|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-288 |
7.08e-109 |
|
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: 315.96 E-value: 7.08e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 11 LIVSEIGFGSWAIGGDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILSTKgglIGHHY 90
Cdd:cd19086 1 LEVSEIGFGTWGLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIATK---FGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 91 DPNQPAVYG-DPQKIIDAFEASLLRLKTDYIDVYFCHIWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKHFNQ 169
Cdd:cd19086 78 DGGPERPQDfSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 170 DNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKfnhetqfpdddlrkdwpkekwfkdslnkveklr 249
Cdd:cd19086 158 RGGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK--------------------------------- 204
|
250 260 270
....*....|....*....|....*....|....*....
gi 1041868156 250 slvrsnrsLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19086 205 --------LAQAALRFILSHPAVSTVIPGARSPEQVEEN 235
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-288 |
3.19e-108 |
|
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: 317.12 E-value: 3.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGGDeWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIIL 79
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGP-WGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRpRDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STKgglIGHHYDPNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTN 159
Cdd:COG0667 80 ATK---VGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLH-RPDPDTPIEETLGALDELVREGKIRYIGVSNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 160 DLD----YIKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDD-LRKDWPK 234
Cdd:COG0667 156 SAEqlrrALAIAEGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDrAATNFVQ 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 235 EKWFKDSLNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:COG0667 236 GYLTERNLALVDALRAIAAEhGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEEN 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-288 |
2.08e-104 |
|
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: 306.76 E-value: 2.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 10 GLIVSEIGFGSWAIGGDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILSTKGGL---I 86
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVIATKCGLrwdG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 87 GHHYDPNqpavyGDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKH---EETeafLQAFQTLKKSGKVRAVGVSTNDLDY 163
Cdd:cd19084 81 GKGVTKD-----LSPESIRKEVEQSLRRLQTDYIDLYQIH-WPDPNtpiEET---AEALEKLKKEGKIRYIGVSNFSVEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 164 IKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWP--KEKWFKDS 241
Cdd:cd19084 152 LEEARKYGPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPffRGENFEKN 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1041868156 242 LNKVEKLRSLV-RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19084 232 LEIVDKLKEIAeKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEEN 279
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-289 |
8.43e-91 |
|
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: 272.99 E-value: 8.43e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 3 YRLLGNTGLIVSEIGFGSWAIGGDEW-GAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILST 81
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGGPWwGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDKVVLAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 82 KGGLI------GHHYDPNQPAVYGD--PQKIIDAFEASLLRLKTDYIDVYFCHiWWDKH---EETeafLQAFQTLKKSGK 150
Cdd:cd19149 81 KCGLRwdreggSFFFVRDGVTVYKNlsPESIREEVEQSLKRLGTDYIDLYQTH-WQDVEtpiEET---MEALEELKRQGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 151 VRAVGVSTNDLDYIKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRK 230
Cdd:cd19149 157 IRAIGASNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDREFDAGDARS 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 231 DWPkekWFK-DSLNKV----EKLRSLV-RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENS 289
Cdd:cd19149 237 GIP---WFSpENREKVlallEKWKPLCeKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENA 298
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-308 |
3.25e-84 |
|
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: 255.81 E-value: 3.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 4 RLLGNTGLIVSEIGFGSWAIGGDE-WGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILST 81
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGHNlYPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYnRNEVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 82 KGGligHHYDPNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDL 161
Cdd:cd19083 82 KGA---HKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIH-FPDGETPKAEAVGALQELKDEGKIRAIGVSNFSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 162 DYIKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWP--KEKWFK 239
Cdd:cd19083 158 EQLKEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDLRNDKPlfKGERFS 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 240 DSLNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLtRPLLLDNEIEFIKQL 308
Cdd:cd19083 238 ENLDKVDKLKSIADEkGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKAL-DVTLTEEEIAFIDAL 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-288 |
9.66e-84 |
|
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: 254.05 E-value: 9.66e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 13 VSEIGFGSWAIGGDE-WGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILSTKGGliGHHYD 91
Cdd:cd19085 1 VSRLGLGCWQFGGGYwWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIATKVS--PDNLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 92 PNQpavygdpqkIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKHFNQDN 171
Cdd:cd19085 79 PED---------VRKSCERSLKRLGTDYIDLYQIH-WPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 172 DLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWP---KEKWFKDSLNKVEKL 248
Cdd:cd19085 149 RIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTRLFrhfEPGAEEETFEALEKL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1041868156 249 RSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19085 229 KEIADElGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEEN 269
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-308 |
3.47e-81 |
|
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: 247.97 E-value: 3.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 13 VSEIGFGSWAIGGDE----WGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILSTKGGL--- 85
Cdd:cd19102 1 LTTIGLGTWAIGGGGwgggWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIVATKCGLlwd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 86 ----IGHHYDPNQpavygdpqkIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDL 161
Cdd:cd19102 81 eegrIRRSLKPAS---------IRAECEASLRRLGVDVIDLYQIH-WPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 162 DYIKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHET--QFPDDDLRKDWP--KEKW 237
Cdd:cd19102 151 DQMKRCQAIHPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERvaSLPADDWRRRSPffQEPN 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041868156 238 FKDSLNKVEKLRSL-VRSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSS----HLTrplllDNEIEFIKQL 308
Cdd:cd19102 231 LARNLALVDALRPIaERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGaadlRLT-----PEELAEIEAL 301
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-287 |
3.52e-79 |
|
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: 242.60 E-value: 3.52e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 10 GLIVSEIGFGSWAIGGDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH--RQDIILSTKGGLig 87
Cdd:cd19148 1 DLPVSRIALGTWAIGGWMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYgkRDRVVIATKVGL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 88 hHYDPNQPAVYGD-PQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKH 166
Cdd:cd19148 79 -EWDEGGEVVRNSsPARIRKEVEDSLRRLQTDYIDLYQVH-WPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 167 FNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWPK--EKWFKDSLNK 244
Cdd:cd19148 157 FRKVAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLRRTDPKfqEPRFSQYLAA 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1041868156 245 VEKLRSLVRSN--RSLAQVALRYVLSHPAVSVAIPGAKNSTQVEE 287
Cdd:cd19148 237 VEELDKLAQERygKSVIHLAVRWLLDQPGVSIALWGARKPEQLDA 281
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-288 |
1.50e-74 |
|
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: 230.66 E-value: 1.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIGGDeWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH---RQDIILSTKGGLIGHHYDp 92
Cdd:pfam00248 1 IGLGTWQLGGG-WGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYpvkRDKVVIATKVPDGDGPWP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 93 nqpaVYGDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKHFNQDN- 171
Cdd:pfam00248 79 ----SGGSKENIRKSLEESLKRLGTDYIDLYYLH-WPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGk 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 172 -DLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWPkeKWFKDSLNKVEKLRS 250
Cdd:pfam00248 154 iPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLK--KGTPLNLEALEALEE 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1041868156 251 LVRSN-RSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:pfam00248 232 IAKEHgVSPAQVALRWALSKPGVTIPIPGASNPEQLEDN 270
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-288 |
2.67e-66 |
|
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: 209.76 E-value: 2.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 10 GLIVSEIGFGSWAIGGDEwgaVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILSTKGgligh 88
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQ---VDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWpRESYVISTKV----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 89 hYDPNQPAVY--GDPQK-IIDAFEASLLRLKTDYIDVYFCHiWWDkhEET--EAFLQAFQTLKKSGKVRAVGVSTNDLDY 163
Cdd:cd19074 73 -FWPTGPGPNdrGLSRKhIFESIHASLKRLQLDYVDIYYCH-RYD--PETplEETVRAMDDLIRQGKILYWGTSEWSAEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 164 I---KHFNQDNDLD---VVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHEtQFPDDDLRKDWPKEKW 237
Cdd:cd19074 149 IaeaHDLARQFGLIppvVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDG-IPPPSRSRATDEDNRD 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1041868156 238 FKDS------LNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19074 228 KKRRlltdenLEKVKKLKPIADElGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEEN 285
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-288 |
6.23e-65 |
|
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: 206.65 E-value: 6.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGGDewgaVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILS 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGR----TDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 81 TK-GGLIGHhyDPNQPAVygDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVST- 158
Cdd:cd19087 77 TKvFGPMGD--DPNDRGL--SRRHIRRAVEASLRRLQTDYIDLYQMH-HFDRDTPLEETLRALDDLVRQGKIRYIGVSNf 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 159 --------NDLDYIKHFNQdndLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDL-- 228
Cdd:cd19087 152 aawqiakaQGIAARRGLLR---FVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLve 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041868156 229 RKDWPKEKWFKDSLNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19087 229 RARYQARYGLEEYRDIAERFEALAAEaGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDS 289
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-288 |
2.57e-64 |
|
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: 202.81 E-value: 2.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGswaiggdewGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND-HRQDIIL 79
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFG---------GGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGlRRDKVFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STKGGLighhydpnqPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCH--IWWDKHEETEAFLQAFQTLKKSGKVRAVGVS 157
Cdd:cd19105 72 ATKASP---------RLDKKDKAELLKSVEESLKRLQTDYIDIYQLHgvDTPEERLLNEELLEALEKLKKEGKVRFIGFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 158 T--NDLDYIKHFNQDNDLDVVQFDYSILNKEPE-KDILPYIEKHNLGAVIrgplkMGILTGKFNHEtqfpdddlrkdwpk 234
Cdd:cd19105 143 ThdNMAEVLQAAIESGWFDVIMVAYNFLNQPAElEEALAAAAEKGIGVVA-----MKTLAGGYLQP-------------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1041868156 235 ekwfkdslnkvEKLRSLVRSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19105 204 -----------ALLSVLKAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEEN 246
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-288 |
2.60e-64 |
|
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: 205.15 E-value: 2.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGG-----DEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQ 75
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGgggffGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 76 DIILSTKGGL-IGHhyDPNQpavYGDPQ-KIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRA 153
Cdd:cd19091 81 DVLIATKVRGrMGE--GPND---VGLSRhHIIRAVEASLKRLGTDYIDLYQLH-GFDALTPLEETLRALDDLVRQGKVRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 154 VGVS-------------TNDLDYIKHfnqdndlDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHE 220
Cdd:cd19091 155 IGVSnfsawqimkalgiSERRGLARF-------VALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041868156 221 TQFPDDD-LRKDWP------KEKWFkdslNKVEKLRSLV-RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19091 228 QPAPEGSrLRRTGFdfppvdRERGY----DVVDALREIAkETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDN 299
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-288 |
3.69e-61 |
|
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: 194.27 E-value: 3.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSWAIGGDewgaVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH--RQDIILSTKGgliGHHYD 91
Cdd:cd06660 1 SRLGLGTMTFGGD----GDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRgnRDDVVIATKG---GHPPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 92 PNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKHFNQDN 171
Cdd:cd06660 74 GDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLH-RDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 172 D------LDVVQFDYSILNKEP-EKDILPYIEKHNLGAVIRGPLKMGiltgkfnhetqfpdddlrkdwpkekwfkdslnk 244
Cdd:cd06660 153 KahglpgFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG--------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1041868156 245 veklrslvrsnrsLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd06660 200 -------------PAQLALAWLLSQPFVTVPIVGARSPEQLEEN 230
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-288 |
2.23e-60 |
|
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: 194.74 E-value: 2.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 2 EYRLLGNTGLIVSEIGFG----SWAiggdeWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDI 77
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSAF-----YGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 78 ILSTKGGLighHYDPNQPAVY--GDPQKIIDAFEASLLRLKTDYIDVYFCHIwWDKH---EETeafLQAFQTLKKSGKVR 152
Cdd:cd19076 76 VIATKFGI---VRDPGSGFRGvdGRPEYVRAACEASLKRLGTDVIDLYYQHR-VDPNvpiEET---VGAMAELVEEGKVR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 153 AVGVSTNDLDYIKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDW 232
Cdd:cd19076 149 YIGLSEASADTIRRAHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNN 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1041868156 233 PK--EKWFKDSLNKVEKLRSL-VRSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19076 229 PRfqGENFDKNLKLVEKLEAIaAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEEN 287
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-308 |
1.94e-59 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 193.88 E-value: 1.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIggdewgAVKDNESLDA-IEKAIDLGVNFIDTADVYGlgHSETLVAKAINDHRQDIIL 79
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRL------PRKDEEEAEAlIRRAIDNGINYIDTARGYG--DSEEFLGKALKGPRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STKgglighhydpnQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCH-----IWWDKHEETEAFLQAFQTLKKSGKVRAV 154
Cdd:COG1453 73 ATK-----------LPPWVRDPEDMRKDLEESLKRLQTDYIDLYLIHglnteEDLEKVLKPGGALEALEKAKAEGKIRHI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 155 GVST-NDLDYIKHFNQDNDLDVVQFDYSILN--KEPEKDILPYIEKHNLGAVIRGPLKMGILTgkfnhetqfpdddlrkd 231
Cdd:COG1453 142 GFSThGSLEVIKEAIDTGDFDFVQLQYNYLDqdNQAGEEALEAAAEKGIGVIIMKPLKGGRLA----------------- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041868156 232 wpkekwfkdslNKVEKLRSLVRSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLTRPL-LLDNEIEFIKQL 308
Cdd:COG1453 205 -----------NPPEKLVELLCPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLEpLTEEELAILERL 271
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-296 |
2.91e-58 |
|
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: 188.15 E-value: 2.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSWAIGGdEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLghSETLVAKAINDH-RQDIILSTKGGlighhYDP 92
Cdd:cd19090 1 SALGLGTAGLGG-VFGGVDDDEAVATIRAALDLGINYIDTAPAYGD--SEERLGLALAELpREPLVLSTKVG-----RLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 93 NQPAVYgDPQKIIDAFEASLLRLKTDYIDVYFCH-----IWWDKHEETEAfLQAFQTLKKSGKVRAVGVSTNDLDYIKHF 167
Cdd:cd19090 73 EDTADY-SADRVRRSVEESLERLGRDRIDLLMIHdpervPWVDILAPGGA-LEALLELKEEGLIKHIGLGGGPPDLLRRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 168 NQDNDLDVV--QFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLrkdwpkekwFKDSLNKV 245
Cdd:cd19090 151 IETGDFDVVltANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTYRWL---------SPELLDRA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1041868156 246 EKLRSLVRSNR-SLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLTRPL 296
Cdd:cd19090 222 KRLYELCDEHGvPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPL 273
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-288 |
6.39e-57 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 183.98 E-value: 6.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSWAIGGDeWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLghSETLVAKAI-NDHRQDIILSTKgglIGHHYDP 92
Cdd:cd19095 1 SVLGLGTSGIGRV-WGVPSEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRALaGLRRDDLFIATK---VGTHGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 93 NQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCH---IWwdkhEETEAFLQAFQTLKKSGKVRAVGVSTnDLDYIKHFNQ 169
Cdd:cd19095 75 GRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHgpsDD----ELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 170 DNDLDVVQFDYSILNKEpEKDILPYIEKHNLGAVIRGPLKMGILTGKFnhetqFPDDDLRKDWPKEKWFKDSlnkveklr 249
Cdd:cd19095 150 SGVFDVVQLPYNVLDRE-EEELLPLAAEAGLGVIVNRPLANGRLRRRV-----RRRPLYADYARRPEFAAEI-------- 215
|
250 260 270
....*....|....*....|....*....|....*....
gi 1041868156 250 slvrSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19095 216 ----GGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEEN 250
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-288 |
7.53e-57 |
|
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: 185.87 E-value: 7.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 2 EYRLLGNTGLIVSEIGFGSWAIGGDEWGAVKDNE--SLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH--RQDI 77
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGDPKWRPWVLDEeeSRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFapRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 78 ILSTKGGLIGHHyDPNQpavYGDPQK-IIDAFEASLLRLKTDYIDVYFCHiWWDKH---EETeafLQAFQTLKKSGKVRA 153
Cdd:cd19079 81 VIATKVYFPMGD-GPNG---RGLSRKhIMAEVDASLKRLGTDYIDLYQIH-RWDYEtpiEET---LEALHDVVKSGKVRY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 154 VGVSTNdldYIKHFNQDNDLD---------VVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFP 224
Cdd:cd19079 153 IGASSM---YAWQFAKALHLAekngwtkfvSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERR 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041868156 225 DDDLRKDWPKEKWFKDS----LNKVEKLRSlvRSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19079 230 RSTTDTAKLKYDYFTEAdkeiVDRVEEVAK--ERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDA 295
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-296 |
3.97e-55 |
|
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: 180.82 E-value: 3.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGGdEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND-HRQDIIL 79
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGG-VFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGiPRDSYYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STKGGlighHYDPNQPAVYG-DPQKIIDAFEASLLRLKTDYIDVYFCHiwwDKH---------EETeafLQAFQTLKKSG 149
Cdd:cd19163 80 ATKVG----RYGLDPDKMFDfSAERITKSVEESLKRLGLDYIDIIQVH---DIEfapsldqilNET---LPALQKLKEEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 150 KVRAVGVSTNDLDYIKHF--NQDNDLDVVQF--DYSILNKEpEKDILPYIEKHNLGAVIRGPLKMGILT--GKFnhetqf 223
Cdd:cd19163 150 KVRFIGITGYPLDVLKEVleRSPVKIDTVLSycHYTLNDTS-LLELLPFFKEKGVGVINASPLSMGLLTerGPP------ 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041868156 224 pdddlrkDW-PKEKWFKDSLNKVEKLRSlvRSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLTRPL 296
Cdd:cd19163 223 -------DWhPASPEIKEACAKAAAYCK--SRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEPL 287
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-288 |
4.40e-55 |
|
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: 181.26 E-value: 4.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 6 LGNTGLIVSEIGFGSWAIGgdeWGAvkDNES----LDAIekaIDLGVNFIDTADVYGL-------GHSETLVAKAIND-- 72
Cdd:cd19081 2 LGRTGLSVSPLCLGTMVFG---WTA--DEETsfalLDAF---VDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSrg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 73 HRQDIILSTKGGLighhyDPNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVR 152
Cdd:cd19081 74 KRDRVVIATKVGF-----PMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAH-WDDPATPLEETLGALNDLIRQGKVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 153 AVGVSTNDLDYIKHFNQ---DNDL---DVVQFDYSILNKEP-EKDILPYIEKHNLGAVIRGPLKMGILTGKFNhetqfPD 225
Cdd:cd19081 148 YIGASNYSAWRLQEALElsrQHGLpryVSLQPEYNLVDRESfEGELLPLCREEGIGVIPYSPLAGGFLTGKYR-----SE 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041868156 226 DDLRKDWPKEKWFKDSLNK-----VEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19081 223 ADLPGSTRRGEAAKRYLNErglriLDALDEVAAEhGATPAQVALAWLLARPGVTAPIAGARTVEQLEDL 291
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-288 |
3.57e-54 |
|
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: 178.57 E-value: 3.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 4 RLLGNTGLIVSEIGFGSWAIGGDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILSTKG 83
Cdd:cd19080 1 RLLGRSGLRVSPLALGTMTFGTEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDRIVLATKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 84 GLighHYDPNQPAVYGDPQK-IIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVStnD-- 160
Cdd:cd19080 81 TM---NRRPGDPNAGGNHRKnLRRSVEASLRRLQTDYIDLLYVH-AWDFTTPVEEVMRALDDLVRAGKVLYVGIS--Dtp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 161 ------LDYIKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWPK 234
Cdd:cd19080 155 awvvarANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVTVG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1041868156 235 EKWFKD-SLNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19080 235 FGKLTErNWAIVDVVAAVAEElGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDN 290
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-288 |
5.29e-54 |
|
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: 178.20 E-value: 5.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 10 GLIVSEIGFG----SWAIGgdewgAVKD-NESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILSTKGg 84
Cdd:cd19078 1 GLEVSAIGLGcmgmSHGYG-----PPPDkEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 85 liGHHYDPNQPAVYG---DPQKIIDAFEASLLRLKTDYIDVYFCH-IwwDKHEETEAFLQAFQTLKKSGKVRAVGVSTND 160
Cdd:cd19078 75 --GFKIDGGKPGPLGldsRPEHIRKAVEGSLKRLQTDYIDLYYQHrV--DPNVPIEEVAGTMKELIKEGKIRHWGLSEAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 161 LDYIKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWP--KEKWF 238
Cdd:cd19078 151 VETIRRAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDRASLPrfTPEAL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1041868156 239 KDSLNKVEKLRSLV-RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19078 231 EANQALVDLLKEFAeEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEEN 281
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-288 |
3.70e-52 |
|
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: 171.13 E-value: 3.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 3 YRLLGNTGLIVSEIGFGSWAIGGdewgaVKDNESLDAIEKAIDLGVNFIDTADVYglGHSETLVAKAINDHRQDIILSTK 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGR-----LSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKGRRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 83 gglIGHHydpnqpavygDPQKIIDAFEASLLRLKTDYIDVYFCHI-----WWDKHEETEAFLQAFQTLKKSGKVRAVGVS 157
Cdd:cd19100 74 ---TGAR----------DYEGAKRDLERSLKRLGTDYIDLYQLHAvdteeDLDQVFGPGGALEALLEAKEEGKIRFIGIS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 158 TNDLDYIKHFNQDNDLDVVQFDYSIL---NKEPEKDILPYIEKHNLGAVIRGPLKMGiltgkfnhetqfpdddlrkdwpk 234
Cdd:cd19100 141 GHSPEVLLRALETGEFDVVLFPINPAgdhIDSFREELLPLAREKGVGVIAMKVLAGG----------------------- 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1041868156 235 eKWFKDSLNKVEKlrslvrsnrslaqvALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19100 198 -RLLSGDPLDPEQ--------------ALRYALSLPPVDVVIVGMDSPEELDEN 236
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
13-288 |
3.77e-52 |
|
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: 172.03 E-value: 3.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 13 VSEIGFGSWAIGG-DEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILSTKggLIGHHY 90
Cdd:cd19072 4 VPVLGLGTWGIGGgMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFdREDLFITTK--VSPDHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 91 DPNqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiwWDKH----EETeafLQAFQTLKKSGKVRAVGVS---TNDLDY 163
Cdd:cd19072 82 KYD---------DVIKAAKESLKRLGTDYIDLYLIH--WPNPsipiEET---LRAMEELVEEGKIRYIGVSnfsLEELEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 164 IKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETqfpdddlrkdwpkekwfkdsln 243
Cdd:cd19072 148 AQSYLKKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL---------------------- 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1041868156 244 kvekLRSLVRS-NRSLAQVALRYVLSHPAVsVAIPGAKNSTQVEEN 288
Cdd:cd19072 206 ----LDEIAKKyGKTPAQIALNWLISKPNV-IAIPKASNIEHLEEN 246
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-288 |
9.20e-52 |
|
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: 172.03 E-value: 9.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 13 VSEIGFGSWAIG---GDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND--HRQDIILSTKggLIG 87
Cdd:cd19093 2 VSPLGLGTWQWGdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKElgDRDEVVIATK--FAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 88 HHYDPNqpavygdPQKIIDAFEASLLRLKTDYIDVYFCHIWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKHF 167
Cdd:cd19093 80 LPWRLT-------RRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 168 NQ---DNDLDVV--QFDYSILNKEPEKD-ILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDD----LRKDWPKEKW 237
Cdd:cd19093 153 HKalkERGVPLAsnQVEYSLLYRDPEQNgLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRrrlfGRKNLEKVQP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1041868156 238 FKDSLNKVEKlrslvRSNRSLAQVALRYVLSHPAvsVAIPGAKNSTQVEEN 288
Cdd:cd19093 233 LLDALEEIAE-----KYGKTPAQVALNWLIAKGV--VPIPGAKNAEQAEEN 276
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-288 |
8.41e-51 |
|
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: 170.47 E-value: 8.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGGDEwgaVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND---HRQDI 77
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQ---VDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKElgwPRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 78 ILSTK--GGLIGHhyDPNQpavYGDPQK-IIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAV 154
Cdd:cd19143 78 VVSTKifWGGGGP--PPND---RGLSRKhIVEGTKASLKRLQLDYVDLVFCH-RPDPATPIEETVRAMNDLIDQGKAFYW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 155 GVSTNDLDYIKHFNQDND-LDVV-----QFDYSILNKEP-EKDILPYIEKHNLGAVIRGPLKMGILTGKFNHEtqFPDDD 227
Cdd:cd19143 152 GTSEWSAQQIEEAHEIADrLGLIppvmeQPQYNLFHRERvEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNG--IPEGS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 228 lRKDWPKEKWFKDS--------LNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19143 230 -RLALPGYEWLKDRkeelgqekIEKVRKLKPIAEElGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEEN 298
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-287 |
6.03e-49 |
|
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: 165.52 E-value: 6.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 2 EYRLLGNTGLIVSEIGFGSWAIGGdEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILST 81
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGG-LMGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 82 KGGLIghhyDPNQPAVYGdpqKIIDAFEASLLRLKTDYIDVYFCH-----------------IWWDKheeTEAFLQAFQT 144
Cdd:cd19104 80 KVRLD----PDDLGDIGG---QIERSVEKSLKRLKRDSVDLLQLHnrigderdkpvggtlstTDVLG---LGGVADAFER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 145 LKKSGKVRAVGVST-NDLDYIKHFNQDNDLDVVQFDYSILN-----KEPEK-------DILPYIEKHNLGA-VIRgPLKM 210
Cdd:cd19104 150 LRSEGKIRFIGITGlGNPPAIRELLDSGKFDAVQVYYNLLNpsaaeARPRGwsaqdygGIIDAAAEHGVGVmGIR-VLAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 211 GILTGKFNH---ETQFPDDDLRKDwpkekwfkdsLNKVEKLRSLVR-SNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVE 286
Cdd:cd19104 229 GALTTSLDRgreAPPTSDSDVAID----------FRRAAAFRALAReWGETLAQLAHRFALSNPGVSTVLVGVKNREELE 298
|
.
gi 1041868156 287 E 287
Cdd:cd19104 299 E 299
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-303 |
9.32e-46 |
|
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: 157.34 E-value: 9.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 13 VSEIGFGSWAIGGdewgavKDNESlDAIE---KAIDLGVNFIDTADVYGL-------GHSETLVAK--AINDHRQDIILS 80
Cdd:cd19094 1 VSEICLGTMTWGE------QNTEA-EAHEqldYAFDEGVNFIDTAEMYPVppspetqGRTEEIIGSwlKKKGNRDKVVLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 81 TK---GGLIGHHYDPNQPAVygDPQKIIDAFEASLLRLKTDYIDVYFCHiWWD---------------KHEETEAF---L 139
Cdd:cd19094 74 TKvagPGEGITWPRGGGTRL--DRENIREAVEGSLKRLGTDYIDLYQLH-WPDrytplfgggyytepsEEEDSVSFeeqL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 140 QAFQTLKKSGKVRAVGVStNDLDY-IKHFNQDNDLDV------VQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGI 212
Cdd:cd19094 151 EALGELVKAGKIRHIGLS-NETPWgVMKFLELAEQLGlprivsIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 213 LTGKFNHETQFPDD---DLRKDWpkEKWFKDSLNK--VEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVE 286
Cdd:cd19094 230 LTGKYLDGAARPEGgrlNLFPGY--MARYRSPQALeaVAEYVKLARKhGLSPAQLALAWVRSRPFVTSTIIGATTLEQLK 307
|
330
....*....|....*..
gi 1041868156 287 ENSSHLTRPllLDNEIE 303
Cdd:cd19094 308 ENIDAFDVP--LSDELL 322
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-288 |
1.64e-42 |
|
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: 146.98 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 13 VSEIGFGSWAI-GGDEWGAVKDNE-SLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILSTKGGLIghHY 90
Cdd:cd19088 1 VSRLGYGAMRLtGPGIWGPPADREeAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIATKGGLV--RT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 91 DPNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHIWWDKHEETEAFlQAFQTLKKSGKVRAVGVSTNDLDYIKHFNQD 170
Cdd:cd19088 79 GPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQL-GALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 171 NDLDVVQFDYSILNKEPEkDILPYIEKHNLGAVIRGPLKMGiltgkfnhetqfpddDLRKDwpkekwfkdslnkVEKLRS 250
Cdd:cd19088 158 VRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGG---------------DLAQP-------------GGLLAE 208
|
250 260 270
....*....|....*....|....*....|....*....
gi 1041868156 251 LVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19088 209 VAARlGATPAQVALAWLLARSPVMLPIPGTSSVEHLEEN 247
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-288 |
2.06e-40 |
|
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: 143.23 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 11 LIVSEIGFGSWAIGGDEWGavkDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-------RQDIILSTKG 83
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDET---DEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekggikRDEVVIVTKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 84 GLI-GHHYDPNQPAVYG---------------------DPQKIIDAFEASLLRLKTDYIDVYFCH------IWWDKHEET 135
Cdd:cd19099 78 GYIpGDGDEPLRPLKYLeeklgrglidvadsaglrhciSPAYLEDQIERSLKRLGLDTIDLYLLHnpeeqlLELGEEEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 136 EAFLQAF---QTLKKSGKVRAVGVSTNDL-----DYIKHF-------------NQDNDLDVVQFDYSILNKEPE------ 188
Cdd:cd19099 158 DRLEEAFealEEAVAEGKIRYYGISTWDGfrappALPGHLsleklvaaaeevgGDNHHFKVIQLPLNLLEPEALtekntv 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 189 ----KDILPYIEKHNLGAVIRGPLKMGILTGkfnhetqfpdddlrkdwpkekwfkdslNKVEKLRSLVRSNRSLAQVALR 264
Cdd:cd19099 238 kgeaLSLLEAAKELGLGVIASRPLNQGQLLG---------------------------ELRLADLLALPGGATLAQRALQ 290
|
330 340
....*....|....*....|....
gi 1041868156 265 YVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19099 291 FARSTPGVDSALVGMRRPEHVDEN 314
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-288 |
4.63e-40 |
|
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: 141.98 E-value: 4.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSWAIGGdEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILSTK---------- 82
Cdd:cd19152 1 PKLGFGTAPLGN-LYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELgREDYVISTKvgrllvplqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 83 ---GGLIGHHYDPNQPAVYgD--PQKIIDAFEASLLRLKTDYIDVYFCH-----IWWDKHEE------TEAFlQAFQTLK 146
Cdd:cd19152 80 vepTFEPGFWNPLPFDAVF-DysYDGILRSIEDSLQRLGLSRIDLLSIHdpdedLAGAESDEhfaqaiKGAF-RALEELR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 147 KSGKVRAVGVSTNDLDYIKHFNQDNDLDVVQF--DYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTG---KFNHET 221
Cdd:cd19152 158 EEGVIKAIGLGVNDWEVILRILEEADLDWVMLagRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGgdnFDYYEY 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041868156 222 QFPDDDLrkdwpkekwfkdsLNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19152 238 GPAPPEL-------------IARRDRIEALCEQhGVSLAAAALQFALAPPAVASVAPGASSPERVEEN 292
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-288 |
9.26e-40 |
|
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: 139.62 E-value: 9.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSWAIGGDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILSTKGGlighhydP 92
Cdd:cd19096 1 SVLGFGTMRLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGpREKFYLATKLP-------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 93 NQPAVYGDPQKIidaFEASLLRLKTDYIDVYFCH-IWWDKHEET---EAFLQAFQTLKKSGKVRAVGVSTND-LDYIKHF 167
Cdd:cd19096 74 WSVKSAEDFRRI---LEESLKRLGVDYIDFYLLHgLNSPEWLEKarkGGLLEFLEKAKKEGLIRHIGFSFHDsPELLKEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 168 NQDNDLDVVQFDYSILNKEPEKDI--LPYIEKHNLGAVIRGPLKMGILtgkfnheTQFPDDDLRKDWpkekwfkdslnkv 245
Cdd:cd19096 151 LDSYDFDFVQLQYNYLDQENQAGRpgIEYAAKKGMGVIIMEPLKGGGL-------ANNPPEALAILC------------- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1041868156 246 eklrslvRSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19096 211 -------GAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDEN 246
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-288 |
2.12e-39 |
|
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: 140.66 E-value: 2.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGGDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND-HRQDIIL 79
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGDSEELIGRWFKQNPgKREKIFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STKGGlIGHHYDPNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTN 159
Cdd:cd19144 81 ATKFG-IEKNVETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH-RVDGKTPIEKTVAAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 160 DLDYIKHFNQDNDLDVVQFDYS--ILNKE-PEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWPK-- 234
Cdd:cd19144 159 SAETLRRAHAVHPIAAVQIEYSpfSLDIErPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGDFRRMAPRfq 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 235 EKWFKDSLNKVEKLRSLV-RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19144 239 AENFPKNLELVDKIKAIAkKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEEN 293
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-288 |
1.98e-38 |
|
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: 137.84 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSWAIGGdEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILSTKGGLI------ 86
Cdd:cd19161 1 SELGLGTAGLGN-LYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKpRDEFVLSTKVGRLlkpare 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 87 ------GHHYDPNQPAVYGD--PQKIIDAFEASLLRLKTDYIDVYFCH-IWWDKHEETEAF----------LQAFQTLKK 147
Cdd:cd19161 80 gsvpdpNGFVDPLPFEIVYDysYDGIMRSFEDSLQRLGLNRIDILYVHdIGVYTHGDRKERhhfaqlmsggFKALEELKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 148 SGKVRAVGVSTNDLDYIkhfnqDNDLDVVQFD-------YSILNKEPEKDILPYIEKHNLGAVIRGPLKMGIL-TG---- 215
Cdd:cd19161 160 AGVIKAFGLGVNEVQIC-----LEALDEADLDcfllagrYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILaTGtksg 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 216 -KFNHetqfpdddlrKDWPKEKwfkdsLNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19161 235 aKFNY----------GDAPAEI-----ISRVMEIEKICDAyNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQN 294
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
6-288 |
1.40e-37 |
|
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: 135.25 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 6 LGNTGLIVSEIGFGSWAIGGDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILSTKGG 84
Cdd:cd19145 5 LGSQGLEVSAQGLGCMGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGpREKVQLATKFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 85 LigHHYDPNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCH-IwwDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDY 163
Cdd:cd19145 85 I--HEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHrI--DTTVPIEITMGELKKLVEEGKIKYIGLSEASADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 164 IKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWPKEKWFKDSLN 243
Cdd:cd19145 161 IRRAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRKSHPRFQGENLEKN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1041868156 244 KV--EKLRSLVRSNR-SLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19145 241 KVlyERVEALAKKKGcTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQN 288
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-288 |
3.53e-37 |
|
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: 133.14 E-value: 3.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 9 TGLIVSEIGFGSWAIGGDewgAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHRQDIILSTKggligh 88
Cdd:cd19138 7 DGTKVPALGQGTWYMGED---PAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVSK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 89 hydpnqpaVY---GDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKH--EETeafLQAFQTLKKSGKVRAVGVSTNDLDY 163
Cdd:cd19138 78 --------VLpsnASRQGTVRACERSLRRLGTDYLDLYLLH-WRGGVplAET---VAAMEELKKEGKIRAWGVSNFDTDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 164 IKHFNQ---DNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGiltgkfnhetQFPDDDLRKDwpkekwfkD 240
Cdd:cd19138 146 MEELWAvpgGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQG----------GLLRRGLLEN--------P 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1041868156 241 SLNKVEKlrslvRSNRSLAQVALRYVLSHPAVsVAIPGAKNSTQVEEN 288
Cdd:cd19138 208 TLKEIAA-----RHGATPAQVALAWVLRDGNV-IAIPKSGSPEHAREN 249
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-302 |
9.82e-37 |
|
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: 133.15 E-value: 9.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 3 YRLLGNTGLIVSEIGFGSWaiggDEWGAVKDNESLDAI-EKAIDLGVNFIDTADVYGL--GHSETLVAKAIND----HRQ 75
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLW----HNFGDYTSPEEARELlRTAFDLGITHFDLANNYGPppGSAEENFGRILKRdlrpYRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 76 DIILSTKGGlighhYDPnQPAVYGD--PQK-IIDAFEASLLRLKTDYIDVyFCHIWWDKH---EETeafLQAFQTLKKSG 149
Cdd:cd19089 77 ELVISTKAG-----YGM-WPGPYGDggSRKyLLASLDQSLKRMGLDYVDI-FYHHRYDPDtplEET---MTALADAVRSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 150 KVRAVGVSTNDLDYIKHFNQD-NDLDV----VQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETqfP 224
Cdd:cd19089 147 KALYVGISNYPGAKARRAIALlRELGVpliiHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGI--P 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 225 DDDLRKdwPKEKWFKDS------LNKVEKLRSLVRSN-RSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLTRPLL 297
Cdd:cd19089 225 PDSRRA--AESKFLTEEaltpekLEQLRKLNKIAAKRgQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDF 302
|
....*
gi 1041868156 298 LDNEI 302
Cdd:cd19089 303 SEEEL 307
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-308 |
3.46e-36 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 131.69 E-value: 3.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIG-GDEWGAVKDNESLD------AIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILSTKgglig 87
Cdd:cd19103 7 IALGTWSWGsGGAGGDQVFGNHLDedtlkaVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYpREDYIISTK----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 88 hhYDPNQPAVYGDPqkIIDAFEASLLRLKTDYIDVYFCHIWWDkheeTEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKHF 167
Cdd:cd19103 82 --FTPQIAGQSADP--VADMLEGSLARLGTDYIDIYWIHNPAD----VERWTPELIPLLKSGKVKHVGVSNHNLAEIKRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 168 NQ---DNDLDV--VQFDYSILNKEPEKD-ILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKdwpkeKWFKDS 241
Cdd:cd19103 154 NEilaKAGVSLsaVQNHYSLLYRSSEEAgILDYCKENGITFFAYMVLEQGALSGKYDTKHPLPEGSGRA-----ETYNPL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041868156 242 LNKVEKLRSLVRS-----NRSLAQVALRYVLSHPavSVAIPGAKNSTQVEE--NSSHLTrplLLDNEIEFIKQL 308
Cdd:cd19103 229 LPQLEELTAVMAEigakhGASIAQVAIAWAIAKG--TTPIIGVTKPHHVEDaaRAASIT---LTDDEIKELEQL 297
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-271 |
1.46e-35 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 129.89 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGgdEWGAVKDnESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH---RQDI 77
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLG--EWDLSPA-EAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSpslREKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 78 ILSTKGGLI---------GHHYDpnqpavyGDPQKIIDAFEASLLRLKTDYIDVYFCH---IWWDkHEETEAflqAFQTL 145
Cdd:COG4989 78 ELQTKCGIRlpseardnrVKHYD-------TSKEHIIASVEGSLRRLGTDYLDLLLLHrpdPLMD-PEEVAE---AFDEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 146 KKSGKVRAVGVS---TNDLDYIKHFNqDNDLDVVQFDYSILNKEP-EKDILPYIEKHNLGAVIRGPLKMGILTGKFNHET 221
Cdd:COG4989 147 KASGKVRHFGVSnftPSQFELLQSAL-DQPLVTNQIELSLLHTDAfDDGTLDYCQLNGITPMAWSPLAGGRLFGGFDEQF 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1041868156 222 QfpddDLRKdwpkekwfkdslnKVEKLRSlvRSNRSLAQVALRYVLSHPA 271
Cdd:COG4989 226 P----RLRA-------------ALDELAE--KYGVSPEAIALAWLLRHPA 256
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-296 |
1.34e-34 |
|
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: 127.09 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSWAIGgdEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILSTKgglIGHHYDP 92
Cdd:cd19162 1 PRLGLGAASLG--NLARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHpRAEYVVSTK---VGRLLEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 93 NQPAVYGDPQKIID--------AFEASLLRLKTDYIDVYFCHIWwDKHEE---TEAFlQAFQTLKKSGKVRAVGVSTNDL 161
Cdd:cd19162 76 GAAGRPAGADRRFDfsadgirrSIEASLERLGLDRLDLVFLHDP-DRHLLqalTDAF-PALEELRAEGVVGAIGVGVTDW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 162 DYIKHFNQDNDLDVVQF--DYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTgkfnheTQFPDDDlRKDW---PKEK 236
Cdd:cd19162 154 AALLRAARRADVDVVMVagRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILA------TDDPAGD-RYDYrpaTPEV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041868156 237 WfkdslNKVEKLRSLVRSNR-SLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLTRPL 296
Cdd:cd19162 227 L-----ARARRLAAVCRRYGvPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPI 282
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-288 |
1.84e-34 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 127.59 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 3 YRLLGNTGLIVSEIGFGSWAIGgDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH---RQDIIL 79
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLG-SVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALgipREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STKGGLIGHHYDPNqpavygdPQKIIDAFEASLLRLKTDYIDVYFCH-IWWDKHE----ETeafLQAFQTLKKSGKVRAV 154
Cdd:PLN02587 80 STKCGRYGEGFDFS-------AERVTKSVDESLARLQLDYVDILHCHdIEFGSLDqivnET---IPALQKLKESGKVRFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 155 GVSTNDLD---YIKHFNQDNDLDVV--QFDYSIlNKEPEKDILPYIEKHNLGAVIRGPLKMGILTgkfnhETQFPdddlr 229
Cdd:PLN02587 150 GITGLPLAiftYVLDRVPPGTVDVIlsYCHYSL-NDSSLEDLLPYLKSKGVGVISASPLAMGLLT-----ENGPP----- 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 230 kDW-PKEKWFKDSLNKVEKLRSLvrSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:PLN02587 219 -EWhPAPPELKSACAAAATHCKE--KGKNISKLALQYSLSNKDISTTLVGMNSVQQVEEN 275
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-288 |
2.64e-34 |
|
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: 125.76 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 10 GLIVSEIGFGSWAIGGDEW-GAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH-RQDIILSTKGGLIG 87
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTpDYSRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFpREDLFIVTKVWPTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 88 HHYDpnqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKHF 167
Cdd:cd19137 81 LRYD-----------DLLRSLQNSLRRLDTDYIDLYLIH-WPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 168 NQDNDLDVV--QFDYSILNKEPEKD-ILPYIEKHNLGAVIRGPLKMGILtgkfnhetqfpdddlrkdwPKekwfKDSLNK 244
Cdd:cd19137 149 ISKSQTPIVcnQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLRRGLE-------------------KT----NRTLEE 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1041868156 245 VEKlrslvRSNRSLAQVALRYVLSHPAVsVAIPGAKNSTQVEEN 288
Cdd:cd19137 206 IAK-----NYGKTIAQIALAWLIQKPNV-VAIPKAGRVEHLKEN 243
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-295 |
8.54e-32 |
|
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: 119.58 E-value: 8.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGgdEWGAVkDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDH---RQDIILSTKGG 84
Cdd:cd19092 1 PEGLEVSRLVLGCMRLA--DWGES-AEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNpglREKIEIQTKCG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 85 LI-GHHYDPNQPAVYG-DPQKIIDAFEASLLRLKTDYIDVYFCHiwwdkHE----ETEAFLQAFQTLKKSGKVRAVGVS- 157
Cdd:cd19092 78 IRlGDDPRPGRIKHYDtSKEHILASVEGSLKRLGTDYLDLLLLH-----RPdplmDPEEVAEAFDELVKSGKVRYFGVSn 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 158 --TNDLDYIKHFnQDNDLDVVQFDYSILNKEPEKD-ILPYIEKHNLGAVIRGPLKMGILTGKFNHETQfpddDLRKdwpk 234
Cdd:cd19092 153 ftPSQIELLQSY-LDQPLVTNQIELSLLHTEAIDDgTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQ----RLRA---- 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 235 ekwfkdslnKVEKLRslVRSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN----SSHLTRP 295
Cdd:cd19092 224 ---------ALEELA--EEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAvkalDIELTRE 277
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-297 |
2.77e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 117.63 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSWAIGGD-----EWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLghSETLVAKAI-NDHRQDIIlsTKgglig 87
Cdd:cd19097 1 SKLALGTAQFGLDygianKSGKPSEKEAKKILEYALKAGINTLDTAPAYGD--SEKVLGKFLkRLDKFKII--TK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 88 hhYDPNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHIWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKHF 167
Cdd:cd19097 72 --LPPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 168 NQDNDLDVVQFDYSILNKEPEK-DILPYIEKHNLGAVIRGPLKMGILTGKfnhetqfpdddlRKDWPkeKWFKDSLNKVE 246
Cdd:cd19097 150 LESFKIDIIQLPFNILDQRFLKsGLLAKLKKKGIEIHARSVFLQGLLLME------------PDKLP--AKFAPAKPLLK 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1041868156 247 KLRSLV-RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLTRPLL 297
Cdd:cd19097 216 KLHELAkKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-288 |
4.74e-31 |
|
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: 118.11 E-value: 4.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 9 TGLIVSEIGFG----SWAiggdeWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLG---HSETLVAKAINDH---RQDII 78
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR-----PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPdphANLKLLARFFRKYpeyADKVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 79 LSTKGGLIGHHYDPnqpavYGDPQKIIDAFEASLLRLK-TDYIDVYFCHIwWDKHEETEAFLQAFQTLKKSGKVRAVGVS 157
Cdd:cd19077 76 LSVKGGLDPDTLRP-----DGSPEAVRKSIENILRALGgTKKIDIFEPAR-VDPNVPIEETIKALKELVKEGKIRGIGLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 158 TNDLDYIKHFNQDNDLDVVQFDYSILNKEPEK-DILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLRKDWPK-- 234
Cdd:cd19077 150 EVSAETIRRAHAVHPIAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHLDRfn 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1041868156 235 EKWFKDSLNKVEKLRSLVRSNR-SLAQVALRYVLS-HPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19077 230 GENFEKNLKLVDALQELAEKKGcTPAQLALAWILAqSGPKIIPIPGSTTLERVEEN 285
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
16-288 |
2.41e-30 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 115.15 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIGGDEWgavkdnesLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKggLIGHHYDP 92
Cdd:COG0656 8 LGLGTWQLPGEEA--------AAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIAASgvpREELFVTTK--VWNDNHGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 93 nqpavygdpQKIIDAFEASLLRLKTDYIDVYFCHiwW---DKHEETeafLQAFQTLKKSGKVRAVGVStNdldyikhFNQ 169
Cdd:COG0656 75 ---------DDTLAAFEESLERLGLDYLDLYLIH--WpgpGPYVET---WRALEELYEEGLIRAIGVS-N-------FDP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 170 DnDLD-----------VVQFDYSILNkePEKDILPYIEKHNlgavIR----GPLKMGILtgkFNHETqfpdddlrkdwpk 234
Cdd:COG0656 133 E-HLEellaetgvkpaVNQVELHPYL--QQRELLAFCREHG----IVveaySPLGRGKL---LDDPV------------- 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 235 ekwfkdsLNKV-EKLrslvrsNRSLAQVALRYVLSHPAvsVAIPGAKNSTQVEEN 288
Cdd:COG0656 190 -------LAEIaEKH------GKTPAQVVLRWHLQRGV--VVIPKSVTPERIREN 229
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-303 |
7.31e-28 |
|
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: 109.80 E-value: 7.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 2 EYRLLGNTGLIVSEIGFGSWaiggDEWGAVKDNE-SLDAIEKAIDLGVNFIDTADVYG--LGHSET----LVAKAINDHR 74
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLW----HNFGDVDRYEnSRAMLRRAFDLGITHFDLANNYGppPGSAEEnfgrILKEDLKPYR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 75 QDIILSTKGGLighhydPNQPAVYGD---PQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKV 151
Cdd:cd19151 77 DELIISTKAGY------TMWPGPYGDwgsKKYLIASLDQSLKRMGLDYVDIFYHH-RPDPETPLEETMGALDQIVRQGKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 152 RAVGVSTNDLDYIKH-FNQDNDLDVV----QFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKFNHetQFPDD 226
Cdd:cd19151 150 LYVGISNYPPEEAREaAAILKDLGTPclihQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLN--GIPED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 227 D-LRKDW---PKEKWFKDSLNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLTRPLLLDNE 301
Cdd:cd19151 228 SrAAKGSsflKPEQITEEKLAKVRRLNEIAQArGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNREFSEEE 307
|
..
gi 1041868156 302 IE 303
Cdd:cd19151 308 LA 309
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-288 |
2.87e-27 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 108.07 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 13 VSEIGFGSWAIGGDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGlgHSETLVAKAINDHRQDIILSTKggLIGHH--- 89
Cdd:cd19101 2 ISRVINGMWQLSGGHGGIRDEDAAVRAMAAYVDAGLTTFDCADIYG--PAEELIGEFRKRLRRERDAADD--VQIHTkwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 90 YDPNQPAVygDPQKIIDAFEASLLRLKTDYID-VYFcHiWWDKheETEAFLQAFQTL---KKSGKVRAVGVsTN-DLdyi 164
Cdd:cd19101 78 PDPGELTM--TRAYVEAAIDRSLKRLGVDRLDlVQF-H-WWDY--SDPGYLDAAKHLaelQEEGKIRHLGL-TNfDT--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 165 KHFNQ--DNDLDVV--QFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKF---------NHETQfpddDLRK- 230
Cdd:cd19101 148 ERLREilDAGVPIVsnQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYlgvpeptgpALETR----SLQKy 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041868156 231 -----DWPKEKWFKDSLnkvEKLRSLVRSNR-SLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19101 224 klmidEWGGWDLFQELL---RTLKAIADKHGvSIANVAVRWVLDQPGVAGVIVGARNSEHIDDN 284
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-288 |
3.57e-27 |
|
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: 107.25 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSwAIGGDEWGAVKDNESLDAiekAIDLGVNFIDTADVYG----LGHSETLVAKAINDH--RQDIILSTKGGlig 87
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDA---FVELGGNFIDTARVYGdwveRGASERVIGEWLKSRgnRDKVVIATKGG--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 88 HHY--DPNQPAVygDPQKIIDAFEASLLRLKTDYIDVYFCHIwwDKHEET-EAFLQAFQTLKKSGKVRAVGVSTNDLDYI 164
Cdd:cd19082 74 HPDleDMSRSRL--SPEDIRADLEESLERLGTDYIDLYFLHR--DDPSVPvGEIVDTLNELVRAGKIRAFGASNWSTERI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 165 KHFN---QDNDLD---VVQFDYSI--LNKEP---------EKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQfPDDD 227
Cdd:cd19082 150 AEANayaKAHGLPgfaASSPQWSLarPNEPPwpgptlvamDEEMRAWHEENQLPVFAYSSQARGFFSKRAAGGAE-DDSE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1041868156 228 LRKDWpkekWFKDSLNKVEKLRSLVRS-NRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19082 229 LRRVY----YSEENFERLERAKELAEEkGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDS 286
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-288 |
1.41e-25 |
|
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: 101.96 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 15 EIGFGSWAIGGDEwgavkdneSLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND---HRQDIILSTKGGLIGHHYD 91
Cdd:cd19073 3 ALGLGTWQLRGDD--------CANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAEsgvPREDLFITTKVWRDHLRPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 92 pnqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDldyIKHFNQ-- 169
Cdd:cd19073 72 -----------DLKKSVDRSLEKLGTDYVDLLLIH-WPNPTVPLEETLGALKELKEAGKVKSIGVSNFT---IELLEEal 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 170 ---DNDLDVVQFDYSILnkEPEKDILPYIEKHNLGAVIRGPLKMGILtgkFNHETqfpdddlrkdwpkekwfkdslnkve 246
Cdd:cd19073 137 disPLPIAVNQVEFHPF--LYQAELLEYCRENDIVITAYSPLARGEV---LRDPV------------------------- 186
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1041868156 247 kLRSLV-RSNRSLAQVALRYVLSHPavSVAIPGAKNSTQVEEN 288
Cdd:cd19073 187 -IQEIAeKYDKTPAQVALRWLVQKG--IVVIPKASSEDHLKEN 226
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
4-305 |
2.20e-24 |
|
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: 100.58 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 4 RLLGNT-GLIVSEIGFGSWAIGgDEW----GAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAK--AINDHRQD 76
Cdd:cd19146 1 RQLSPTaGVRVSPLCLGAMSFG-EAWksmmGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEwmASRGNRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 77 IILSTK--GGLIGHHYDPNQPAVYGDPQKIID-AFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRA 153
Cdd:cd19146 80 MVLATKytTGYRRGGPIKIKSNYQGNHAKSLRlSVEASLKKLQTSYIDILYVH-WWDYTTSIPELMQSLNHLVAAGKVLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 154 VGVSTND---LDYIKHFNQDNDLD---VVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKmgilTGKFNHETQFPDDD 227
Cdd:cd19146 159 LGVSDTPawvVSKANAYARAHGLTqfvVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLG----QGQFRTEEEFKRRG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 228 --LRKDWPKEKWFKDSLNKVEKLRSlvRSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLtRPLLLDNEIEFI 305
Cdd:cd19146 235 rsGRKGGPQTEKERKVSEKLEKVAE--EKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEAL-GISLSDEEIQEI 311
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-288 |
2.68e-24 |
|
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: 98.71 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIGGDEwgaVKDnesldAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKGGLIGHHYDp 92
Cdd:cd19071 4 IGLGTYKLKPEE---TAE-----AVLAALEAGYRHIDTAAAYG---NEAEVGEAIRESgvpREELFITTKLWPTDHGYE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 93 nqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiW---WDKHEETEAFL---QAFQTLKKSGKVRAVGVStndldyikH 166
Cdd:cd19071 72 ----------RVREALEESLKDLGLDYLDLYLIH-WpvpGKEGGSKEARLetwRALEELVDEGLVRSIGVS--------N 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 167 FNQDnDLD-----------VVQFDYSILNkePEKDILPYIEKHNLGAVIRGPLKMGILtGKFNHETqfpdddlrkdwpke 235
Cdd:cd19071 133 FNVE-HLEellaaarikpaVNQIELHPYL--QQKELVEFCKEHGIVVQAYSPLGRGRR-PLLDDPV-------------- 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1041868156 236 kwfkdsLNKVEKlrslvRSNRSLAQVALRYVLSHPavSVAIPGAKNSTQVEEN 288
Cdd:cd19071 195 ------LKEIAK-----KYGKTPAQVLLRWALQRG--VVVIPKSSNPERIKEN 234
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-307 |
3.42e-24 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 100.45 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWaiggDEWGAVKDNESLDAI-EKAIDLGVNFIDTADVYG--LGHSETLVAKAIND----H 73
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLW----HNFGHVNALESQRAIlRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdfaaY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 74 RQDIILSTKGGlighhYD--PNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKV 151
Cdd:PRK09912 89 RDELIISTKAG-----YDmwPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSH-RVDENTPMEETASALAHAVQSGKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 152 RAVGVSTNDLDYIKHFNQ-----DNDLDVVQFDYSILNKEPEKD-ILPYIEKHNLGAVIRGPLKMGILTGKFNHetQFPD 225
Cdd:PRK09912 163 LYVGISSYSPERTQKMVEllrewKIPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYLN--GIPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 226 DD-LRKDWPKEKWFKDSLNKVEKLRSLVRSN-------RSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLTRPLL 297
Cdd:PRK09912 241 DSrMHREGNKVRGLTPKMLTEANLNSLRLLNemaqqrgQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLTF 320
|
330
....*....|
gi 1041868156 298 LDNEIEFIKQ 307
Cdd:PRK09912 321 STEELAQIDQ 330
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-302 |
1.32e-23 |
|
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: 97.99 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 4 RLLGNTGLIVSEIGFGSWAIGGDEWGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND---HRQDIILS 80
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAAlqvPRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 81 TKGGLIG---HHYdpnqpavygDPQKIIDAFEASLLRLKTDYIDVYFCHI--WWDKHEETEAFLQAFQTLKKSGKVRAVG 155
Cdd:cd19153 83 TKVGRYRdseFDY---------SAERVRASVATSLERLHTTYLDVVYLHDieFVDYDTLVDEALPALRTLKDEGVIKRIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 156 VSTNDLDYIKHFNQDND---LDVVQfDYSILNKEPEK--DILPYIEKHNLGAVIRG-PLKMGILTgkfnheTQFPdddlr 229
Cdd:cd19153 154 IAGYPLDTLTRATRRCSpgsLDAVL-SYCHLTLQDARleSDAPGLVRGAGPHVINAsPLSMGLLT------SQGP----- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 230 KDW-PKEKWFKDSLNKVEKLRSLVrsNRSLAQVALRYVLS-HPAVSVAIPGAKNSTQVEENSSHLTRPLLLDNEI 302
Cdd:cd19153 222 PPWhPASGELRHYAAAADAVCASV--EASLPDLALQYSLAaHAGVGTVLLGPSSLAQLRSMLAAVDAVASLGAAI 294
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
23-308 |
2.75e-23 |
|
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: 97.24 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 23 IGGDEWGAVKDNESLDAIEKAIDL----GVNFIDTADVYGLGHSETLVAKAiNDHRQDIILSTK--GGLIGHHydpnqpa 96
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAflerGHTEIDTARVYPDGTSEELLGEL-GLGERGFKIDTKanPGVGGGL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 97 vygDPQKIIDAFEASLLRLKTDYIDVYFCHIWWDKH--EETeafLQAFQTLKKSGKVRAVGVStN----DLDYIKHFNQD 170
Cdd:cd19075 77 ---SPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTplEET---LAAIDELYKEGKFKEFGLS-NysawEVAEIVEICKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 171 NDL---DVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLKMGILTGKF-NHETQ------FPDDDLRKdWPKEKWFKD 240
Cdd:cd19075 150 NGWvlpTVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYkYSEDKagggrfDPNNALGK-LYRDRYWKP 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 241 SLNK-VEKLRSLVRSNR-SLAQVALRYVLSHPAVSVA-----IPGAKNSTQVEENSSHLTRPLLLDNEIEFIKQL 308
Cdd:cd19075 229 SYFEaLEKVEEAAEKEGiSLAEAALRWLYHHSALDGEkgdgvILGASSLEQLEENLAALEKGPLPEEVVKAIDEA 303
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-288 |
2.85e-23 |
|
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: 97.14 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 3 YRLLGNTGLIVSEIGFGSW-AIGGDEWGAVKDneslDAIEKAIDLGVNFIDTADVYG--LGHSET----LVAKAINDHRQ 75
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWhNFGDDTPLETQR----AILRTAFDLGITHFDLANNYGppPGSAEEnfgrILREDFAGYRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 76 DIILSTKGGlighhYD--PNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRA 153
Cdd:cd19150 78 ELIISTKAG-----YDmwPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSH-RFDPDTPLEETMGALDHAVRSGKALY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 154 VGVSTND-------LDYIKHFNqdNDLDVVQFDYSILNKEPEKD-ILPYIEKHNLGAVIRGPLKMGILTGKF-------- 217
Cdd:cd19150 152 VGISSYSpertreaAAILRELG--TPLLIHQPSYNMLNRWVEESgLLDTLQELGVGCIAFTPLAQGLLTDKYlngipegs 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041868156 218 --NHETQFPDDDLRKDwpkekwfkdSLNKVEKLRSLV-RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19150 230 raSKERSLSPKMLTEA---------NLNSIRALNEIAqKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEEN 294
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-288 |
3.79e-23 |
|
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: 97.03 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGGdewGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND---HRQDI 77
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 78 ILSTKggligHHYDPNQPAVYGDPQK-IIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGV 156
Cdd:cd19159 78 VITTK-----LYWGGKAETERGLSRKhIIEGLKGSLQRLQLEYVDVVFAN-RPDSNTPMEEIVRAMTHVINQGMAMYWGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 157 ST-NDLDYIKHFNQDNDLDVV-----QFDYSILNKEPEKDILPYI-EKHNLGAVIRGPLKMGILTGKFnhETQFPDDDlR 229
Cdd:cd19159 152 SRwSAMEIMEAYSVARQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKY--GNGVPESS-R 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1041868156 230 KDWPKEKWFKDSLNKVE------KLRSLV----RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19159 229 ASLKCYQWLKERIVSEEgrkqqnKLKDLSpiaeRLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIEN 297
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-288 |
3.81e-23 |
|
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: 96.75 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 3 YRLLGNTGLIVSEIGFGSWAIGGdewGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND---HRQDIIL 79
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFG---SQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKkgwRRSSYVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STK---GGlighhydpNQPAVYGDPQK-IIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVG 155
Cdd:cd19141 79 TTKifwGG--------KAETERGLSRKhIIEGLKASLERLQLEYVDIVFAN-RPDPNTPMEEIVRAFTHVINQGMAMYWG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 156 VST-NDLDYIKHFN---QDNDLD--VVQFDYSILNKEPEKDILPYI-EKHNLGAVIRGPLKMGILTGKFNHETQFPDDDL 228
Cdd:cd19141 150 TSRwSAMEIMEAYSvarQFNLIPpiVEQAEYHLFQREKVEMQLPELfHKIGVGAMTWSPLACGILSGKYDDGVPEYSRAS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041868156 229 RK--DWPKEKWFKDSLNKVE-KLRSLV----RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19141 230 LKgyQWLKEKILSEEGRRQQaKLKELQiiadRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYEN 296
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
37-288 |
4.62e-22 |
|
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: 93.50 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 37 LDAIEKAIDLGVNFIDTADVYGlgHSETLVAKAI----NDH-RQDIILSTKGGLIG---HHYDPnqpavygdpQKIIDAF 108
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYG--PSEIILGRALkalrDEFpRDTYFIITKVGRYGpddFDYSP---------EWIRASV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 109 EASLLRLKTDYIDVYFCH-IWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLD-------YIKHfnQDND-LDVVqFD 179
Cdd:cd19164 106 ERSLRRLHTDYLDLVYLHdVEFVADEEVLEALKELFKLKDEGKIRNVGISGYPLPvllrlaeLART--TAGRpLDAV-LS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 180 YSILNkePEKDILP-YIEK-HNLGAVIR----GPLKMGILTgkfnheTQFPdddlrKDW-PKEKWFKDSLNKVEKLrsLV 252
Cdd:cd19164 183 YCHYT--LQNTTLLaYIPKfLAAAGVKVvlnaSPLSMGLLR------SQGP-----PEWhPASPELRAAAAKAAEY--CQ 247
|
250 260 270
....*....|....*....|....*....|....*..
gi 1041868156 253 RSNRSLAQVALRYVLSH-PAVSVAIPGAKNSTQVEEN 288
Cdd:cd19164 248 AKGTDLADVALRYALREwGGEGPTVVGCSNVDELEEA 284
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-288 |
9.50e-22 |
|
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: 93.23 E-value: 9.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGGdewGAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND---HRQDI 77
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFG---GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 78 ILSTK---GGlighhydpNQPAVYGDPQK-IIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRA 153
Cdd:cd19158 78 VITTKifwGG--------KAETERGLSRKhIIEGLKASLERLQLEYVDVVFAN-RPDPNTPMEETVRAMTHVINQGMAMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 154 VGVST-NDLDYIKHFNQDNDLDVV-----QFDYSILNKEPEKDILPYI-EKHNLGAVIRGPLKMGILTGKFNheTQFPDD 226
Cdd:cd19158 149 WGTSRwSSMEIMEAYSVARQFNLIppiceQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKYD--SGIPPY 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1041868156 227 DlRKDWPKEKWFKDSL---------NKVEKLRSLV-RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19158 227 S-RASLKGYQWLKDKIlseegrrqqAKLKELQAIAeRLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMEN 297
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-288 |
1.32e-19 |
|
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: 87.35 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGGDEwgaVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAIND---HRQDI 77
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQ---ISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 78 ILSTK---GGlighhydpNQPAVYGDPQK-IIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRA 153
Cdd:cd19160 80 VVTTKiywGG--------QAETERGLSRKhIIEGLRGSLDRLQLEYVDIVFAN-RSDPNSPMEEIVRAMTYVINQGMAMY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 154 VGVST-NDLDYIKHFNQDNDLDVV-----QFDYSILNKEPEKDILPYI-EKHNLGAVIRGPLKMGILTGKFnhETQFPDD 226
Cdd:cd19160 151 WGTSRwSAMEIMEAYSVARQFNLIppvceQAEYHLFQREKVEMQLPELyHKIGVGSVTWSPLACGLITGKY--DGRVPDT 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1041868156 227 DlRKDWPKEKWFKDSLN---------KVEKLRSLV-RSNRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEEN 288
Cdd:cd19160 229 C-RAAVKGYQWLKEKVQseegkkqqaKVKELHPIAdRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEN 299
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-157 |
1.41e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 86.62 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 14 SEIGFGSWAIGGdewgAVKDNESLDAIEKAIDLGVNFIDTADVYGL-------GHSETLVAKAINDH--RQDIILSTKGG 84
Cdd:cd19752 1 SELCLGTMYFGT----RTDEETSFAILDRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKDRgnRDDVVIATKVG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041868156 85 liGHHYDPNQPAV--YG-DPQKIIDAFEASLLRLKTDYIDVYFCHIwWDKHEETEAFLQAFQTLKKSGKVRAVGVS 157
Cdd:cd19752 77 --AGPRDPDGGPEspEGlSAETIEQEIDKSLRRLGTDYIDLYYAHV-DDRDTPLEETLEAFNELVKAGKVRAIGAS 149
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-288 |
2.20e-19 |
|
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: 85.39 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 10 GLIVSEIGFGSWAIGGDEwgavkdneSLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKgglI 86
Cdd:cd19140 5 GVRIPALGLGTYPLTGEE--------CTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAASgvpRDELFLTTK---V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 87 GHHYDPnqpavygdPQKIIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVStndldyikH 166
Cdd:cd19140 71 WPDNYS--------PDDFLASVEESLRKLRTDYVDLLLLH-WPNKDVPLAETLGALNEAQEAGLARHIGVS--------N 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 167 FNQ----------DNDLDVVQFDYSI-LNKEPekdILPYIEKHNLGAVIRGPLKMGiltgkfnhetQFPDDDLrkdwpke 235
Cdd:cd19140 134 FTVallreavelsEAPLFTNQVEYHPyLDQRK---LLDAAREHGIALTAYSPLARG----------EVLKDPV------- 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1041868156 236 kwfkdsLNKVEKlrslvRSNRSLAQVALRYVLSHPAVsVAIPGAKNSTQVEEN 288
Cdd:cd19140 194 ------LQEIGR-----KHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEEN 234
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
16-289 |
4.51e-19 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 84.68 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIGGdewgavkdnESLDAIEKAI-DLGVNFIDTADVYGlghSETLVAKAIND---HRQDIILSTKgglighhyd 91
Cdd:cd19135 16 LGLGTSHSGG---------YSHEAVVYALkECGYRHIDTAKRYG---CEELLGKAIKEsgvPREDLFLTTK--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 92 pNQPAVYGDpQKIIDAFEASLLRLKTDYIDVYFCHiwW--------DKHEETEAFLQAFQTLKKSGKVRAVGVStNDLdy 163
Cdd:cd19135 75 -LWPSDYGY-ESTKQAFEASLKRLGVDYLDLYLLH--WpdcpssgkNVKETRAETWRALEELYDEGLCRAIGVS-NFL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 164 IKHFNQ-DNDLDVV----QFDYSILNkePEKDILPYIEKHNLgaVIRG--PLKMGILtgkFNHETqfpdddlrkdwpkek 236
Cdd:cd19135 148 IEHLEQlLEDCSVVphvnQVEFHPFQ--NPVELIEYCRDNNI--VFEGycPLAKGKA---LEEPT--------------- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1041868156 237 wfkdslnkVEKLRSlvRSNRSLAQVALRYVLSHPAvsVAIPGAKNSTQVEENS 289
Cdd:cd19135 206 --------VTELAK--KYQKTPAQILIRWSIQNGV--VTIPKSTKEERIKENC 246
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-290 |
3.72e-18 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 82.44 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEwgavkdnESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAI---NDHRQDIILSTKGG 84
Cdd:cd19157 5 NNGVKMPWLGLGVFKVEEGS-------EVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIkesGIPREELFITSKVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 85 LIGHHYDpnqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiwWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYI 164
Cdd:cd19157 75 NADQGYD-----------STLKAFEASLERLGLDYLDLYLIH--WPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 165 KHFNQDNDLD--VVQFDYSilNKEPEKDILPYIEKHNLGAVIRGPLKMGiltgkfnhetQFPDDDLRKDWPKekwfkdsl 242
Cdd:cd19157 142 EDLLADAEIVpmVNQVEFH--PRLTQKELRDYCKKQGIQLEAWSPLMQG----------QLLDNPVLKEIAE-------- 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1041868156 243 nkveklrslvRSNRSLAQVALRYVLSHPAVSvaIPGAKNSTQVEENSS 290
Cdd:cd19157 202 ----------KYNKSVAQVILRWDLQNGVVT--IPKSIKEHRIIENAD 237
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-157 |
7.20e-18 |
|
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: 81.26 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEWGAvkdnesldAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKGG 84
Cdd:cd19131 5 NDGNTIPQLGLGVWQVSNDEAAS--------AVREALEVGYRSIDTAAIYG---NEEGVGKAIRASgvpREELFITTKLW 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041868156 85 LIGHHYDpnqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiwW-----DKHEETeafLQAFQTLKKSGKVRAVGVS 157
Cdd:cd19131 74 NSDQGYD-----------STLRAFDESLRKLGLDYVDLYLIH--WpvpaqDKYVET---WKALIELKKEGRVKSIGVS 135
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-157 |
1.47e-17 |
|
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: 80.39 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEwgAVKdnesldAIEKAIDLGVNFIDTADVYglgHSETLVAKAINDH---RQDIILSTKgg 84
Cdd:cd19132 2 NDGTQIPAIGFGTYPLKGDE--GVE------AVVAALQAGYRLLDTAFNY---ENEGAVGEAVRRSgvpREELFVTTK-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 85 LIG--HHYDpnqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiwW-----DKHeeTEAFlQAFQTLKKSGKVRAVGVS 157
Cdd:cd19132 69 LPGrhHGYE-----------EALRTIEESLYRLGLDYVDLYLIH--WpnpsrDLY--VEAW-QALIEAREEGLVRSIGVS 132
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
16-274 |
3.27e-17 |
|
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: 79.58 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGS---WAIGGDewgAVKDNESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKgglighh 89
Cdd:cd19120 7 IAFGTgtaWYKSGD---DDIQRDLVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALKESgvpREDLFITTK------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 90 YDPNQPAVYGdpqkiidAFEASLLRLKTDYIDVYFCHI-WWDKHEET--EAFLQAFQTLKKSGKVRAVGVSTNDLDYIKH 166
Cdd:cd19120 74 VSPGIKDPRE-------ALRKSLAKLGVDYVDLYLIHSpFFAKEGGPtlAEAWAELEALKDAGLVRSIGVSNFRIEDLEE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 167 FNQDNDL--DVVQFDYSILNKEPEKDILPYIEKHnlgavirgplkmGILTGKF---NHETQFPDDDLrkdwpkekwfKDS 241
Cdd:cd19120 147 LLDTAKIkpAVNQIEFHPYLYPQQPALLEYCREH------------GIVVSAYsplSPLTRDAGGPL----------DPV 204
|
250 260 270
....*....|....*....|....*....|...
gi 1041868156 242 LNKVEKlrslvRSNRSLAQVALRYVLSHPAVSV 274
Cdd:cd19120 205 LEKIAE-----KYGVTPAQVLLRWALQKGIVVV 232
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-307 |
3.51e-17 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 80.67 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIGgdewgavKDNESLDA---IEKAIDLGVNFIDTADVYGL-------GHSETLVAKAI 70
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFG-------EQNSEADAhaqLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 71 NDH--RQDIILSTK-GGLIGHHYDPNQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHiwWDKhEETEAF--------- 138
Cdd:PRK10625 74 AKRgsREKLIIASKvSGPSRNNDKGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVH--WPQ-RPTNCFgklgyswtd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 139 ----------LQAFQTLKKSGKVRAVGVSTND----LDYIkHFNQDNDLD---VVQFDYSILNKEPEKDILPYIEKHNLG 201
Cdd:PRK10625 151 sapavslletLDALAEQQRAGKIRYIGVSNETafgvMRYL-HLAEKHDLPrivTIQNPYSLLNRSFEVGLAEVSQYEGVE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 202 AVIRGPLKMGILTGKFNHETQFPD--DDLRKDWPKEKWFKDSLNKVEKLRSLVRSNRSLAQVALRYVLSHPAVSVAIPGA 279
Cdd:PRK10625 230 LLAYSCLAFGTLTGKYLNGAKPAGarNTLFSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330 340 350
....*....|....*....|....*....|
gi 1041868156 280 KNSTQVEEN--SSHLTRPLLLDNEIEFIKQ 307
Cdd:PRK10625 310 TTMEQLKTNieSLHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-288 |
1.18e-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: 78.48 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEWGAvkdneslDAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND-------HRQDIILS 80
Cdd:cd19116 6 NDGNEIPAIALGTWKLKDDEGVR-------QAVKHAIEAGYRHIDTAYLYG---NEAEVGEAIREkiaegvvKREDLFIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 81 TKggLIGHHYDPNQpavygdpqkIIDAFEASLLRLKTDYIDVYFCHI----------WWDKHEETE--AFL---QAFQTL 145
Cdd:cd19116 76 TK--LWNSYHEREQ---------VEPALRESLKRLGLDYVDLYLIHWpvafkenndsESNGDGSLSdiDYLetwRGMEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 146 KKSGKVRAVGVSTNDLDYIKHFNQDNDLD--VVQFDYSILNKepEKDILPYIEKHNLGAVIRGPLkmGILtgkfnhetqf 223
Cdd:cd19116 145 VKLGLTRSIGVSNFNSEQINRLLSNCNIKpaVNQIEVHPTLT--QEKLVAYCQSNGIVVMAYSPF--GRL---------- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041868156 224 pddDLRKDWPKEKWFKDslnkvEKLRSLVRS-NRSLAQVALRYVLSHPAVSvaIPGAKNSTQVEEN 288
Cdd:cd19116 211 ---VPRGQTNPPPRLDD-----PTLVAIAKKyGKTTAQIVLRYLIDRGVVP--IPKSSNKKRIKEN 266
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-288 |
2.13e-16 |
|
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: 77.09 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGgdewgavKDNESLDAIEKAIDLGVNFIDTADVYglgHSETLVAKAINDH---RQDIILSTKgg 84
Cdd:cd19126 4 NNGTRMPWLGLGVFQTP-------DGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESgvpREELFVTTK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 85 lighhydpnqpaVYGDPQ---KIIDAFEASLLRLKTDYIDVYFCHiwW---DKHEETeafLQAFQTLKKSGKVRAVGVST 158
Cdd:cd19126 72 ------------LWNDDQrarRTEDAFQESLDRLGLDYVDLYLIH--WpgkDKFIDT---WKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 159 NDLDYIKHFNQDNDLD--VVQFDYS-ILNKepeKDILPYIEKHNLGAVIRGPLKMGILTgkfnhetqfpdDDLRKDWPKE 235
Cdd:cd19126 135 FQEHHLEELLAHADVVpaVNQVEFHpYLTQ---KELRGYCKSKGIVVEAWSPLGQGGLL-----------SNPVLAAIGE 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1041868156 236 KWfkdslnkveklrslvrsNRSLAQVALRYVLSHPAVSvaIPGAKNSTQVEEN 288
Cdd:cd19126 201 KY-----------------GKSAAQVVLRWDIQHGVVT--IPKSVHASRIKEN 234
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-292 |
2.21e-16 |
|
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: 78.27 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNTGLIVSEIGFGSWAIggdeWGAVKDNESLDAI-EKAIDLGVNFIDTADVYGLGHSETLVAKAI---NDHRQD 76
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWST----FSTAISEEQAEEIvTLAYENGINYFDTSDAFTSGQAETELGRILkkkGWKRSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 77 IILSTKgglIGHHYDPNQPAVygDPQKIIDAFEASLLRLKTDYIDVYFCHIwWDKHEETEAFLQAFQTLKKSGKVRAVGV 156
Cdd:cd19142 77 YIVSTK---IYWSYGSEERGL--SRKHIIESVRASLRRLQLDYIDIVIIHK-ADPMCPMEEVVRAMSYLIDNGLIMYWGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 157 ST-NDLDYIKHFNQDNDLDVV-----QFDYSILNKEP-EKDILPYIEKHNLGAVIRGPLKMGILTGKFNHETQFPDDDLR 229
Cdd:cd19142 151 SRwSPVEIMEAFSIARQFNCPtpiceQSEYHMFCREKmELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSF 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1041868156 230 K--DWPKEKWFKDSLNKV----EKLRSLV----RSNRSLAQVALRYVLSHPAVSVAIPGAknsTQVEENSSHL 292
Cdd:cd19142 231 KssKYKVGSDGNGIHEETrrasHKLRELSliaeRLGCDLTQLLIAWSLKNENVQCVLIGA---SSLEQLYSQL 300
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
10-305 |
4.21e-16 |
|
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: 77.17 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 10 GLIVSEIGFGSWAIGgDEW----GAVKDNESLDAIEKAIDLGVNFIDTADVYGLGHSETLVAK--AINDHRQDIILSTKG 83
Cdd:cd19147 7 GIRVSPLILGAMSIG-DAWsgfmGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEwmKSRKNRDQIVIATKF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 84 GLIGHHYDPNQPAV--YGDPQK--IIDAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFLQAFQTLKKSGKVRAVGVS-- 157
Cdd:cd19147 86 TTDYKAYEVGKGKAvnYCGNHKrsLHVSVRDSLRKLQTDWIDILYVH-WWDYTTSIEEVMDSLHILVQQGKVLYLGVSdt 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 158 ----TNDLDYIKHFNQDNDLDVVQFDYSILNKEPEKDILPyIEKHNLGAVIRGPLKMGiltGKFN-----HETQFPDDDL 228
Cdd:cd19147 165 pawvVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIP-MARHFGMALAPWDVLGG---GKFQskkavEERKKNGEGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 229 R------KDWPKEKWFKDSLNKVEKLRSLvrsnRSLAQVALRYVLSHPAVSVAIPGAKNSTQVEENSSHLTRPLLLDnEI 302
Cdd:cd19147 241 RsfvggtEQTPEEVKISEALEKVAEEHGT----ESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPE-EI 315
|
...
gi 1041868156 303 EFI 305
Cdd:cd19147 316 EYL 318
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-308 |
9.09e-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: 75.30 E-value: 9.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEwgavkdnESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKGG 84
Cdd:cd19133 4 NNGVEMPILGFGVFQIPDPE-------ECERAVLEAIKAGYRLIDTAAAYG---NEEAVGRAIKKSgipREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 85 LIGHHYDpnqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiwWDKHEETEAFlQAFQTLKKSGKVRAVGVSTNDLDYI 164
Cdd:cd19133 74 IQDAGYE-----------KAKKAFERSLKRLGLDYLDLYLIH--QPFGDVYGAW-RAMEELYKEGKIRAIGVSNFYPDRL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 165 KHFNQDNDLD--VVQFDYSILNKEPEkdILPYIEKHNLGAVIRGPLKMGiLTGKFNHETqfpdddlrkdwpkekwfkdsl 242
Cdd:cd19133 140 VDLILHNEVKpaVNQIETHPFNQQIE--AVEFLKKYGVQIEAWGPFAEG-RNNLFENPV--------------------- 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041868156 243 nkvekLRSLVRS-NRSLAQVALRYVLSHPAvsVAIPGAKNSTQVEENSS----HLTrplllDNEIEFIKQL 308
Cdd:cd19133 196 -----LTEIAEKyGKSVAQVILRWLIQRGI--VVIPKSVRPERIAENFDifdfELS-----DEDMEAIAAL 254
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-288 |
2.18e-14 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 72.06 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAiggdewgaVKDNESLDAIEKAIDLGVNFIDTADVYglgHSETLVAKAINDH-------RQDIILS 80
Cdd:cd19154 7 SNGVKMPLIGLGTWQ--------SKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAELleegvvkREDLFIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 81 TKGGLIGHHydpnqpavygdPQKIIDAFEASLLRLKTDYIDVYFCHIWWD-KHEETEAFL-----------------QAF 142
Cdd:cd19154 76 TKLWTHEHA-----------PEDVEEALRESLKKLQLEYVDLYLIHAPAAfKDDEGESGTmengmsihdavdvedvwRGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 143 QTLKKSGKVRAVGVSTNDLDYIKHF--NQDNDLDVVQFDYSILnkEPEKDILPYIEKHNLGAVIRGPLKMgilTGKFNHE 220
Cdd:cd19154 145 EKVYDEGLTKAIGVSNFNNDQIQRIldNARVKPHNNQVECHLY--FPQKELVEFCKKHNISVTSYATLGS---PGRANFT 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041868156 221 TQfpdddlRKDWPKEKWFKDSLnkVEKLRSlvRSNRSLAQVALRYVLSHpAVSVaIPGAKNSTQVEEN 288
Cdd:cd19154 220 KS------TGVSPAPNLLQDPI--VKAIAE--KHGKTPAQVLLRYLLQR-GIAV-IPKSATPSRIKEN 275
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-169 |
2.49e-14 |
|
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: 71.51 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIGGDEwgavkdnESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND-------HRQDIILSTKGGLIGH 88
Cdd:cd19136 4 LGLGTFRLRGEE-------EVRQAVDAALKAGYRLIDTASVYR---NEADIGKALRDllpkyglSREDIFITSKLAPKDQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 89 HYDpnqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiwW----------DKHEETEA-FLQAFQTLKKSGKVRAVGVS 157
Cdd:cd19136 74 GYE-----------KARAACLGSLERLGTDYLDLYLIH--WpgvqglkpsdPRNAELRReSWRALEDLYKEGKLRAIGVS 140
|
170
....*....|...
gi 1041868156 158 tndlDY-IKHFNQ 169
Cdd:cd19136 141 ----NYtVRHLEE 149
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-157 |
5.80e-14 |
|
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: 70.51 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEwgavkdneSLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKGG 84
Cdd:cd19127 4 NNGVEMPALGLGVFQTPPEE--------TADAVATALADGYRLIDTAAAYG---NEREVGEGIRRSgvdRSDIFVTTKLW 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1041868156 85 LIGHHYDpnqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiwWDKHEETEAFLQAFQTLKK---SGKVRAVGVS 157
Cdd:cd19127 73 ISDYGYD-----------KALRGFDASLRRLGLDYVDLYLLH--WPVPNDFDRTIQAYKALEKllaEGRVRAIGVS 135
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-157 |
8.17e-14 |
|
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: 69.69 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAiggdewgaVKDNESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKgglighhydp 92
Cdd:cd19139 4 FGLGTFR--------LKDDVVIDSVRTALELGYRHIDTAQIYD---NEAAVGQAIAESgvpRDELFITTK---------- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041868156 93 nqpaVYGD---PQKIIDAFEASLLRLKTDYIDVYFCHiwW---DKHEETEAFLQAFQTLKKSGKVRAVGVS 157
Cdd:cd19139 63 ----IWIDnlsKDKLLPSLEESLEKLRTDYVDLTLIH--WpspNDEVPVEEYIGALAEAKEQGLTRHIGVS 127
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
16-288 |
1.54e-12 |
|
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: 66.75 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIGGDEWGAvkdnesldAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH-------RQDIILSTKggligh 88
Cdd:cd19111 7 IGLGTYQSPPEEVRA--------AVDYALFVGYRHIDTALSYQ---NEKAIGEALKWWlkngklkREEVFITTK------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 89 hydpnQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCHIWW------DKHE------ETEAFLQAFQTLKKSGKVRAVGV 156
Cdd:cd19111 70 -----LPPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHHPCgfvnkkDKGErelassDVTSVWRAMEALVSEGKVKSIGL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 157 STNDLDYIkhfnqDNDLDVVQFDYSILNKE-----PEKDILPYIEKHNLGAVIRGPLKMgilTGKFNHETQFPDDDLRKD 231
Cdd:cd19111 145 SNFNPRQI-----NKILAYAKVKPSNLQLEchaylQQRELRKFCNKKNIVVTAYAPLGS---PGRANQSLWPDQPDLLED 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1041868156 232 wPKekwfkdsLNKVEKlrslvRSNRSLAQVALRYVLSHPavSVAIPGAKNSTQVEEN 288
Cdd:cd19111 217 -PT-------VLAIAK-----ELDKTPAQVLLRFVLQRG--TGVLPKSTNKERIEEN 258
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-165 |
2.54e-12 |
|
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: 65.98 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAiggdewgaVKDNESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKGG 84
Cdd:cd19117 9 NTGAEIPAVGLGTWQ--------SKPNEVAKAVEAALKAGYRHIDTAAIYG---NEEEVGQGIKDSgvpREEIFITTKLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 85 LIGHHydpnqpavygDPQKIIDAfeaSLLRLKTDYIDVYFCHiwW-------------------DKHEETEAFLQA---F 142
Cdd:cd19117 78 CTWHR----------RVEEALDQ---SLKKLGLDYVDLYLMH--WpvpldpdgndflfkkddgtKDHEPDWDFIKTwelM 142
|
170 180
....*....|....*....|...
gi 1041868156 143 QTLKKSGKVRAVGVSTNDLDYIK 165
Cdd:cd19117 143 QKLPATGKVKAIGVSNFSIKNLE 165
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
10-288 |
1.72e-11 |
|
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: 63.31 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 10 GLIVSEIGFGSWAiggdewgaVKD-NESLDAIEKAIDLGVNFIDTADVYglgHSETLVAKAINDH---RQDIILSTKGGL 85
Cdd:cd19156 6 GVEMPRLGLGVWR--------VQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESgvpREEVFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 86 IGHHYDpnqpavygdpqKIIDAFEASLLRLKTDYIDVYFCHiwW---DKHEETeafLQAFQTLKKSGKVRAVGVSTNDLD 162
Cdd:cd19156 75 SDQGYE-----------STLAAFEESLEKLGLDYVDLYLIH--WpvkGKFKDT---WKAFEKLYKEKKVRAIGVSNFHEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 163 YIKHFNQDNDLD--VVQFD-YSILNKEPEKDilpYIEKHNLGAVIRGPLKMGILTGkfNHEtqfpdddlrkdwpkekwfk 239
Cdd:cd19156 139 HLEELLKSCKVApmVNQIElHPLLTQEPLRK---FCKEKNIAVEAWSPLGQGKLLS--NPV------------------- 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1041868156 240 dsLNKVEKlrslvRSNRSLAQVALRYVLSHPavSVAIPGAKNSTQVEEN 288
Cdd:cd19156 195 --LKAIGK-----KYGKSAAQVIIRWDIQHG--IITIPKSVHEERIQEN 234
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
10-157 |
1.41e-10 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 10 GLIVSEIGFGSWAiggdewgaVKDNESLDAIEKAIDLGVNFIDTADVYglgHSETLVAKAINDH---RQDIILSTKggli 86
Cdd:PRK11565 12 GNVMPQLGLGVWQ--------ASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEAsvaREELFITTK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 87 ghhydpnqpaVYGDPQKIID-AFEASLLRLKTDYIDVYFCHiWWDKHEETeaFLQAFQ---TLKKSGKVRAVGVS 157
Cdd:PRK11565 77 ----------LWNDDHKRPReALEESLKKLQLDYVDLYLMH-WPVPAIDH--YVEAWKgmiELQKEGLIKSIGVC 138
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-166 |
2.62e-10 |
|
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: 59.85 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGdewGAVKDnesldAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND------HRQDIILST 81
Cdd:cd19121 7 NTGASIPAVGLGTWQAKA---GEVKA-----AVAHALKIGYRHIDGALCYQ---NEDEVGEGIKEaiaggvKREDLFVTT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 82 KggLIGHHYDpnqpavygDPQKIIDAfeaSLLRLKTDYIDVYFCH------------------------IWWDKHEETEA 137
Cdd:cd19121 76 K--LWSTYHR--------RVELCLDR---SLKSLGLDYVDLYLVHwpvllnpngnhdlfptlpdgsrdlDWDWNHVDTWK 142
|
170 180
....*....|....*....|....*....
gi 1041868156 138 FLQAfqtLKKSGKVRAVGVSTNDLDYIKH 166
Cdd:cd19121 143 QMEK---VLKTGKTKAIGVSNYSIPYLEE 168
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-157 |
2.69e-10 |
|
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: 60.05 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEWGavkdneslDAIEKAIDLGVNFIDTADVY------GLGHSETLVAKAINdhRQDIILST 81
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVG--------NAVKTAIKEGYRHIDCAAIYgnekeiGKALKKLFEDGVVK--REDLFITS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 82 KGGLIGHhydpnqpavygDPQKIIDAFEASLLRLKTDYIDVYFCHiwW-------DKHEETEAFLQ--------AFQTLK 146
Cdd:cd19125 76 KLWCTDH-----------APEDVPPALEKTLKDLQLDYLDLYLIH--WpvrlkkgAHMPEPEEVLPpdipstwkAMEKLV 142
|
170
....*....|.
gi 1041868156 147 KSGKVRAVGVS 157
Cdd:cd19125 143 DSGKVRAIGVS 153
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
32-157 |
3.00e-10 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 59.65 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 32 KDNESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKgglighhydpnqpaVYGD---PQKII 105
Cdd:PRK11172 14 KDQVVIDSVKTALELGYRAIDTAQIYD---NEAAVGQAIAESgvpRDELFITTK--------------IWIDnlaKDKLI 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1041868156 106 DAFEASLLRLKTDYIDVYFCHiwW---DKHEETEAFLQAFQTLKKSGKVRAVGVS 157
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIH--WpspNDEVSVEEFMQALLEAKKQGLTREIGIS 129
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-308 |
4.51e-10 |
|
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: 59.56 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEwgavkdNESLDAIEKAIDLGVNFIDTADVYglgHSETLVAKAIND--------HRQDIIL 79
Cdd:cd19122 4 NNGVKIPAVGFGTFANEGAK------GETYAAVTKALDVGYRHLDCAWFY---LNEDEVGDAVRDflkenpsvKREDLFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STKgglIGHHYDpnqpavygDPQKIIDAFEASLLRLKTDYIDVYFCH----------------------IWWDKHEETEA 137
Cdd:cd19122 75 CTK---VWNHLH--------EPEDVKWSIDNSLKNLKLDYIDLFLVHwpiaaekndqrspklgpdgkyvILKDLTENPEP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 138 FLQAFQTLKKSGKVRAVGVSTNDLDYIKHFNQDNDLDVVQFDYSILNKEPEKDILPYIEKHNLGAVIRGPLkmgiltgkf 217
Cdd:cd19122 144 TWRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPL--------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 218 NHETQFPDDDLRKDWPKekwfkdSLNKVEKlrslvRSNRSLAQVALRYVLSHPavSVAIPGAKNSTQVEENsshLTRPLL 297
Cdd:cd19122 215 GSQNQVPSTGERVSENP------TLNEVAE-----KGGYSLAQVLIAWGLRRG--YVVLPKSSTPSRIESN---FKSIEL 278
|
330
....*....|.
gi 1041868156 298 LDNEIEFIKQL 308
Cdd:cd19122 279 SDEDFEAINQV 289
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
1-158 |
6.60e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 58.83 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 1 MEYRLLGNT----GLIVSEIGFGSWAIGG-DEWGAVKDNES-LDAIEKAIDLGVNFIDTADVYGLGHSETLVAKAINDHR 74
Cdd:PRK10376 1 MSTIMSSGTftlgGRSVNRLGYGAMQLAGpGVFGPPKDRDAaIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 75 QDIILSTKgglIGHHYDPN---QPAVygDPQKIIDAFEASLLRLKTDYIDVYFCHIWWDKHEETE----AFLQAFQTLKK 147
Cdd:PRK10376 81 DDLTIVTK---VGARRGEDgswLPAF--SPAELRRAVHDNLRNLGLDVLDVVNLRLMGDGHGPAEgsieEPLTVLAELQR 155
|
170
....*....|.
gi 1041868156 148 SGKVRAVGVST 158
Cdd:PRK10376 156 QGLVRHIGLSN 166
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-157 |
8.42e-10 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 58.38 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAiggdewgaVKDNESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKGG 84
Cdd:cd19130 5 NDGNSIPQLGYGVFK--------VPPADTQRAVATALEVGYRHIDTAAIYG---NEEGVGAAIAASgipRDELFVTTKLW 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041868156 85 LIGHhydpnqpavygDPQKIIDAFEASLLRLKTDYIDVYFCHiwW-----DKHEETEAflqAFQTLKKSGKVRAVGVS 157
Cdd:cd19130 74 NDRH-----------DGDEPAAAFAESLAKLGLDQVDLYLVH--WptpaaGNYVHTWE---AMIELRAAGRTRSIGVS 135
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
16-157 |
1.65e-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: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIggdewgavKDNESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH---RQDIILSTKGGLIGHHYDP 92
Cdd:cd19134 14 IGLGVGEL--------SDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASgipRGELFVTTKLATPDQGFTA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041868156 93 NQpavygdpqkiiDAFEASLLRLKTDYIDVYFCHiwWDKHEETEaFLQAFQTL---KKSGKVRAVGVS 157
Cdd:cd19134 83 SQ-----------AACRASLERLGLDYVDLYLIH--WPAGREGK-YVDSWGGLmklREEGLARSIGVS 136
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-165 |
1.95e-08 |
|
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: 54.34 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEWGAvkdnesldAIEKAIDLGVNFIDTADVYGLGHS-----ETLVAKAINDHRQDIILSTK 82
Cdd:cd19118 2 NTGNKIPAIGLGTWQAEPGEVGA--------AVKIALKAGYRHLDLAKVYQNQHEvgqalKELLKEEPGVKREDLFITSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 83 GGLIGHHydpnqpavygdPQKIIDAFEASLLRLKTDYIDVYFCHiwW---------------DKHEETEAFL-------- 139
Cdd:cd19118 74 LWNNSHR-----------PEYVEPALDDTLKELGLDYLDLYLIH--WpvafkptgdlnpltaVPTNGGEVDLdlsvslvd 140
|
170 180
....*....|....*....|....*...
gi 1041868156 140 --QAFQTLKKSGKVRAVGVSTNDLDYIK 165
Cdd:cd19118 141 twKAMVELKKTGKVKSIGVSNFSIDHLQ 168
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
7-288 |
4.56e-07 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 50.57 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 7 GNTgliVSEIGFGSWAiggDEWGAVKDNeSLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND-------HRQDIIL 79
Cdd:cd19109 1 GNS---IPIIGLGTYS---EPKTTPKGA-CAEAVKVAIDTGYRHIDGAYIYQ---NEHEVGQAIREkiaegkvKREDIFY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STKGGLIGHhydpnqpavygDPQKIIDAFEASLLRLKTDYIDVYFCHI---------WWDKHE-------ETE--AFLQA 141
Cdd:cd19109 71 CGKLWNTCH-----------PPELVRPTLERTLKVLQLDYVDLYIIEMpmafkpgdeIYPRDEngkwlyhKTNlcATWEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 142 FQTLKKSGKVRAVGVStndldyikHFNQdNDLDVvqfdysILNK-----EP------------EKDILPYIEKHNLGAVI 204
Cdd:cd19109 140 LEACKDAGLVKSIGVS--------NFNR-RQLEL------ILNKpglkhKPvsnqvechpyftQPKLLEFCQQHDIVIVA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 205 RGPLKMgiltgkfnhetqfPDDDLRKDWPKEKWFKDS-LNKVEKlrslvRSNRSLAQVALRYVLSHPAvsVAIPGAKNST 283
Cdd:cd19109 205 YSPLGT-------------CRDPIWVNVSSPPLLEDPlLNSIGK-----KYNKTAAQVVLRFNIQRGV--VVIPKSFNPE 264
|
....*
gi 1041868156 284 QVEEN 288
Cdd:cd19109 265 RIKEN 269
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
16-157 |
3.80e-06 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 47.65 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIGgdewgavKDNESL-DAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND--------HRQDIILSTKGGLI 86
Cdd:cd19124 8 IGMGTASDP-------PSPEDIkAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEalrlglvkSRDELFVTSKLWCS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 87 GHHydpnqpavygdPQKIIDAFEASLLRLKTDYIDVYFCH---------IWWDKHEE------TEAFLQAFQTLKKSGKV 151
Cdd:cd19124 78 DAH-----------PDLVLPALKKSLRNLQLEYVDLYLIHwpvslkpgkFSFPIEEEdflpfdIKGVWEAMEECQRLGLT 146
|
....*.
gi 1041868156 152 RAVGVS 157
Cdd:cd19124 147 KAIGVS 152
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-126 |
8.56e-06 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 46.45 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAigGDEwgaVKDNESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAINDH-------RQDIILS 80
Cdd:cd19108 6 NDGHFIPVLGFGTYA--PEE---VPKSKALEATKLAIDAGFRHIDSAYLYQ---NEEEVGQAIRSKiadgtvkREDIFYT 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1041868156 81 TKGGLIGHHydpnqpavygdPQKIIDAFEASLLRLKTDYIDVYFCH 126
Cdd:cd19108 78 SKLWCTFHR-----------PELVRPALEKSLKKLQLDYVDLYLIH 112
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-157 |
1.43e-05 |
|
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: 45.86 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEWGAvkdnesldAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND-------HRQDIILS 80
Cdd:cd19123 7 SNGDLIPALGLGTWKSKPGEVGQ--------AVKQALEAGYRHIDCAAIYG---NEAEIGAALAEvfkegkvKREDLWIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 81 TKGGLIGHHydpnqpavygdPQKIIDAFEASLLRLKTDYIDVYFCHiwWD--------KHEETEAFL-----------QA 141
Cdd:cd19123 76 SKLWNNSHA-----------PEDVLPALEKTLADLQLDYLDLYLMH--WPvalkkgvgFPESGEDLLslspipledtwRA 142
|
170
....*....|....*.
gi 1041868156 142 FQTLKKSGKVRAVGVS 157
Cdd:cd19123 143 MEELVDKGLCRHIGVS 158
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-288 |
2.00e-05 |
|
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: 45.59 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 5 LLGNTGLIVSEIGFGSWAiggdewgaVKDNESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND-------HRQDI 77
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQ--------SSPEEIETAVDTALEAGYRHIDTAYVYR---NEAAIGNVLKKwidsgkvKREEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 78 ILSTKgglighhydpnQPAVYGDPQKIIDAFEASLLRLKTDYIDVYFCH------------IWWDKHEEteaFLQAFQT- 144
Cdd:cd19155 73 FIVTK-----------LPPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHfpvgslskeddsGKLDPTGE---HKQDYTTd 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 145 ----------LKKSGKVRAVGVSTNDLDY---------IKHFNQDNDLDvVQFDysilnkepEKDILPYIEKHNLGAVIR 205
Cdd:cd19155 139 lldiwkameaQVDQGLTRSIGLSNFNREQmarilknarIKPANLQVELH-VYLQ--------QKDLVDFCSTHSITVTAY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 206 GPL-KMGIltGKFNHETQFPDDDLrkdwpkekwfKDSLNKVEKLRSLVRSNRSLAQVALRYVLSHPAvsVAIPGAKNSTQ 284
Cdd:cd19155 210 APLgSPGA--AHFSPGTGSPSGSS----------PDLLQDPVVKAIAERHGKSPAQVLLRWLMQRGV--VVIPKSTNAAR 275
|
....
gi 1041868156 285 VEEN 288
Cdd:cd19155 276 IKEN 279
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
38-198 |
2.41e-05 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 45.14 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 38 DAIEKAIDLGVNFIDTADVYglgHSETLVAKAIND-------HRQDIILSTKGGLIGHHydpnqpavygdPQKIIDAFEA 110
Cdd:cd19129 23 NAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEvfkagkiRREDLFVTTKLWNTNHR-----------PERVKPAFEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 111 SLLRLKTDYIDVYFCH-------------------IWWDKHEETEAFLQAFQTLKKSGKVRAVGVSTNDLDYIKHFnqdn 171
Cdd:cd19129 89 SLKRLQLDYLDLYLIHtpfafqpgdeqdprdangnVIYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREI---- 164
|
170 180 190
....*....|....*....|....*....|..
gi 1041868156 172 dLDVVQFDYSILNKE-----PEKDILPYIEKH 198
Cdd:cd19129 165 -FEAARIKPAVVQVEshpylPEWELLDFCKNH 195
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-200 |
3.30e-05 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 44.80 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIGGDEwgavkdNESLDAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND-------HRQDIILS 80
Cdd:cd19119 7 NTGASIPALGLGTASPHEDR------AEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRaiddgsiKREELFIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 81 TKgglighhydpNQPAVYgdpQKIIDAFEASLLRLKTDYIDVYFCHiwW------DKHEETEAFL--------------- 139
Cdd:cd19119 78 TK----------VWPTFY---DEVERSLDESLKALGLDYVDLLLVH--WpvcfekDSDDSGKPFTpvnddgktryaasgd 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041868156 140 -----QAFQTLKKSGKVRAVGVSTNDLDYIKHFnqdndLDVVQFDYSILNKE-----PEKDILPYIEKHNL 200
Cdd:cd19119 143 hittyKQLEKIYLDGRAKAIGVSNYSIVYLERL-----IKECKVVPAVNQVElhphlPQMDLRDFCFKHGI 208
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-126 |
1.18e-04 |
|
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: 43.14 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAiggDEWGAVKDnesldAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND--------HRQDIIL 79
Cdd:cd19106 2 HTGQKMPLIGLGTWK---SKPGQVKA-----AVKYALDAGYRHIDCAAVYG---NEQEVGEALKEkvgpgkavPREDLFV 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1041868156 80 STKGGLIGHHYDPNQPAVygdpqkiidafEASLLRLKTDYIDVYFCH 126
Cdd:cd19106 71 TSKLWNTKHHPEDVEPAL-----------RKTLKDLQLDYLDLYLIH 106
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-157 |
1.30e-04 |
|
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: 42.90 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIggdewgavKDNESLDAIEKAIDLGVNFIDTADVYG----LGHSetlVAKAIND---HRQDIILSTKggLIGH 88
Cdd:cd19128 4 LGFGTYKI--------TESESKEAVKNAIKAGYRHIDCAYYYGneafIGIA---FSEIFKDggvKREDLFITSK--LWPT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 89 HYdpnqpavygDPQKIIDAFEASLLRLKTDYIDVYFCH--IWWDKHEETEAFL----------------QAFQTLKKSGK 150
Cdd:cd19128 71 MH---------QPENVKEQLLITLQDLQLEYLDLFLIHwpLAFDMDTDGDPRDdnqiqslskkpledtwRAMEQCVDEKL 141
|
....*..
gi 1041868156 151 VRAVGVS 157
Cdd:cd19128 142 TKNIGVS 148
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-157 |
3.45e-04 |
|
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: 41.63 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAiggDEWGAVKDnesldAIEKAIDLGVNFIDTADVYglgHSETLVAKAIND-------HRQDIILSTKGGLIGH 88
Cdd:cd19107 7 LGLGTWK---SPPGQVTE-----AVKVAIDAGYRHIDCAYVY---QNENEVGEAIQEkikeqvvKREDLFIVSKLWCTFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 89 hydpNQPAVYGdpqkiidAFEASLLRLKTDYIDVYFCHiWWDKHEETEAFL-------------------QAFQTLKKSG 149
Cdd:cd19107 76 ----EKGLVKG-------ACQKTLSDLKLDYLDLYLIH-WPTGFKPGKELFpldesgnvipsdttfldtwEAMEELVDEG 143
|
....*...
gi 1041868156 150 KVRAVGVS 157
Cdd:cd19107 144 LVKAIGVS 151
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-157 |
7.39e-04 |
|
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: 40.51 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 8 NTGLIVSEIGFGSWAIggdewgavkDNESL-DAIEKAIDLGVNFIDTADVYGlghSETLVAKAIND-------HRQDIIL 79
Cdd:cd19113 6 NSGYKMPSVGFGCWKL---------DNATAaDQIYQAIKAGYRLFDGAEDYG---NEKEVGEGVNRaideglvKREELFL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 80 STKggLIGHhydpnqpavYGDPQKIIDAFEASLLRLKTDYIDVYFCHIWW--------------------DKHEETEAFL 139
Cdd:cd19113 74 TSK--LWNN---------FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIafkfvpieekyppgfycgdgDNFVYEDVPI 142
|
170 180
....*....|....*....|..
gi 1041868156 140 ----QAFQTLKKSGKVRAVGVS 157
Cdd:cd19113 143 ldtwKALEKLVDAGKIKSIGVS 164
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
16-126 |
7.74e-04 |
|
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: 40.62 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041868156 16 IGFGSWAIggdewgavKDNESLDAIEKAIDLGVNFIDTADVYG----LGHSetlVAKAIND---HRQDIILSTKGGLIGH 88
Cdd:cd19114 7 VGFGTAKI--------KANETEEVIYNAIKVGYRLIDGALLYGneaeVGRG---IRKAIQEglvKREDLFIVTKLWNNFH 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1041868156 89 HYDPNQPavygdpqkiidAFEASLLRLKTDYIDVYFCH 126
Cdd:cd19114 76 GKDHVRE-----------AFDRQLKDYGLDYIDLYLIH 102
|
|
| |
