnrigderdkpvggtlsTTDVLGL-GGVADA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 147 FDRLVRAGKVRALGCSnhhTWRVEKA-RNISKSHHWASyscIQQRYTYLRPKPGADFGVQISAND--ELLNYCQTHdDFS 223
Cdd:cd19104 147 FERLRSEGKIRFIGIT---GLGNPPAiRELLDSGKFDA---VQVYYNLLNPSAAEARPRGWSAQDygGIIDAAAEH-GVG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 224 LLAYSPLLNGSYTRS-DAPLQKQYESEDAQA----RLRVLSEVAQETGGTLNQIVLAWLL--QSTPTTlsIIAASKPEQL 296
Cdd:cd19104 220 VMGIRVLAAGALTTSlDRGREAPPTSDSDVAidfrRAAAFRALAREWGETLAQLAHRFALsnPGVSTV--LVGVKNREEL 297
|
330 340
....*....|....*....|..
gi 1133861166 297 QENLDSLNI-RLTQDQLHRLHT 317
Cdd:cd19104 298 EEAVAAEAAgPLPAENLARLEA 319
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-316 |
8.80e-28 |
|
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: 109.64 E-value: 8.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 9 TGIQVSALGLGCLNF---GSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwneGCSGGESEL-LLGQWLKDRG-NREHIV 83
Cdd:cd19077 1 NGKLVGPIGLGLMGLtwrPNPTPDEEAFETMKAALDAGSNLWNGGEFY-----GPPDPHANLkLLARFFRKYPeYADKVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVGAQPT--IPGGgfesmeglSRKAIEQAIDGSLRRLG-TDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALG 160
Cdd:cd19077 76 LSVKGGLDPDtlRPDG--------SPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 161 CSnhhtwrvE-KARNISKSHHWASYSCIQQRYTYlrpkpgadFGVQISANDELlnycQTHDDFS--LLAYSPL----LNG 233
Cdd:cd19077 148 LS-------EvSAETIRRAHAVHPIAAVEVEYSL--------FSREIEENGVL----ETCAELGipIIAYSPLgrglLTG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 234 SY-TRSDAP------LQKQYESEDAQARL---RVLSEVAQETGGTLNQIVLAWLL-QSTPTTLSIIAASKPEQLQENLDS 302
Cdd:cd19077 209 RIkSLADIPegdfrrHLDRFNGENFEKNLklvDALQELAEKKGCTPAQLALAWILaQSGPKIIPIPGSTTLERVEENLKA 288
|
330
....*....|....
gi 1133861166 303 LNIRLTQDQLHRLH 316
Cdd:cd19077 289 ANVELTDEELKEIN 302
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
6-305 |
1.29e-27 |
|
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: 109.48 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGCL-NFGSRTDKETSYRLLDQYVDAGGSFLDTSnnyafwnEGCSGGESELLLGQWLKDRG-NREHIV 83
Cdd:cd19142 6 LGKSGLRVSNVGLGTWsTFSTAISEEQAEEIVTLAYENGINYFDTS-------DAFTSGQAETELGRILKKKGwKRSSYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVGAQPTipgggfESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSN 163
Cdd:cd19142 79 VSTKIYWSYG------SEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 164 HHTWRVEKARNISKSHHWASYSCIQQRYTYL-RPKpgadfgVQISAnDELLNYC------------QTHDDFSLLAYSPL 230
Cdd:cd19142 153 WSPVEIMEAFSIARQFNCPTPICEQSEYHMFcREK------MELYM-PELYNKVgvglitwsplslGLDPGISEETRRLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 231 LNGSYTRSDAPLQKQY-----ESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNI 305
Cdd:cd19142 226 TKLSFKSSKYKVGSDGngiheETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQL 305
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-316 |
1.98e-27 |
|
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: 107.34 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLnfgsRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsggESELLLGQWLKDRG-NREHIVLATKV 88
Cdd:cd19140 5 GVRIPALGLGTY----PLTGEECTRAVEHALELGYRHIDTAQMY----------GNEAQVGEAIAASGvPRDELFLTTKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 89 GaqptipgggfesMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTPLEETMEAFDRLVRAGKVRALGCSNHHTWR 168
Cdd:cd19140 71 W------------PDNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 169 VEKARNISKshhwASYSCIQQRY-TYLRPKPgadfgvqisandeLLNYCQTHdDFSLLAYSPLLNGSYTRsDAplqkqye 247
Cdd:cd19140 139 LREAVELSE----APLFTNQVEYhPYLDQRK-------------LLDAAREH-GIALTAYSPLARGEVLK-DP------- 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133861166 248 sedaqarlrVLSEVAQETGGTLNQIVLAWLLQStPTTLSIIAASKPEQLQENLDSLNIRLTQDQLHRLH 316
Cdd:cd19140 193 ---------VLQEIGRKHGKTPAQVALRWLLQQ-EGVAAIPKATNPERLEENLDIFDFTLSDEEMARIA 251
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-303 |
5.14e-27 |
|
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: 107.06 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNFG--SRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRgNREHIVLATKVGA- 90
Cdd:cd19162 1 PRLGLGAASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYG-------LGLSERRLGAALARH-PRAEYVVSTKVGRl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 91 ---QPTIPGGGFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHI--DDVNTPLEETMEAFDRLVRAGKVRALGCSnhh 165
Cdd:cd19162 73 lepGAAGRPAGADRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDpdRHLLQALTDAFPALEELRAEGVVGAIGVG--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 166 TWRVEKARNISKSHHWASYsCIQQRYTYLRPkpgadfgvqiSANDELLNYCQtHDDFSLLAYSPlLNGSYTRSDAPLQKQ 245
Cdd:cd19162 150 VTDWAALLRAARRADVDVV-MVAGRYTLLDR----------RAATELLPLCA-AKGVAVVAAGV-FNSGILATDDPAGDR 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133861166 246 YE----SEDAQARLRVLSEVAQETGGTLNQIVLAWLLQStPTTLSIIA-ASKPEQLQENLDSL 303
Cdd:cd19162 217 YDyrpaTPEVLARARRLAAVCRRYGVPLPAAALQFPLRH-PAVASVVVgAASPAELRDNLALL 278
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-319 |
2.03e-24 |
|
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: 100.49 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 23 FGSRTDKETSYRLLDQYVDAGGSFLDTSNNYAFwnegcsgGESELLLGQWLKDRgNREHIVLATKVGAQptipgggfesM 102
Cdd:cd19103 25 FGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGM-------GASEKILGEFLKRY-PREDYIISTKFTPQ----------I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 103 EGLSRKAIEQAIDGSLRRLGTDYVDLYYAHI-DDV--NTPleetmEAFDrLVRAGKVRALGCSNHHTWRVEKARNI-SKS 178
Cdd:cd19103 87 AGQSADPVADMLEGSLARLGTDYIDIYWIHNpADVerWTP-----ELIP-LLKSGKVKHVGVSNHNLAEIKRANEIlAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 179 HhwASYSCIQQRYTYLRpkpgadfgvQISANDELLNYCQTHdDFSLLAYSPL----LNGSYTRSDAPLQKQYESEDAQAR 254
Cdd:cd19103 161 G--VSLSAVQNHYSLLY---------RSSEEAGILDYCKEN-GITFFAYMVLeqgaLSGKYDTKHPLPEGSGRAETYNPL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133861166 255 LR-------VLSEVAQETGGTLNQIVLAWLLqsTPTTLSIIAASKPEQLQENLDSLNIRLTQDQLHRLHTAG 319
Cdd:cd19103 229 LPqleeltaVMAEIGAKHGASIAQVAIAWAI--AKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQLA 298
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-304 |
6.13e-24 |
|
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: 98.02 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNF----GSRTDKETSYRLLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRGnREHIVLATKvg 89
Cdd:cd19096 1 SVLGFGTMRLpesdDDSIDEEKAIEMIRYAIDAGINYFDTAYGYG-------GGKSEEILGEALKEGP-REKFYLATK-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 90 aqptIPGGGFESMEglsrkAIEQAIDGSLRRLGTDYVDLYYAHidDVNTP-LEETM------EAFDRLVRAGKVRALGCS 162
Cdd:cd19096 71 ----LPPWSVKSAE-----DFRRILEESLKRLGVDYIDFYLLH--GLNSPeWLEKArkggllEFLEKAKKEGLIRHIGFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 163 NHhtwrvEKARNISK---SHHWasySCIQQRYTYLRPKPGadfgvqisANDELLNYCQTHdDFSLLAYSPLLNGsytrsd 239
Cdd:cd19096 140 FH-----DSPELLKEildSYDF---DFVQLQYNYLDQENQ--------AGRPGIEYAAKK-GMGVIIMEPLKGG------ 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133861166 240 aplQKQYESEDAQARLRvlsevaqETGGTLNQIVLAWLLqSTP--TTLSiIAASKPEQLQENLDSLN 304
Cdd:cd19096 197 ---GLANNPPEALAILC-------GAPLSPAEWALRFLL-SHPevTTVL-SGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
41-319 |
4.41e-23 |
|
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: 96.15 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 41 DAGGSFLDTSNNYafwnegcsggESELLLGQWLKDRG-NREHIVLATKVGaqptiPGGgfesmeglsrKAIEQAIDGSLR 119
Cdd:cd19120 36 KAGFRHIDTAEMY----------GNEKEVGEALKESGvPREDLFITTKVS-----PGI----------KDPREALRKSLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 120 RLGTDYVDLYYAH----IDDVNTPLEETMEAFDRLVRAGKVRALGCSNhhtWRVEKarniskshhwasyscIQQRYTYLR 195
Cdd:cd19120 91 KLGVDYVDLYLIHspffAKEGGPTLAEAWAELEALKDAGLVRSIGVSN---FRIED---------------LEELLDTAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 196 PKPGADfgvQISAN-------DELLNYCQTHdDFSLLAYSPLLngSYTRS-DAPLQKqyesedaqarlrVLSEVAQETGG 267
Cdd:cd19120 153 IKPAVN---QIEFHpylypqqPALLEYCREH-GIVVSAYSPLS--PLTRDaGGPLDP------------VLEKIAEKYGV 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1133861166 268 TLNQIVLAWLLQS--TPTTLSiiaaSKPEQLQENLDSLNIRLTQDQLHRLHTAG 319
Cdd:cd19120 215 TPAQVLLRWALQKgiVVVTTS----SKEERMKEYLEAFDFELTEEEVEEIDKAG 264
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-301 |
6.50e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 96.62 E-value: 6.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 12 QVSALGLGCLNFGSRTDKETSYR-LLDQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRGN-----REHIVLA 85
Cdd:cd19099 2 TLSSLGLGTYRGDSDDETDEEYReALKAALDSGINVIDTAINYR-------GGRSERLIGKALRELIEkggikRDEVVIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 86 TKVG------AQPTIPGGGFESMEG---------------LSRKAIEQAIDGSLRRLGTDYVDLYYAHI----------D 134
Cdd:cd19099 75 TKAGyipgdgDEPLRPLKYLEEKLGrglidvadsaglrhcISPAYLEDQIERSLKRLGLDTIDLYLLHNpeeqllelgeE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 135 DVNTPLEETMEAFDRLVRAGKVRALGCSnhhTWRVEKARNISKSHHwASYSCIQQRYTYLRPKPGADFgVQISAN---DE 211
Cdd:cd19099 155 EFYDRLEEAFEALEEAVAEGKIRYYGIS---TWDGFRAPPALPGHL-SLEKLVAAAEEVGGDNHHFKV-IQLPLNllePE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 212 LLNYCQTHDD--FSLL--AYSpllNGSYTRSDAPLQKQYESEdaqaRLRVLSEVAQETGGTLNQIVLAWLLqSTP-TTLS 286
Cdd:cd19099 230 ALTEKNTVKGeaLSLLeaAKE---LGLGVIASRPLNQGQLLG----ELRLADLLALPGGATLAQRALQFAR-STPgVDSA 301
|
330
....*....|....*
gi 1133861166 287 IIAASKPEQLQENLD 301
Cdd:cd19099 302 LVGMRRPEHVDENLA 316
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-317 |
9.12e-21 |
|
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: 89.64 E-value: 9.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLNFgsrtDKETSYRLLDQYVDAGGSFLDTSNNYAfwNEGCsggesellLGQWLKDRG-NREHIVLAT 86
Cdd:cd19132 2 NDGTQIPAIGFGTYPL----KGDEGVEAVVAALQAGYRLLDTAFNYE--NEGA--------VGEAVRRSGvPREELFVTT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 87 KvgaqptIPGG--GFEsmeglsrkAIEQAIDGSLRRLGTDYVDLYYAHiddvnTPLE------ETMEAFDRLVRAGKVRA 158
Cdd:cd19132 68 K------LPGRhhGYE--------EALRTIEESLYRLGLDYVDLYLIH-----WPNPsrdlyvEAWQALIEAREEGLVRS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 159 LGCSN---HHTWRVEKARNISKShhwasyscIQQrytylrpkpgadfgVQISAN---DELLNYCQTHDDFSlLAYSPLLN 232
Cdd:cd19132 129 IGVSNflpEHLDRLIDETGVTPA--------VNQ--------------IELHPYfpqAEQRAYHREHGIVT-QSWSPLGR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 233 GSYTRSDAPLQkqyesedaqarlrvlsEVAQETGGTLNQIVLAWLLQStpTTLSIIAASKPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19132 186 GSGLLDEPVIK----------------AIAEKHGKTPAQVVLRWHVQL--GVVPIPKSANPERQRENLAIFDFELSDEDM 247
|
....*
gi 1133861166 313 HRLHT 317
Cdd:cd19132 248 AAIAA 252
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-315 |
2.99e-20 |
|
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: 88.22 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGClnFGSRTDKETSyRLLDQYVDAGGSFLDTSNNYafwnegcsggESELLLGQWLKDRG-NREHIVLAT 86
Cdd:cd19157 5 NNGVKMPWLGLGV--FKVEEGSEVV-NAVKTALKNGYRSIDTAAIY----------GNEEGVGKGIKESGiPREELFITS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 87 KV-----GAQPTIpgggfesmeglsrkaieQAIDGSLRRLGTDYVDLYYAHIdDVNTPLEETMEAFDRLVRAGKVRALGC 161
Cdd:cd19157 72 KVwnadqGYDSTL-----------------KAFEASLERLGLDYLDLYLIHW-PVKGKYKETWKALEKLYKDGRVRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 162 SNHHTwrvekarnisksHHwasyscIQQRYTYLRPKPGADfgvQIS-----ANDELLNYCQTHdDFSLLAYSPLLNGsyt 236
Cdd:cd19157 134 SNFQV------------HH------LEDLLADAEIVPMVN---QVEfhprlTQKELRDYCKKQ-GIQLEAWSPLMQG--- 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133861166 237 rsdaplqKQYESEdaqarlrVLSEVAQETGGTLNQIVLAWLLQSTPTTlsIIAASKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19157 189 -------QLLDNP-------VLKEIAEKYNKSVAQVILRWDLQNGVVT--IPKSIKEHRIIENADVFDFELSQEDMDKI 251
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-317 |
8.04e-20 |
|
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: 87.55 E-value: 8.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNfgSRTDKETSyrLLDQYVDAGGSFLDTSNNYAfwNEGCSGGeselLLGQWLKD-RGNREHIVLATKV 88
Cdd:cd19111 1 GFPMPVIGLGTYQ--SPPEEVRA--AVDYALFVGYRHIDTALSYQ--NEKAIGE----ALKWWLKNgKLKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 89 gaqPTIpgggfesmeGLSRKAIEQAIDGSLRRLGTDYVDLYYAH-------------IDDVNTPLEETMEAFDRLVRAGK 155
Cdd:cd19111 71 ---PPV---------YLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 156 VRALGCSNHHTWRVEKARNISKSH-HWASYSC---IQQRytylrpkpgadfgvqisandELLNYCQTHdDFSLLAYSPLl 231
Cdd:cd19111 139 VKSIGLSNFNPRQINKILAYAKVKpSNLQLEChayLQQR--------------------ELRKFCNKK-NIVVTAYAPL- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 232 nGSYTRsdAPLQKQYESEDAQARLRVLSeVAQETGGTLNQIVLAWLLQStpTTLSIIAASKPEQLQENLDSLNIRLTQDQ 311
Cdd:cd19111 197 -GSPGR--ANQSLWPDQPDLLEDPTVLA-IAKELDKTPAQVLLRFVLQR--GTGVLPKSTNKERIEENFEVFDFELTEEH 270
|
....*.
gi 1133861166 312 LHRLHT 317
Cdd:cd19111 271 FKKLKT 276
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-315 |
1.66e-19 |
|
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: 86.40 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLnfgsRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsGGESELllGQWLKDRG-NREHIVLAT 86
Cdd:cd19117 9 NTGAEIPAVGLGTW----QSKPNEVAKAVEAALKAGYRHIDTAAIY--------GNEEEV--GQGIKDSGvPREEIFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 87 KVgaqptipgggfesmEGLSRKAIEQAIDGSLRRLGTDYVDLYYAH---------------------IDDVNTPLEETME 145
Cdd:cd19117 75 KL--------------WCTWHRRVEEALDQSLKKLGLDYVDLYLMHwpvpldpdgndflfkkddgtkDHEPDWDFIKTWE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 146 AFDRLVRAGKVRALGCSNHHTWRVEKarniskshhwasysCIQQRYTYLRPkpgADFGVQISAN---DELLNYCQThDDF 222
Cdd:cd19117 141 LMQKLPATGKVKAIGVSNFSIKNLEK--------------LLASPSAKIVP---AVNQIELHPLlpqPKLVDFCKS-KGI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 223 SLLAYSPLlnGSytrSDAPLQKqyesedaqarLRVLSEVAQETGGTLNQIVLAWLLQStptTLSIIAAS-KPEQLQENLD 301
Cdd:cd19117 203 HATAYSPL--GS---TNAPLLK----------EPVIIKIAKKHGKTPAQVIISWGLQR---GYSVLPKSvTPSRIESNFK 264
|
330
....*....|....
gi 1133861166 302 SlnIRLTQDQLHRL 315
Cdd:cd19117 265 L--FTLSDEEFKEI 276
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-315 |
1.90e-19 |
|
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: 86.88 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 24 GSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsgGESELLLGQWLKDRGNREH----IVLATKVgaqptIPGGGF 99
Cdd:cd19101 17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIY---------GPAEELIGEFRKRLRRERDaaddVQIHTKW-----VPDPGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 100 ESMeglSRKAIEQAIDGSLRRLGTDYVDLYYAHIDDVNTP-LEETMEAFDRLVRAGKVRALGCSNHHTWRVEKARN--IS 176
Cdd:cd19101 83 LTM---TRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDagVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 177 KSHHWASYSCIQQRytylrpkpgadfgvqisANDELLNYCQTHdDFSLLAYSPLLNG----------------SYTRSda 240
Cdd:cd19101 160 IVSNQVQYSLLDRR-----------------PENGMAALCEDH-GIKLLAYGTLAGGllsekylgvpeptgpaLETRS-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 241 pLQKQYESEDA-------QARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRLTQDQLH 313
Cdd:cd19101 220 -LQKYKLMIDEwggwdlfQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRA 298
|
..
gi 1133861166 314 RL 315
Cdd:cd19101 299 AI 300
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-305 |
2.39e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 82.96 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNFGS---------RTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsgGESELLLGQWLKdrgNREHIVL 84
Cdd:cd19097 1 SKLALGTAQFGLdygianksgKPSEKEAKKILEYALKAGINTLDTAPAY---------GDSEKVLGKFLK---RLDKFKI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 85 ATKVgaqPTIPGGGFESmeglsRKAIEQAIDGSLRRLGTDYVDLYYAH-IDDVNTPLEETMEAFDRLVRAGKVRALGCSN 163
Cdd:cd19097 69 ITKL---PPLKEDKKED-----EAAIEASVEASLKRLKVDSLDGLLLHnPDDLLKHGGKLVEALLELKKEGLIRKIGVSV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 164 HHTWRVEKARNiskshhwasysciqqrytylRPKPGAdfgVQISANdeLLN-YCQTHDDFSLL--------AYSPLLNGS 234
Cdd:cd19097 141 YSPEELEKALE--------------------SFKIDI---IQLPFN--ILDqRFLKSGLLAKLkkkgieihARSVFLQGL 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133861166 235 YTRSDAPLQKQyeSEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNI 305
Cdd:cd19097 196 LLMEPDKLPAK--FAPAKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKK 264
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-315 |
3.27e-18 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 82.40 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 13 VSALGLGclnfgsrtdketSYRLLDQYV--------DAGGSFLDTSNNYafwnegcsggESELLLGQWLKDRG-NREHIV 83
Cdd:cd19139 1 IPAFGLG------------TFRLKDDVVidsvrtalELGYRHIDTAQIY----------DNEAAVGQAIAESGvPRDELF 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVGAqptipgggfesmEGLSRKAIEQAIDGSLRRLGTDYVDLYYAH---IDDVnTPLEETMEAFDRLVRAGKVRALG 160
Cdd:cd19139 59 ITTKIWI------------DNLSKDKLLPSLEESLEKLRTDYVDLTLIHwpsPNDE-VPVEEYIGALAEAKEQGLTRHIG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 161 CSNHHTWRVEKARNISKSHHWASYSCiqQRYTYLrpkpgadfgvqisANDELLNYCQTHDdFSLLAYSPLLNGSYTRSDa 240
Cdd:cd19139 126 VSNFTIALLDEAIAVVGAGAIATNQI--ELSPYL-------------QNRKLVAHCKQHG-IHVTSYMTLAYGKVLDDP- 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133861166 241 plqkqyesedaqarlrVLSEVAQETGGTLNQIVLAWLLQstpTTLSIIAAS-KPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19139 189 ----------------VLAAIAERHGATPAQIALAWAMA---RGYAVIPSStKREHLRSNLLALDLTLDADDMAAI 245
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-315 |
4.56e-18 |
|
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: 82.85 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGC-------LNFGSRTDKETSYRLLDqyvdaggsfldTSNNYafwnegcsggESELLLGQWLKD----- 75
Cdd:cd19154 7 SNGVKMPLIGLGTwqskgaeGITAVRTALKAGYRLID-----------TAFLY----------QNEEAIGEALAElleeg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 76 RGNREHIVLATKVGAQPTIPGggfesmeglsrkAIEQAIDGSLRRLGTDYVDLYYAHI------------DDVN------ 137
Cdd:cd19154 66 VVKREDLFITTKLWTHEHAPE------------DVEEALRESLKKLQLEYVDLYLIHApaafkddegesgTMENgmsihd 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 138 -TPLEETMEAFDRLVRAGKVRALGCSNHHTWRVEKARNISKSH-HWASYSCiqqrYTYLRPKpgadfgvqisandELLNY 215
Cdd:cd19154 134 aVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARVKpHNNQVEC----HLYFPQK-------------ELVEF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 216 CQTHdDFSLLAYSPLlnGSYTRSDAPLQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQStptTLSIIAAS-KPE 294
Cdd:cd19154 197 CKKH-NISVTSYATL--GSPGRANFTKSTGVSPAPNLLQDPIVKAIAEKHGKTPAQVLLRYLLQR---GIAVIPKSaTPS 270
|
330 340
....*....|....*....|.
gi 1133861166 295 QLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19154 271 RIKENFNIFDFSLSEEDMATL 291
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-305 |
1.41e-17 |
|
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: 81.60 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNFG---SRTDKETSYRLLDQYVDAGGSFLDTSNNYAFwnegcsgGESELLLGQWLKDRGnREHIVLATKVG- 89
Cdd:cd19161 1 SELGLGTAGLGnlyTAVSNADADATLDAAWDSGIRYFDTAPMYGH-------GLAEHRLGDFLREKP-RDEFVLSTKVGr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 90 ----AQP--TIPGGGFesMEGL--------SRKAIEQAIDGSLRRLGTDYVDLYYAH-ID-----DVNTPLE--ETME-- 145
Cdd:cd19161 73 llkpAREgsVPDPNGF--VDPLpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHdIGvythgDRKERHHfaQLMSgg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 146 --AFDRLVRAGKVRALGCSnhhtwrVEKARNISKSHHWASYSC--IQQRYTYLrpkpgadfgvQISANDELLNYCQTHdD 221
Cdd:cd19161 151 fkALEELKKAGVIKAFGLG------VNEVQICLEALDEADLDCflLAGRYSLL----------DQSAEEEFLPRCEQR-G 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 222 FSLLAYSPLLNGSYTRSDAPLQK-QYES--EDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQE 298
Cdd:cd19161 214 TSLVIGGVFNSGILATGTKSGAKfNYGDapAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQ 293
|
....*..
gi 1133861166 299 NLDSLNI 305
Cdd:cd19161 294 NVEAFQT 300
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-312 |
1.59e-17 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 80.56 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGClnFGSRTDKETSyRLLDQYVDAGGSFLDTSnnyAFWNegcsggeSELLLGQWLKDRG-NREHIVLAT 86
Cdd:cd19126 4 NNGTRMPWLGLGV--FQTPDGDETE-RAVQTALENGYRSIDTA---AIYK-------NEEGVGEAIRESGvPREELFVTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 87 KVgaqptipgggFESMEGLSRkaIEQAIDGSLRRLGTDYVDLYYAHIdDVNTPLEETMEAFDRLVRAGKVRALGCSNHHT 166
Cdd:cd19126 71 KL----------WNDDQRARR--TEDAFQESLDRLGLDYVDLYLIHW-PGKDKFIDTWKALEKLYASGKVKAIGVSNFQE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 167 wrvekarnisksHHwasyscIQQRYTYLRPKPGADfgvQIS-----ANDELLNYCQTHdDFSLLAYSPLLNGSYTRSdap 241
Cdd:cd19126 138 ------------HH------LEELLAHADVVPAVN---QVEfhpylTQKELRGYCKSK-GIVVEAWSPLGQGGLLSN--- 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133861166 242 lqkqyesedaqarlRVLSEVAQETGGTLNQIVLAWLLQSTPTTlsIIAASKPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19126 193 --------------PVLAAIGEKYGKSAAQVVLRWDIQHGVVT--IPKSVHASRIKENADIFDFELSEDDM 247
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-315 |
2.15e-17 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 80.53 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGClnFGSRTDKETS---------YRLLDqyvdaggsfldTSNNYafwnegcsGGESELllGQWLKDRG- 77
Cdd:cd19127 4 NNGVEMPALGLGV--FQTPPEETADavataladgYRLID-----------TAAAY--------GNEREV--GEGIRRSGv 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 78 NREHIVLATKVgaqpTIPGGGFEsmeglsrkAIEQAIDGSLRRLGTDYVDLYYAHiDDVNTPLEETMEAF---DRLVRAG 154
Cdd:cd19127 61 DRSDIFVTTKL----WISDYGYD--------KALRGFDASLRRLGLDYVDLYLLH-WPVPNDFDRTIQAYkalEKLLAEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 155 KVRALGCSNHHTWRVEkaRNISKShhwASYSCIQQryTYLRPkpgadfgvqISANDELLNYCQTHdDFSLLAYSPLlnGS 234
Cdd:cd19127 128 RVRAIGVSNFTPEHLE--RLIDAT---TVVPAVNQ--VELHP---------YFSQKDLRAFHRRL-GIVTQAWSPI--GG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 235 YTRsdaplqkqYESEDAQARLRVLS-----EVAQETGGTLNQIVLAWLLQStptTLSIIAAS-KPEQLQENLDSLNIRLT 308
Cdd:cd19127 189 VMR--------YGASGPTGPGDVLQdptitGLAEKYGKTPAQIVLRWHLQN---GVSAIPKSvHPERIAENIDIFDFALS 257
|
....*..
gi 1133861166 309 QDQLHRL 315
Cdd:cd19127 258 AEDMAAI 264
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-317 |
2.54e-17 |
|
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: 80.99 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLnfgsRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsggESELLLGQWLK---DRG--NREHI 82
Cdd:cd19112 6 NSGHKMPVIGLGVW----RMEPGEIKELILNAIKIGYRHFDCAADY----------KNEKEVGEALAeafKTGlvKREDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 83 VLATKVgaqptipgggFESMEGLSRKAIEQaidgSLRRLGTDYVDLYYAHI-----------------------DDVNTP 139
Cdd:cd19112 72 FITTKL----------WNSDHGHVIEACKD----SLKKLQLDYLDLYLVHFpvatkhtgvgttgsalgedgvldIDVTIS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 140 LEETMEAFDRLVRAGKVRALGCSNHhtwrvekarNISKSHHWASYSCIqqrytylrpKPGADfgvQISAN-----DELLN 214
Cdd:cd19112 138 LETTWHAMEKLVSAGLVRSIGISNY---------DIFLTRDCLAYSKI---------KPAVN---QIETHpyfqrDSLVK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 215 YCQTHdDFSLLAYSPL----LNGSYTRSDAPLQKQyesedaqarlrVLSEVAQETGGTLNQIVLAWLLQStpTTLSIIAA 290
Cdd:cd19112 197 FCQKH-GISVTAHTPLggaaANAEWFGSVSPLDDP-----------VLKDLAKKYGKSAAQIVLRWGIQR--NTAVIPKS 262
|
330 340
....*....|....*....|....*..
gi 1133861166 291 SKPEQLQENLDSLNIRLTQDQLHRLHT 317
Cdd:cd19112 263 SKPERLKENIDVFDFQLSKEDMKLIKS 289
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-305 |
3.53e-17 |
|
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: 80.36 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGclNFGSRTDKETSYRLLDQYVDAGGSFLDTSnnYAFWNEGCSGGEsellLGQWLKDRGN--REHIVLA 85
Cdd:cd19122 4 NNGVKIPAVGFG--TFANEGAKGETYAAVTKALDVGYRHLDCA--WFYLNEDEVGDA----VRDFLKENPSvkREDLFIC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 86 TKVGAQPTIPgggfesmeglsrKAIEQAIDGSLRRLGTDYVDLYYAHI------DDVNTPL-----------------EE 142
Cdd:cd19122 76 TKVWNHLHEP------------EDVKWSIDNSLKNLKLDYIDLFLVHWpiaaekNDQRSPKlgpdgkyvilkdltenpEP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 143 TMEAFDRLVRAGKVRALGCSNhhtWRVEKARNISKshhwasysciqqrytYLRPKPGADfgvQIS-----ANDELLNYCQ 217
Cdd:cd19122 144 TWRAMEEIYESGKAKAIGVSN---WTIPGLKKLLS---------------FAKVKPHVN---QIEihpflPNEELVDYCF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 218 THDDFSlLAYSPLlnGSytRSDAPLQKQYESEDaqarlRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSiiAASKPEQLQ 297
Cdd:cd19122 203 SNDILP-EAYSPL--GS--QNQVPSTGERVSEN-----PTLNEVAEKGGYSLAQVLIAWGLRRGYVVLP--KSSTPSRIE 270
|
....*...
gi 1133861166 298 ENLDSLNI 305
Cdd:cd19122 271 SNFKSIEL 278
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
28-316 |
7.19e-17 |
|
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: 78.83 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 28 DKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsggESELLLGQWLKDRG-----NREHIVLATKVGaqptiPgggfesm 102
Cdd:cd19136 13 GEEEVRQAVDAALKAGYRLIDTASVY----------RNEADIGKALRDLLpkyglSREDIFITSKLA-----P------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 103 EGLSRKAIEQAIDGSLRRLGTDYVDLYYAH---------IDDVNTPLE-ETMEAFDRLVRAGKVRALGCSN---HH---- 165
Cdd:cd19136 71 KDQGYEKARAACLGSLERLGTDYLDLYLIHwpgvqglkpSDPRNAELRrESWRALEDLYKEGKLRAIGVSNytvRHleel 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 166 --TWRVEKARNISKSHHWasysCIQQrytylrpkpgadfgvqisandELLNYCQTHDDFsLLAYSPLLNGSYTRSDAPlq 243
Cdd:cd19136 151 lkYCEVPPAVNQVEFHPH----LVQK---------------------ELLKFCKDHGIH-LQAYSSLGSGDLRLLEDP-- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133861166 244 kqyesedaqarlRVLsEVAQETGGTLNQIVLAWLLQstpTTLSIIA-ASKPEQLQENLDSLNIRLTQDQLHRLH 316
Cdd:cd19136 203 ------------TVL-AIAKKYGRTPAQVLLRWALQ---QGIGVIPkSTNPERIAENIKVFDFELSEEDMAELN 260
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-312 |
1.08e-16 |
|
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: 78.86 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLNFGsrtDKETSYRLLDQYVDAGGSFLDTSnnYAFWNEGcsggeselLLGQWLKD---RGN--REHI 82
Cdd:cd19116 6 NDGNEIPAIALGTWKLK---DDEGVRQAVKHAIEAGYRHIDTA--YLYGNEA--------EVGEAIREkiaEGVvkREDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 83 VLATKVGaqptipgGGFESmeglsRKAIEQAIDGSLRRLGTDYVDLYYAHI----------------DDVNTPLEETMEA 146
Cdd:cd19116 73 FITTKLW-------NSYHE-----REQVEPALRESLKRLGLDYVDLYLIHWpvafkenndsesngdgSLSDIDYLETWRG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 147 FDRLVRAGKVRALGCSNHhtwrvekarNISKshhwasyscIQQRYTYLRPKPGADfgvQISAN-----DELLNYCQTHdD 221
Cdd:cd19116 141 MEDLVKLGLTRSIGVSNF---------NSEQ---------INRLLSNCNIKPAVN---QIEVHptltqEKLVAYCQSN-G 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 222 FSLLAYSPLlnGSYTRSDAPLQKQYESEdaqarlRVLSEVAQETGGTLNQIVLAWLLQStpTTLSIIAASKPEQLQENLD 301
Cdd:cd19116 199 IVVMAYSPF--GRLVPRGQTNPPPRLDD------PTLVAIAKKYGKTTAQIVLRYLIDR--GVVPIPKSSNKKRIKENID 268
|
330
....*....|.
gi 1133861166 302 SLNIRLTQDQL 312
Cdd:cd19116 269 IFDFQLTPEEV 279
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-310 |
1.17e-16 |
|
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: 78.00 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLNFgsrTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsggESELLLGQWLKDRG-NREHIVLAT 86
Cdd:cd19133 4 NNGVEMPILGFGVFQI---PDPEECERAVLEAIKAGYRLIDTAAAY----------GNEEAVGRAIKKSGiPREELFITT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 87 KVgaqpTIPGGGFESmeglsrkaIEQAIDGSLRRLGTDYVDLYYAH--IDDVntplEETMEAFDRLVRAGKVRALGCSNH 164
Cdd:cd19133 71 KL----WIQDAGYEK--------AKKAFERSLKRLGLDYLDLYLIHqpFGDV----YGAWRAMEELYKEGKIRAIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 165 HTWRVekaRNISKSHHwasysciqqrytylrPKPGADfgvQIsandELLNYCQTHDDFSLLAYspllNGSYTRSDAPLQk 244
Cdd:cd19133 135 YPDRL---VDLILHNE---------------VKPAVN---QI----ETHPFNQQIEAVEFLKK----YGVQIEAWGPFA- 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133861166 245 qyESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQStpttlSIIAASK---PEQLQENLDSLNIRLTQD 310
Cdd:cd19133 185 --EGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQR-----GIVVIPKsvrPERIAENFDIFDFELSDE 246
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
1-319 |
1.97e-15 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 75.01 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLGNT----GIQVSALGLGCLN------FGSRTDKETSYRLLDQYVDAGGSFLDTSNNYA--FWNEgcsggeselL 68
Cdd:PRK10376 1 MSTIMSSGTftlgGRSVNRLGYGAMQlagpgvFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGphVTNQ---------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 69 LGQWLKDRGNREHIVlaTKVGAQPTIPGGGFESmegLSRKAIEQAIDGSLRRLGTDYVDLYYAHID-DVNTP----LEET 143
Cdd:PRK10376 72 IREALHPYPDDLTIV--TKVGARRGEDGSWLPA---FSPAELRRAVHDNLRNLGLDVLDVVNLRLMgDGHGPaegsIEEP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 144 MEAFDRLVRAGKVRALGCSNHHTWRVEKARNIskshhwASYSCIQQRYtylrpkpgadfgvqisandellNYCQTHDDFS 223
Cdd:PRK10376 147 LTVLAELQRQGLVRHIGLSNVTPTQVAEARKI------AEIVCVQNHY----------------------NLAHRADDAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 224 L-------LAYSPLLN-GSYTrsdaPLQKQyesedaqarlrVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQ 295
Cdd:PRK10376 199 IdalardgIAYVPFFPlGGFT----PLQSS-----------TLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAH 263
|
330 340
....*....|....*....|....
gi 1133861166 296 LQENLDSLNIRLTQDQLHRLHTAG 319
Cdd:PRK10376 264 LRENLAAAELVLSEEVLAELDGIA 287
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-301 |
2.30e-15 |
|
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: 75.19 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCL-NFGSRTDKETSYRLldqyvDAGGSFLDTSNNYAfwNEGCSGGESELLLgqwlkDRGN--REHIVL 84
Cdd:cd19129 1 NGSGAIPALGFGTLiPDPSATRNAVKAAL-----EAGFRHFDCAERYR--NEAEVGEAMQEVF-----KAGKirREDLFV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 85 ATKVGAQPTIPgggfesmeglsrKAIEQAIDGSLRRLGTDYVDLYYAH--------------------IDDVNTPLEETM 144
Cdd:cd19129 69 TTKLWNTNHRP------------ERVKPAFEASLKRLQLDYLDLYLIHtpfafqpgdeqdprdangnvIYDDGVTLLDTW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 145 EAFDRLVRAGKVRALGCSNhhtWRVEKARNIskshhwasysciqqrYTYLRPKPGAdfgVQISAND-----ELLNYCQTH 219
Cdd:cd19129 137 RAMERLVDEGRCKAIGLSD---VSLEKLREI---------------FEAARIKPAV---VQVESHPylpewELLDFCKNH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 220 dDFSLLAYSPLLNGSYTRsdaPLqkqyesEDAqarlrVLSEVAQETGGTLNQIVLAWLLQSTPTTLSiiAASKPEQLQEN 299
Cdd:cd19129 196 -GIVLQAFAPLGHGMEPK---LL------EDP-----VITAIARRVNKTPAQVLLAWAIQRGTALLT--TSKTPSRIREN 258
|
..
gi 1133861166 300 LD 301
Cdd:cd19129 259 FD 260
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
10-317 |
2.65e-15 |
|
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: 74.28 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNFGSRTDKETSYRLldqyVDAGGSFLDTSNNYafwneGCsggesELLLGQWLKDRG-NREHIVLATKV 88
Cdd:cd19135 10 GVEMPILGLGTSHSGGYSHEAVVYAL----KECGYRHIDTAKRY-----GC-----EELLGKAIKESGvPREDLFLTTKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 89 -----GAQPTIpgggfesmeglsrkaieQAIDGSLRRLGTDYVDLYYAH-------IDDVNTPLEETMEAFDRLVRAGKV 156
Cdd:cd19135 76 wpsdyGYESTK-----------------QAFEASLKRLGVDYLDLYLLHwpdcpssGKNVKETRAETWRALEELYDEGLC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 157 RALGCSN---HH------TWRVEKARNISKSHhwasysciqqryTYLRPKpgadfgvqisandELLNYCQTHdDFSLLAY 227
Cdd:cd19135 139 RAIGVSNfliEHleqlleDCSVVPHVNQVEFH------------PFQNPV-------------ELIEYCRDN-NIVFEGY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 228 SPLLNGSytrsdaPLQKQyesedaqarlrVLSEVAQETGGTLNQIVLAWLLQSTPTTlsIIAASKPEQLQENLDSLNIRL 307
Cdd:cd19135 193 CPLAKGK------ALEEP-----------TVTELAKKYQKTPAQILIRWSIQNGVVT--IPKSTKEERIKENCQVFDFSL 253
|
330
....*....|
gi 1133861166 308 TQDQLHRLHT 317
Cdd:cd19135 254 SEEDMATLDS 263
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
6-300 |
2.67e-15 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 75.20 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGCLNFG------SRTDKETSYRlldQYVDAGGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRG-N 78
Cdd:PLN02587 4 LGSTGLKVSSVGFGASPLGsvfgpvSEEDAIASVR---EAFRLGINFFDTSPYYG-------GTLSEKVLGKALKALGiP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 79 REHIVLATKVGAQptipGGGFEsmegLSRKAIEQAIDGSLRRLGTDYVDLYYAH---IDDVNTPLEETMEAFDRLVRAGK 155
Cdd:PLN02587 74 REKYVVSTKCGRY----GEGFD----FSAERVTKSVDESLARLQLDYVDILHCHdieFGSLDQIVNETIPALQKLKESGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 156 VRALGCSNHHTwrvekarniskshhwASYsciqqRYTYLRPKPGA--------DFGVQISANDELLNYCQThDDFSLLAY 227
Cdd:PLN02587 146 VRFIGITGLPL---------------AIF-----TYVLDRVPPGTvdvilsycHYSLNDSSLEDLLPYLKS-KGVGVISA 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133861166 228 SPLLNGSYTRSDAPlQKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENL 300
Cdd:PLN02587 205 SPLAMGLLTENGPP-EWHPAPPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENV 276
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-315 |
3.23e-15 |
|
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: 74.75 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 1 MQQLLLgNTGIQVSALGLGCLNFGsrtdKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsGGESELllGQWLKDRGN-- 78
Cdd:cd19123 1 MKTLPL-SNGDLIPALGLGTWKSK----PGEVGQAVKQALEAGYRHIDCAAIY--------GNEAEI--GAALAEVFKeg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 79 ---REHIVLATKVGAQPTIPgggfesmeglsrKAIEQAIDGSLRRLGTDYVDLYYAH------------------IDDVN 137
Cdd:cd19123 66 kvkREDLWITSKLWNNSHAP------------EDVLPALEKTLADLQLDYLDLYLMHwpvalkkgvgfpesgedlLSLSP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 138 TPLEETMEAFDRLVRAGKVRALGCSN---------HHTWRVEKARNISKSHHWasyscIQQRytylrpkpgadfgvqisa 208
Cdd:cd19123 134 IPLEDTWRAMEELVDKGLCRHIGVSNfsvkkledlLATARIKPAVNQVELHPY-----LQQP------------------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 209 ndELLNYCQtHDDFSLLAYSPLlnGSYTRSDAplqKQYESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQStpTTLSII 288
Cdd:cd19123 191 --ELLAFCR-DNGIHLTAYSPL--GSGDRPAA---MKAEGEPVLLEDPVINKIAEKHGASPAQVLIAWAIQR--GTVVIP 260
|
330 340
....*....|....*....|....*..
gi 1133861166 289 AASKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19123 261 KSVNPERIQQNLEAAEVELDASDMATI 287
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-315 |
1.24e-14 |
|
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: 72.40 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLnfgsRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsggESELLLGQWLKDRG-NREHIVLAT 86
Cdd:cd19131 5 NDGNTIPQLGLGVW----QVSNDEAASAVREALEVGYRSIDTAAIY----------GNEEGVGKAIRASGvPREELFITT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 87 KVgaqptipgggFESMEGlsRKAIEQAIDGSLRRLGTDYVDLYYAHIDdvnTPLE----ETMEAFDRLVRAGKVRALGCS 162
Cdd:cd19131 71 KL----------WNSDQG--YDSTLRAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 163 N---HHTWR------VEKARNISKSHHWasyscIQQRytylrpkpgadfgvqisandELLNYCQTHdDFSLLAYSPLLNG 233
Cdd:cd19131 136 NftiEHLQRlidetgVVPVVNQIELHPR-----FQQR--------------------ELRAFHAKH-GIQTESWSPLGQG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 234 SYTRSdaplqkqyesedaqarlRVLSEVAQETGGTLNQIVLAWLLQStptTLSIIAAS-KPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19131 190 GLLSD-----------------PVIGEIAEKHGKTPAQVVIRWHLQN---GLVVIPKSvTPSRIAENFDVFDFELDADDM 249
|
...
gi 1133861166 313 HRL 315
Cdd:cd19131 250 QAI 252
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
20-312 |
1.05e-13 |
|
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: 69.86 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 20 CLNFGS-RTDKETSYRLLDQYVDAGGSFLDTSnnYAFWNEGCSGgeseLLLGQWLKDRG-NREHIVLATKVgaQPTipgg 97
Cdd:cd19128 3 RLGFGTyKITESESKEAVKNAIKAGYRHIDCA--YYYGNEAFIG----IAFSEIFKDGGvKREDLFITSKL--WPT---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 98 gFESMEglsrKAIEQaIDGSLRRLGTDYVDLYYAH--------------ID-----DVNTPLEETMEAFDRLVRAGKVRA 158
Cdd:cd19128 71 -MHQPE----NVKEQ-LLITLQDLQLEYLDLFLIHwplafdmdtdgdprDDnqiqsLSKKPLEDTWRAMEQCVDEKLTKN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 159 LGCSNHHTwrvekarniskshhwasySCIQQRYTYLRPKPgadFGVQISA-----NDELLNYCQTHDdFSLLAYSPLlNG 233
Cdd:cd19128 145 IGVSNYST------------------KLLTDLLNYCKIKP---FMNQIEChpyfqNDKLIKFCIENN-IHVTAYRPL-GG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 234 SYTRSDAPLQkqyesEDAQarlrvLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASK-PEQLQENLDSLNIRLTQDQL 312
Cdd:cd19128 202 SYGDGNLTFL-----NDSE-----LKALATKYNTTPPQVIIAWHLQKWPKNYSVIPKSAnKSRCQQNFDINDLALTKEDM 271
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
2-315 |
1.25e-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: 70.25 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 2 QQLLLGNTGIQVSALGLGCLNfGSRTDKETSyrlLDQYVDAGGSFLDTSNNYAfwNEGCSGGeselLLGQWLKD-RGNRE 80
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWQ-SSPEEIETA---VDTALEAGYRHIDTAYVYR--NEAAIGN----VLKKWIDSgKVKRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATKVgaqptipgggfeSMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHID---------------------DVNTP 139
Cdd:cd19155 71 ELFIVTKL------------PPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 140 LEETMEAFDRLVRAGKVRALGCSNHHTWRVE--------KARNISKSHHwasysciqqryTYLRPKpgadfgvqisandE 211
Cdd:cd19155 139 LLDIWKAMEAQVDQGLTRSIGLSNFNREQMArilknariKPANLQVELH-----------VYLQQK-------------D 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 212 LLNYCQTHdDFSLLAYSPL-----LNGSYTRSDAPLQKQYESEDAqarlrVLSEVAQETGGTLNQIVLAWLLQstpTTLS 286
Cdd:cd19155 195 LVDFCSTH-SITVTAYAPLgspgaAHFSPGTGSPSGSSPDLLQDP-----VVKAIAERHGKSPAQVLLRWLMQ---RGVV 265
|
330 340 350
....*....|....*....|....*....|
gi 1133861166 287 IIAAS-KPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19155 266 VIPKStNAARIKENFQVFDFELTEADMAKL 295
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
10-315 |
1.82e-13 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 69.08 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNFGSRTDKETSYRLLdqyVDAGGSFLDTSnnYAFWNEgcsggESellLGQWLKDRG-NREHIVLATKV 88
Cdd:cd19156 6 GVEMPRLGLGVWRVQDGAEAENAVKWA---IEAGYRHIDTA--AIYKNE-----EG---VGQGIRESGvPREEVFVTTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 89 GAQPTipggGFESMEglsrkaieQAIDGSLRRLGTDYVDLYYAHIdDVNTPLEETMEAFDRLVRAGKVRALGCSNHHtwr 168
Cdd:cd19156 73 WNSDQ----GYESTL--------AAFEESLEKLGLDYVDLYLIHW-PVKGKFKDTWKAFEKLYKEKKVRAIGVSNFH--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 169 vekarniskSHHwasyscIQQRYTYLRPKPGADfgvQIS-----ANDELLNYCQTHdDFSLLAYSPLLNGSYTRSDaplq 243
Cdd:cd19156 137 ---------EHH------LEELLKSCKVAPMVN---QIElhpllTQEPLRKFCKEK-NIAVEAWSPLGQGKLLSNP---- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133861166 244 kqyesedaqarlrVLSEVAQETGGTLNQIVLAWLLQSTPTTlsIIAASKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19156 194 -------------VLKAIGKKYGKSAAQVIIRWDIQHGIIT--IPKSVHEERIQENFDVFDFELTAEEIRQI 250
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-315 |
1.85e-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: 69.30 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLnfgsRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsGGESELllGQWLK---DRG--NREHI 82
Cdd:cd19125 6 NTGAKIPAVGLGTW----QADPGVVGNAVKTAIKEGYRHIDCAAIY--------GNEKEI--GKALKklfEDGvvKREDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 83 VLATKVGAqptipgggfesmEGLSRKAIEQAIDGSLRRLGTDYVDLYYAH--------------IDDVNTPLEETMEAFD 148
Cdd:cd19125 72 FITSKLWC------------TDHAPEDVPPALEKTLKDLQLDYLDLYLIHwpvrlkkgahmpepEEVLPPDIPSTWKAME 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 149 RLVRAGKVRALGCSNHHTWRVEKARNISkshhwasysciqqrytylRPKPGADfgvQIS-----ANDELLNYCQTHdDFS 223
Cdd:cd19125 140 KLVDSGKVRAIGVSNFSVKKLEDLLAVA------------------RVPPAVN---QVEchpgwQQDKLHEFCKSK-GIH 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 224 LLAYSPLLNGSYTRSDAPLQKqyesedaqarLRVLSEVAQETGGTLNQIVLAWLLQstpTTLSIIAAS-KPEQLQENLDS 302
Cdd:cd19125 198 LSAYSPLGSPGTTWVKKNVLK----------DPIVTKVAEKLGKTPAQVALRWGLQ---RGTSVLPKStNEERIKENIDV 264
|
330
....*....|...
gi 1133861166 303 LNIRLTQDQLHRL 315
Cdd:cd19125 265 FDWSIPEEDFAKF 277
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-304 |
2.39e-13 |
|
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: 69.18 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 14 SALGLGCLNFGS---RTDKETSYRLLDQYVDAGGSFLDTSNNYafwneGCsgGESELLLGQWLKDRGnREHIVLATKVG- 89
Cdd:cd19152 1 PKLGFGTAPLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWY-----GA--GLSEERLGAALRELG-REDYVISTKVGr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 90 -------AQPTIPGG-----GFESMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAH-IDDVNTPLEETME----------A 146
Cdd:cd19152 73 llvplqeVEPTFEPGfwnplPFDAVFDYSYDGILRSIEDSLQRLGLSRIDLLSIHdPDEDLAGAESDEHfaqaikgafrA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 147 FDRLVRAGKVRALGC-SNhhTWRVekarnISKSHHWASYSC--IQQRYTYLrpkpgaDFgvqiSANDELLNYCQTHdDFS 223
Cdd:cd19152 153 LEELREEGVIKAIGLgVN--DWEV-----ILRILEEADLDWvmLAGRYTLL------DH----SAARELLPECEKR-GVK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 224 LLAYSPLLNGSYTRSDAPLQKQY--ESEDAQARLRVLSEVAQETGGTLNQIVLAWLLQStPTTLSII-AASKPEQLQENL 300
Cdd:cd19152 215 VVNAGPFNSGFLAGGDNFDYYEYgpAPPELIARRDRIEALCEQHGVSLAAAALQFALAP-PAVASVApGASSPERVEENV 293
|
....
gi 1133861166 301 DSLN 304
Cdd:cd19152 294 ALLA 297
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-162 |
8.72e-13 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 67.56 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 6 LGNTGIQVSALGLGCLNFGSR-TDKETSYRLLDQYVDA---GGSFLDTSNNYAfwnegcsGGESELLLGQWLKDRGN-RE 80
Cdd:cd19153 5 LEIALGNVSPVGLGTAALGGVyGDGLEQDEAVAIVAEAfaaGINHFDTSPYYG-------AESSEAVLGKALAALQVpRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 81 HIVLATKVGaqpTIPGGGFESmeglSRKAIEQAIDGSLRRLGTDYVDLYYAH---IDDVNTPLEETMEAFDRLVRAGKVR 157
Cdd:cd19153 78 SYTVATKVG---RYRDSEFDY----SAERVRASVATSLERLHTTYLDVVYLHdieFVDYDTLVDEALPALRTLKDEGVIK 150
|
....*
gi 1133861166 158 ALGCS 162
Cdd:cd19153 151 RIGIA 155
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
110-315 |
1.74e-12 |
|
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: 66.67 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 110 IEQAIDGSLRRLGTDYVDLYYAH-----------------------ID-DVNTPLEETMEAFDRLVRAGKVRALGCSNHH 165
Cdd:cd19118 84 VEPALDDTLKELGLDYLDLYLIHwpvafkptgdlnpltavptnggeVDlDLSVSLVDTWKAMVELKKTGKVKSIGVSNFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 166 TWRVEKArniskshhwasyscIQQryTYLRPKPgadfgVQISA-----NDELLNYCQTHdDFSLLAYSPLLNgsyTRSDA 240
Cdd:cd19118 164 IDHLQAI--------------IEE--TGVVPAV-----NQIEAhplllQDELVDYCKSK-NIHITAYSPLGN---NLAGL 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133861166 241 PLQKQYEsedaqarlrVLSEVAQETGGTLNQIVLAWLLQStptTLSIIAAS-KPEQLQENLDSlnIRLTQDQLHRL 315
Cdd:cd19118 219 PLLVQHP---------EVKAIAAKLGKTPAQVLIAWGIQR---GHSVIPKSvTPSRIRSNFEQ--VELSDDEFNAV 280
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-312 |
4.05e-12 |
|
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: 65.93 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLNFGSRTDKETSYRLldqyVDAGGSFLDTSNNYafwnegcsGGESELllGQWLK---DRG--NREHI 82
Cdd:cd19113 6 NSGYKMPSVGFGCWKLDNATAADQIYQA----IKAGYRLFDGAEDY--------GNEKEV--GEGVNraiDEGlvKREEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 83 VLATKVGAQPTIPgggfesmeglsrKAIEQAIDGSLRRLGTDYVDLYYAH-------------------------IDDVN 137
Cdd:cd19113 72 FLTSKLWNNFHDP------------KNVETALNKTLSDLKLDYVDLFLIHfpiafkfvpieekyppgfycgdgdnFVYED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 138 TPLEETMEAFDRLVRAGKVRALGCSNHhtwrvekarniskshhwaSYSCIQQRYTYLRPKPGAdfgVQIS-----ANDEL 212
Cdd:cd19113 140 VPILDTWKALEKLVDAGKIKSIGVSNF------------------PGALILDLLRGATIKPAV---LQIEhhpylQQPKL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 213 LNYCQTHdDFSLLAYSPLLNGSYTRSDAPLQKQ----YESEdaqarlrVLSEVAQETGGTLNQIVLAWllqSTPTTLSII 288
Cdd:cd19113 199 IEYAQKA-GITITAYSSFGPQSFVELNQGRALNtptlFEHD-------TIKSIAAKHNKTPAQVLLRW---ATQRGIAVI 267
|
330 340
....*....|....*....|....*
gi 1133861166 289 AAS-KPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19113 268 PKSnLPERLLQNLSVNDFDLTKEDF 292
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
16-162 |
1.25e-11 |
|
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: 64.22 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 16 LGLGCLNFGSRTDKETS--YRLLDQYVDAGGSFLDTSNNYafwnegcsgGESELLLGQWLKDRGN---REHIVLATKVGa 90
Cdd:cd19164 18 FGAATFSYQYTTDPESIppVDIVRRALELGIRAFDTSPYY---------GPSEIILGRALKALRDefpRDTYFIITKVG- 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133861166 91 qpTIPGGGFEsmegLSRKAIEQAIDGSLRRLGTDYVDLYYAHidDVN-TPLEETMEAFDRLVR---AGKVRALGCS 162
Cdd:cd19164 88 --RYGPDDFD----YSPEWIRASVERSLRRLHTDYLDLVYLH--DVEfVADEEVLEALKELFKlkdEGKIRNVGIS 155
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
113-312 |
2.21e-11 |
|
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: 63.01 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 113 AIDGSLRRLGTDYVDLYYAHIDdvnTPLE----ETMEAFDRLVRAGKVRALGCSNHHTWRVEKArniskSHHWASYSCIQ 188
Cdd:cd19130 85 AFAESLAKLGLDQVDLYLVHWP---TPAAgnyvHTWEAMIELRAAGRTRSIGVSNFLPPHLERI-----VAATGVVPAVN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 189 QryTYLRPKpgadfgvqiSANDELLNYCQTHdDFSLLAYSPLLNGSYTrsDAPLqkqyesedaqarlrvLSEVAQETGGT 268
Cdd:cd19130 157 Q--IELHPA---------YQQRTIRDWAQAH-DVKIEAWSPLGQGKLL--GDPP---------------VGAIAAAHGKT 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1133861166 269 LNQIVLAWLLQSTPTTLSiiAASKPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19130 208 PAQIVLRWHLQKGHVVFP--KSVRRERMEDNLDVFDFDLTDTEI 249
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
110-312 |
8.32e-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: 61.63 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 110 IEQAIDGSLRRLGTDYVDLYYAH-------IDDV------------NTPLEETMEAFDRLVRAGKVRALGCSNHHTWRVE 170
Cdd:cd19106 84 VEPALRKTLKDLQLDYLDLYLIHwpyaferGDNPfpknpdgtirydSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQID 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 171 KARNISkshhwasysciqqrytylRPKPgADFGVQIS---ANDELLNYCQTHdDFSLLAYSPLlnGSytrSDAPLQKQYE 247
Cdd:cd19106 164 DILSVA------------------RIKP-AVLQVECHpylAQNELIAHCKAR-GLVVTAYSPL--GS---PDRPWAKPDE 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133861166 248 S---EDAqarlrVLSEVAQETGGTLNQIVLAWLLQSTPTTlsIIAASKPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19106 219 PvllEEP-----KVKALAKKYNKSPAQILLRWQVQRGVVV--IPKSVTPSRIKQNIQVFDFTLSPEEM 279
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
13-317 |
1.12e-10 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 61.19 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 13 VSALGLGclnfgsrtdketSYRLLDQYV--------DAGGSFLDTSNNYafwnegcsGGESELllGQWLKDRG-NREHIV 83
Cdd:PRK11172 3 IPAFGLG------------TFRLKDQVVidsvktalELGYRAIDTAQIY--------DNEAAV--GQAIAESGvPRDELF 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 84 LATKVGaqptipgggfesMEGLSRKAIEQAIDGSLRRLGTDYVDLYYAHI----DDVntPLEETMEAFDRLVRAGKVRAL 159
Cdd:PRK11172 61 ITTKIW------------IDNLAKDKLIPSLKESLQKLRTDYVDLTLIHWpspnDEV--SVEEFMQALLEAKKQGLTREI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 160 GCSNHHTWRVEKARNISKSHHWASysciQQrytylrpkpgadfgVQIS---ANDELLNYCQTH----DDFSLLAYSPLLn 232
Cdd:PRK11172 127 GISNFTIALMKQAIAAVGAENIAT----NQ--------------IELSpylQNRKVVAFAKEHgihvTSYMTLAYGKVL- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 233 gsytrSDAplqkqyesedaqarlrVLSEVAQETGGTLNQIVLAWLLQStptTLSIIAAS-KPEQLQENLDSLNIRLTQDQ 311
Cdd:PRK11172 188 -----KDP----------------VIARIAAKHNATPAQVILAWAMQL---GYSVIPSStKRENLASNLLAQDLQLDAED 243
|
....*.
gi 1133861166 312 LHRLHT 317
Cdd:PRK11172 244 MAAIAA 249
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-312 |
1.88e-08 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 54.48 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGClnfGSRTDKETSyRLLDQYVDAGGSFLDTSNNYAfwnegcsggeSELLLGQWLKDRG-NREHIVLAT 86
Cdd:cd19134 6 NDDNTMPVIGLGV---GELSDDEAE-RSVSAALEAGYRLIDTAAAYG----------NEAAVGRAIAASGiPRGELFVTT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 87 KVGAqptiPGGGFESMEGLSRKaieqaidgSLRRLGTDYVDLYYAHiddvnTPLEET---MEAFDRLVRA---GKVRALG 160
Cdd:cd19134 72 KLAT----PDQGFTASQAACRA--------SLERLGLDYVDLYLIH-----WPAGREgkyVDSWGGLMKLreeGLARSIG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 161 CSNHHTWRVEKARNIskshhwasysciqqryTYLRPKPGadfgvQIS-----ANDELLNYCQTHDDFSlLAYSPLLNGSY 235
Cdd:cd19134 135 VSNFTAEHLENLIDL----------------TFFTPAVN-----QIElhpllNQAELRKVNAQHGIVT-QAYSPLGVGRL 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133861166 236 TrsDAPlqkqyesedaqarlrVLSEVAQETGGTLNQIVLAWLLQSTPTTLSiiAASKPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19134 193 L--DNP---------------AVTAIAAAHGRTPAQVLLRWSLQLGNVVIS--RSSNPERIASNLDVFDFELTADHM 250
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
107-312 |
2.76e-08 |
|
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: 54.35 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 107 RKAIEQAIDGSLRRLGTDYVDLYYAH-------------IDD------VNTPLEETMEAFDRLVRAGKVRALGCSNHHTW 167
Cdd:cd19107 77 KGLVKGACQKTLSDLKLDYLDLYLIHwptgfkpgkelfpLDEsgnvipSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 168 RVEKARNISKshhwasysciqqrytyLRPKPGADfgvQISAN-----DELLNYCQThDDFSLLAYSPLlnGSYTRSDAPL 242
Cdd:cd19107 157 QIERILNKPG----------------LKYKPAVN---QIECHpyltqEKLIQYCQS-KGIVVTAYSPL--GSPDRPWAKP 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133861166 243 QKQYESEDAQarlrvLSEVAQETGGTLNQIVLAWLLQStptTLSIIAAS-KPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19107 215 EDPSLLEDPK-----IKEIAAKHNKTTAQVLIRFPIQR---NLVVIPKSvTPERIAENFKVFDFELSSEDM 277
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-307 |
1.67e-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: 51.79 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGLGCLNFGSRTDKETSYrlldQYVDAGGSFLDTSNNYafwnegcsGGESELllGQWLK---DRG--NREHIVL 84
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIY----NAIKVGYRLIDGALLY--------GNEAEV--GRGIRkaiQEGlvKREDLFI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 85 ATKVGaqptipgGGFESmeglsRKAIEQAIDGSLRRLGTDYVDLYYAH-------IDDV------------------NTP 139
Cdd:cd19114 67 VTKLW-------NNFHG-----KDHVREAFDRQLKDYGLDYIDLYLIHfpipaayVDPAenypflwkdkelkkfpleQSP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 140 LEETMEAFDRLVRAGKVRALGCSNHHTwrvekarniskshhwasySCIQQRYTYLRPKPGAdfgVQISAN-----DELLN 214
Cdd:cd19114 135 MQECWREMEKLVDAGLVRNIGIANFNV------------------QLILDLLTYAKIKPAV---LQIEHHpylqqKRLID 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 215 YCQTHdDFSLLAYSPLLNGSY---TRSDAPLQKQYESEDAQArlrvlseVAQETGGTLNQIVLAWLLQStptTLSIIAAS 291
Cdd:cd19114 194 WAKKQ-GIQITAYSSFGNAVYtkvTKHLKHFTNLLEHPVVKK-------LADKHKRDTGQVLLRWAVQR---NITVIPKS 262
|
330
....*....|....*..
gi 1133861166 292 -KPEQLQENLDSLNIRL 307
Cdd:cd19114 263 vNVERMKTNLDITSYKL 279
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-244 |
2.88e-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: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLNFGSRTDKE-------TSYRLLDQYVdaggsfldtsnnyafwnegCSGGESELllGQWLKDRGN-- 78
Cdd:cd19121 7 NTGASIPAVGLGTWQAKAGEVKAavahalkIGYRHIDGAL-------------------CYQNEDEV--GEGIKEAIAgg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 79 --REHIVLATKVGAQPTipgggfesmeglsrKAIEQAIDGSLRRLGTDYVDLYYAH-----IDDVNTPLEETME----AF 147
Cdd:cd19121 66 vkREDLFVTTKLWSTYH--------------RRVELCLDRSLKSLGLDYVDLYLVHwpvllNPNGNHDLFPTLPdgsrDL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 148 D-------------RLVRAGKVRALGCSNHH---------TWRVEKARNISKSHHwasySCIQQrytylrpkpgadfgvq 205
Cdd:cd19121 132 DwdwnhvdtwkqmeKVLKTGKTKAIGVSNYSipyleellkHATVVPAVNQVENHP----YLPQQ---------------- 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1133861166 206 isandELLNYCQThDDFSLLAYSPL-LNGSYTRSDAPLQK 244
Cdd:cd19121 192 -----ELVDFCKE-KGILIEAYSPLgSTGSPLISDEPVVE 225
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|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
110-315 |
4.24e-07 |
|
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: 50.73 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 110 IEQAIDGSLRRLGTDYVDLYYAHI------DDVNTPLEE-------------TMEAFDRLVRAGKVRALGCSNHHTWRVE 170
Cdd:cd19110 80 VKTACTRSLKALKLNYLDLYLIHWpmgfkpGEPDLPLDRsgmvipsdtdfldTWEAMEDLVIEGLVKNIGVSNFNHEQLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 171 KARNISKshhwasysciqqrytyLRPKPGADfgvQISAN-----DELLNYCQTHdDFSLLAYSPlLNGSytRSDAPLQkq 245
Cdd:cd19110 160 RLLNKPG----------------LRVKPVTN---QIECHpyltqKKLISFCQSR-NVSVTAYRP-LGGS--CEGVDLI-- 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 246 yesEDAqarlrVLSEVAQETGGTLNQIVLAWLLQStpTTLSIIAASKPEQLQENLDSLNIRLTQDQLHRL 315
Cdd:cd19110 215 ---DDP-----VIQRIAKKHGKSPAQILIRFQIQR--NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
110-312 |
4.56e-07 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 50.50 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 110 IEQAIDGSLRRLGTDYVDLYYAH------------------------IDDVNTPLEETMEAFDRLVRAGKVRALGCSNHh 165
Cdd:cd19115 89 VEPICRKQLADWGIDYFDLFLIHfpialkyvdpavryppgwfydgkkVEFSNAPIQETWTAMEKLVDKGLARSIGVSNF- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 166 twrvekarniskshhwaSYSCIQQRYTYLRPKPGAdfgVQIS-----ANDELLNYCQThDDFSLLAYS---PL----LNG 233
Cdd:cd19115 168 -----------------SAQLLMDLLRYARIRPAT---LQIEhhpylTQPRLVKYAQK-EGIAVTAYSsfgPQsfleLDL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 234 SYTRSDAPLqkqYESEdaqarlrVLSEVAQETGGTLNQIVLAWllqSTPTTLSIIAAS-KPEQLQENLDSLNIRLTQDQL 312
Cdd:cd19115 227 PGAKDTPPL---FEHD-------VIKSIAEKHGKTPAQVLLRW---ATQRGIAVIPKSnNPKRLAQNLDVTGFDLEAEEI 293
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-319 |
1.13e-05 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 46.34 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 8 NTGIQVSALGLGCLNfgSRTDKETSYRLLDQYVDAGGSFLDTSNNYafwnegcsggESELLLGQWLK---DRG--NREHI 82
Cdd:cd19119 7 NTGASIPALGLGTAS--PHEDRAEVKEAVEAAIKEGYRHIDTAYAY----------ETEDFVGEAIKraiDDGsiKREEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 83 VLATKVgaQPTIpgggfesmeglsRKAIEQAIDGSLRRLGTDYVDLYYAH------IDDVNTPLEETMEAFDRLVR---- 152
Cdd:cd19119 75 FITTKV--WPTF------------YDEVERSLDESLKALGLDYVDLLLVHwpvcfeKDSDDSGKPFTPVNDDGKTRyaas 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 153 ---------------AGKVRALGCSNHHTWRVEkarniskshhwasySCIQQrytyLRPKPGADfgvQISAND-----EL 212
Cdd:cd19119 141 gdhittykqlekiylDGRAKAIGVSNYSIVYLE--------------RLIKE----CKVVPAVN---QVELHPhlpqmDL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 213 LNYCQTHdDFSLLAYSPLlnGSYTrsdAPLQKqyeSEDAqarlrvlSEVAQETGGTLNQIVLAWLLQStpTTLSIIAASK 292
Cdd:cd19119 200 RDFCFKH-GILVTAYSPL--GSHG---APNLK---NPLV-------KKIAEKYNVSTGDILISYHVRQ--GVIVLPKSLK 261
|
330 340
....*....|....*....|....*..
gi 1133861166 293 PEQLQENLDSlnIRLTQDQLHRLHTAG 319
Cdd:cd19119 262 PVRIVSNGKI--VSLTKEDLQKLDDIG 286
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-315 |
7.06e-04 |
|
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: 40.79 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 10 GIQVSALGL-GCLNFGSRTD----------KETSYRLLDQYVDAGGSFLDTSNNYafwnegcsgGESELLLGQWLKDRG- 77
Cdd:cd19098 4 GLGLAALGRpGYINLGHAADlgsgrsveamRAHTHAVLDAAWAAGVRYFDAARSY---------GRAEEFLGSWLRSRNi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 78 NREHIVLATKVG----AQPTIPGGGFESMEgLSRKAIEQAIDGSLRRLGtDYVDLYYAHIDDVNTPLEETMEAFDRLVRA 153
Cdd:cd19098 75 APDAVFVGSKWGytytADWQVDAAVHEVKD-HSLARLLKQWEETRSLLG-KHLDLYQIHSATLESGVLEDADVLAALAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 154 GKV-RALGCSNHHTWR---VEKARNISKSHHwASYSCIQQRYTYLRPKPGadfgvqisandELLNycQTHD-DFSLLAYS 228
Cdd:cd19098 153 KAEgVKIGLSLSGPQQaetLRRALEIEIDGA-RLFDSVQATWNLLEQSAG-----------EALE--EAHEaGMGVIVKE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133861166 229 PLLNGSYT-RSDAPLQKqyesedaqARLRVLSEVAQETGGTLNQIVLAWLLQSTPTTLSIIAASKPEQLQENLDSLNIRL 307
Cdd:cd19098 219 ALANGRLTdRNPSPELA--------PLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSL 290
|
....*...
gi 1133861166 308 TQDQLHRL 315
Cdd:cd19098 291 DLELLAAL 298
|
|
| |
