|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
14-301 |
2.41e-127 |
|
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: 365.52 E-value: 2.41e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESG----VPRTDIWVTSKLWCNA 89
Cdd:cd19125 2 FFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 90 HRAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGpEELPRNEKgeliYEDVPIEETWQAMEELLETGKVRYIGISNFN 169
Cdd:cd19125 82 HAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKG-AHMPEPEE----VLPPDIPSTWKAMEKLVDSGKVRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 170 NEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNsdISKLIEHKTLVDIANARGEgiT 249
Cdd:cd19125 157 VKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWV--KKNVLKDPIVTKVAEKLGK--T 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19113635 250 PANIAISWAVKRGTSVLPKSVNESRIVSNFLY--IPLTDKEMEAINNIGVVRRF 301
Cdd:cd19125 233 PAQVALRWGLQRGTSVLPKSTNEERIKENIDVfdWSIPEEDFAKFSSIEQQRRV 286
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
19-301 |
1.45e-116 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 337.03 E-value: 1.45e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLVPLA 98
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 99 LEKTLQDLNLEYIDAYLIHWPFallsgpeelprnekgeliyeDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLK 178
Cdd:COG0656 81 FEESLERLGLDYLDLYLIHWPG--------------------PGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 179 IAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANARgeGITPANIAISWA 258
Cdd:COG0656 141 ETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGR---------GKLLDDPVLAEIAEKH--GKTPAQVVLRWH 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 19113635 259 VKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIGVVRRF 301
Cdd:COG0656 210 LQRGVVVIPKSVTPERIRENLdaFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
23-293 |
2.78e-114 |
|
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: 330.98 E-value: 2.78e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 23 IPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLVPLALEKT 102
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 103 LQDLNLEYIDAYLIHWPFAllsgpeelprnekGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLKIAKV 182
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVP-------------GKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 183 KPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNdaynsdiSKLIEHKTLVDIANARgeGITPANIAISWAVKRG 262
Cdd:cd19071 148 KPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGR-------RPLLDDPVLKEIAKKY--GKTPAQVLLRWALQRG 218
|
250 260 270
....*....|....*....|....*....|...
gi 19113635 263 TSVLPKSVNESRIVSNF--LYIPLTDKEMEAIN 293
Cdd:cd19071 219 VVVIPKSSNPERIKENLdvFDFELSEEDMAAID 251
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
13-301 |
6.35e-112 |
|
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: 326.68 E-value: 6.35e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 13 AYFTLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIG----EGIRESGVPRTDIWVTSKLWCN 88
Cdd:cd19123 2 KTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGaalaEVFKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 89 AHRAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGpeeLPRNEKGE--LIYEDVPIEETWQAMEELLETGKVRYIGIS 166
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG---VGFPESGEdlLSLSPIPLEDTWRAMEELVDKGLCRHIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 167 NFNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPL-----ANQNDAYNSDisKLIEHKTLVDIA 241
Cdd:cd19123 159 NFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLgsgdrPAAMKAEGEP--VLLEDPVINKIA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113635 242 NArgEGITPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIGVVRRF 301
Cdd:cd19123 237 EK--HGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLeaAEVELDASDMATIAALDRHHRY 296
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
17-293 |
1.14e-104 |
|
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: 308.54 E-value: 1.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 17 LPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRES-----GVPRTDIWVTSKLWCNAHR 91
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 92 AGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNNE 171
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 172 YLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAY-NSDISKLIEHKTLVDIANARGEgiTP 250
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWaKPDEPVLLEEPKVKALAKKYNK--SP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 19113635 251 ANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAIN 293
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIqvFDFTLSPEEMKQLD 283
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
15-296 |
2.80e-101 |
|
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: 299.03 E-value: 2.80e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 15 FTLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAgl 94
Cdd:cd19117 6 FKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWHRR-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 95 VPLALEKTLQDLNLEYIDAYLIHWPFALL-SGPEELPRNEKGEL-IYEDVPIEETWQAMEELLETGKVRYIGISNFNNEY 172
Cdd:cd19117 84 VEEALDQSLKKLGLDYVDLYLMHWPVPLDpDGNDFLFKKDDGTKdHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSIKN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 173 LDRVLK--IAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNdaynsdiSKLIEHKTLVDIANARgeGITP 250
Cdd:cd19117 164 LEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTN-------APLLKEPVIIKIAKKH--GKTP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19113635 251 ANIAISWAVKRGTSVLPKSVNESRIVSNFLYIPLTDKEMEAINNIG 296
Cdd:cd19117 235 AQVIISWGLQRGYSVLPKSVTPSRIESNFKLFTLSDEEFKEIDELH 280
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
17-295 |
5.97e-98 |
|
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: 290.47 E-value: 5.97e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 17 LPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRES-----GVPRTDIWVTSKLWCNAHR 91
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 92 AGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEE---LPRNEKGELIYED--VPIEETWQAMEELLETGKVRYIGIS 166
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLnplTAVPTNGGEVDLDlsVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 167 NFNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQndayNSDISKLIEHKTLVDIanARGE 246
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNN----LAGLPLLVQHPEVKAI--AAKL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19113635 247 GITPANIAISWAVKRGTSVLPKSVNESRIVSNFLYIPLTDKEMEAINNI 295
Cdd:cd19118 235 GKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVELSDDEFNAVTAL 283
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
14-300 |
2.16e-94 |
|
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: 281.86 E-value: 2.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTLPNGDKIPSIGLGTWRSGKDET-KNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRE----SGVPRTDIWVTSKLWCN 88
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDEGvRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREkiaeGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 89 AHRAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLsgpEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNF 168
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFK---ENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 169 NNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNSDISKLIEHKTLVDIANARGEgi 248
Cdd:cd19116 159 NSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPRLDDPTLVAIAKKYGK-- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19113635 249 TPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIGVVRR 300
Cdd:cd19116 237 TTAQIVLRYLIDRGVVPIPKSSNKKRIKENIdiFDFQLTPEEVAALNSFNTNQR 290
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
14-295 |
2.60e-92 |
|
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: 275.95 E-value: 2.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRES---GVPRTDIWVTSKLWCNAH 90
Cdd:cd19121 3 SFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWSTYH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 91 RAglVPLALEKTLQDLNLEYIDAYLIHWPFALL-SGPEEL-PRNEKGEL-IYEDVPIEETWQAMEELLETGKVRYIGISN 167
Cdd:cd19121 83 RR--VELCLDRSLKSLGLDYVDLYLVHWPVLLNpNGNHDLfPTLPDGSRdLDWDWNHVDTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 168 FNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLAnqndaynSDISKLIEHKTLVDIANARgeG 247
Cdd:cd19121 161 YSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLG-------STGSPLISDEPVVEIAKKH--N 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19113635 248 ITPANIAISWAVKRGTSVLPKSVNESRIVSNFLYIPLTDKEMEAINNI 295
Cdd:cd19121 232 VGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLDDEDMNKLNDI 279
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
15-295 |
5.35e-88 |
|
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: 265.81 E-value: 5.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 15 FTLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRE---SGV-PRTDIWVTSKLWCNAH 90
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 91 RAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNN 170
Cdd:cd19154 84 APEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 171 EYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNSDISKLIEHKTLVDIAN----ARGE 246
Cdd:cd19154 164 DQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTGVSPAPNLLQDPIvkaiAEKH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 19113635 247 GITPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNI 295
Cdd:cd19154 244 GKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFniFDFSLSEEDMATLEEI 294
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
16-292 |
3.14e-85 |
|
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: 257.30 E-value: 3.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWcNAHRAGLV 95
Cdd:cd19131 3 TLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLW-NSDQGYDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PL-ALEKTLQDLNLEYIDAYLIHWPfallsgpeeLPRNEKgeliyedvpIEETWQAMEELLETGKVRYIGISNFNNEYLD 174
Cdd:cd19131 82 TLrAFDESLRKLGLDYVDLYLIHWP---------VPAQDK---------YVETWKALIELKKEGRVKSIGVSNFTIEHLQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 175 RVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANARGEgiTPANIA 254
Cdd:cd19131 144 RLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQ---------GGLLSDPVIGEIAEKHGK--TPAQVV 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19113635 255 ISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAI 292
Cdd:cd19131 213 IRWHLQNGLVVIPKSVTPSRIAENFdvFDFELDADDMQAI 252
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
23-295 |
8.30e-84 |
|
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: 253.71 E-value: 8.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 23 IPSIGLGTWR-SGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRES----GVPRTDIWVTSKLWCNAHRAGLVPL 97
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 98 ALEKTLQDLNLEYIDAYLIHWPFAllSG-PEELPRNEKGELiyedvpieETWQAMEELLETGKVRYIGISNFNNEYLDRV 176
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGV--QGlKPSDPRNAELRR--------ESWRALEDLYKEGKLRAIGVSNYTVRHLEEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 177 LKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDaynsdisKLIEHKTLVDIANArgEGITPANIAIS 256
Cdd:cd19136 151 LKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDL-------RLLEDPTVLAIAKK--YGRTPAQVLLR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19113635 257 WAVKRGTSVLPKSVNESRIVSNFLY--IPLTDKEMEAINNI 295
Cdd:cd19136 222 WALQQGIGVIPKSTNPERIAENIKVfdFELSEEDMAELNAL 262
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
23-293 |
6.30e-83 |
|
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: 250.65 E-value: 6.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 23 IPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLVPLALEKT 102
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 103 LQDLNLEYIDAYLIHWPfallsGPEelprnekgeliyedVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLKIAKV 182
Cdd:cd19073 81 LEKLGTDYVDLLLIHWP-----NPT--------------VPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 183 KPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANARgeGITPANIAISWAVKRG 262
Cdd:cd19073 142 PIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLAR---------GEVLRDPVIQEIAEKY--DKTPAQVALRWLVQKG 210
|
250 260 270
....*....|....*....|....*....|...
gi 19113635 263 TSVLPKSVNESRIVSNF--LYIPLTDKEMEAIN 293
Cdd:cd19073 211 IVVIPKASSEDHLKENLaiFDWELTSEDVAKID 243
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
15-303 |
1.68e-80 |
|
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: 245.38 E-value: 1.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 15 FTLPNGDKIPSIGLGTWRSGKD-ETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWcNAHRAG 93
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEEGsEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVW-NADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 94 LVPL-ALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnekGELIYEdvpieETWQAMEELLETGKVRYIGISNFNNEY 172
Cdd:cd19157 81 DSTLkAFEASLERLGLDYLDLYLIHWP---------------VKGKYK-----ETWKALEKLYKDGRVRAIGVSNFQVHH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 173 LDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANARGEgiTPAN 252
Cdd:cd19157 141 LEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQ---------GQLLDNPVLKEIAEKYNK--SVAQ 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19113635 253 IAISWAVKRGTSVLPKSVNESRIVSN--FLYIPLTDKEMEAINNIGVVRRFSH 303
Cdd:cd19157 210 VILRWDLQNGVVTIPKSIKEHRIIENadVFDFELSQEDMDKIDALNENLRVGP 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
16-292 |
3.69e-80 |
|
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: 244.02 E-value: 3.69e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWR-SGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGL 94
Cdd:cd19133 2 TLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 95 VPLALEKTLQDLNLEYIDAYLIHWPFAllsgpeelprnekgeliyeDVpiEETWQAMEELLETGKVRYIGISNFNNEYLD 174
Cdd:cd19133 82 AKKAFERSLKRLGLDYLDLYLIHQPFG-------------------DV--YGAWRAMEELYKEGKIRAIGVSNFYPDRLV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 175 RVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAynsdiskLIEHKTLVDIANARGEgiTPANIA 254
Cdd:cd19133 141 DLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN-------LFENPVLTEIAEKYGK--SVAQVI 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19113635 255 ISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAI 292
Cdd:cd19133 212 LRWLIQRGIVVIPKSVRPERIAENFdiFDFELSDEDMEAI 251
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
17-295 |
4.16e-80 |
|
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: 245.60 E-value: 4.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 17 LPNGDKIPSIGLGTWRSG---KDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIR---ESG-VPRTDIWVTSKLWCNA 89
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPEevpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRskiADGtVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 90 HRAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFN 169
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 170 NEYLDRVLKIA--KVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNSDISK--LIEHKTLVDIA--NA 243
Cdd:cd19108 165 RRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSpvLLEDPVLCALAkkHK 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19113635 244 RgegiTPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNI 295
Cdd:cd19108 245 R----TPALIALRYQLQRGVVVLAKSFNEKRIKENLqvFEFQLTSEDMKALDGL 294
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
20-292 |
6.18e-80 |
|
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: 245.41 E-value: 6.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGI----RESGVPRTDIWVTSKLWCNAHRAGLV 95
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDR 175
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 176 VLKIA--KVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNS--DISkLIEHKTLVDIANARGEgiTPA 251
Cdd:cd19107 161 ILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKpeDPS-LLEDPKIKEIAAKHNK--TTA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 19113635 252 NIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAI 292
Cdd:cd19107 238 QVLIRFPIQRNLVVIPKSVTPERIAENFkvFDFELSSEDMATI 280
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
14-301 |
2.24e-79 |
|
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: 244.28 E-value: 2.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIR----ESGVPRTDIWVTSKLWCNA 89
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNraidEGLVKREELFLTSKLWNNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 90 HRAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGP--EELPRN----EKGELIYEDVPIEETWQAMEELLETGKVRYI 163
Cdd:cd19113 82 HDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVPieEKYPPGfycgDGDNFVYEDVPILDTWKALEKLVDAGKIKSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 164 GISNFNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQ-----NDAYNSDISKLIEHKTLV 238
Cdd:cd19113 162 GVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRALNTPTLFEHDTIK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113635 239 DIANARGEgiTPANIAISWAVKRGTSVLPKSVNESRIVSN--FLYIPLTDKEMEAINNIGVVRRF 301
Cdd:cd19113 242 SIAAKHNK--TPAQVLLRWATQRGIAVIPKSNLPERLLQNlsVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
16-296 |
6.19e-79 |
|
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: 241.54 E-value: 6.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLV 95
Cdd:cd19127 2 TLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PLALEKTLQDLNLEYIDAYLIHWPFallsgPEELPRNekgeliyedvpiEETWQAMEELLETGKVRYIGISNFNNEYLDR 175
Cdd:cd19127 82 LRGFDASLRRLGLDYVDLYLLHWPV-----PNDFDRT------------IQAYKALEKLLAEGRVRAIGVSNFTPEHLER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 176 VLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLA---NQNDAYNSDISKLIEHKTLVDIANARGEgiTPAN 252
Cdd:cd19127 145 LIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmRYGASGPTGPGDVLQDPTITGLAEKYGK--TPAQ 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19113635 253 IAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIG 296
Cdd:cd19127 223 IVLRWHLQNGVSAIPKSVHPERIAENIdiFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
16-295 |
2.10e-78 |
|
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: 239.65 E-value: 2.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRSGK-DETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGL 94
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 95 VPLALEKTLQDLNLEYIDAYLIHWPfallsGPEElprnekgeliyedvpIEETWQAMEELLETGKVRYIGISNFNNEYLD 174
Cdd:cd19126 82 TEDAFQESLDRLGLDYVDLYLIHWP-----GKDK---------------FIDTWKALEKLYASGKVKAIGVSNFQEHHLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 175 RVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANARGEgiTPANIA 254
Cdd:cd19126 142 ELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQ---------GGLLSNPVLAAIGEKYGK--SAAQVV 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 19113635 255 ISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNI 295
Cdd:cd19126 211 LRWDIQHGVVTIPKSVHASRIKENAdiFDFELSEDDMTAIDAL 253
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
19-301 |
1.04e-77 |
|
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: 239.28 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRE----SGVPRTDIWVTSKLWCNAHRAGL 94
Cdd:cd19129 2 GSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHRPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 95 VPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYED-VPIEETWQAMEELLETGKVRYIGISNFNNEYL 173
Cdd:cd19129 82 VKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 174 DRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDaynsdiSKLIEHKTLVDIANARGEgiTPANI 253
Cdd:cd19129 162 REIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME------PKLLEDPVITAIARRVNK--TPAQV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19113635 254 AISWAVKRGTSVLPKSVNESRIVSNFLYIPLTDKEMEAINNIGVVR-RF 301
Cdd:cd19129 234 LLAWAIQRGTALLTTSKTPSRIRENFDISTLPEDAMREINEGIKTRyRF 282
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
24-295 |
5.29e-77 |
|
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: 237.04 E-value: 5.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 24 PSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRE----SGVPRTDIWVTSKLWCNAHRAGLVPLAL 99
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 100 EKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLKI 179
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 180 AKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQndaYNSDISKLIEHKTLVDIANARgeGITPANIAISWAV 259
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGS---YGDGNLTFLNDSELKALATKY--NTTPPQVIIAWHL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19113635 260 KRGT---SVLPKSVNESRIVSNF--LYIPLTDKEMEAINNI 295
Cdd:cd19128 237 QKWPknySVIPKSANKSRCQQNFdiNDLALTKEDMDAINTL 277
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
17-294 |
6.84e-77 |
|
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: 236.01 E-value: 6.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 17 LPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLVP 96
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 97 LALEKTLQDLNLEYIDAYLIHWPfallsgpeeLPRNEKgeliYedvpiEETWQAMEELLETGKVRYIGISNFNNEYLDRV 176
Cdd:cd19132 81 RTIEESLYRLGLDYVDLYLIHWP---------NPSRDL----Y-----VEAWQALIEAREEGLVRSIGVSNFLPEHLDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 177 LKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQndaynsdiSKLIEHKTLVDIANARGEgiTPANIAIS 256
Cdd:cd19132 143 IDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRG--------SGLLDEPVIKAIAEKHGK--TPAQVVLR 212
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19113635 257 WAVKRGTSVLPKSVNESRIVSNfLYI---PLTDKEMEAINN 294
Cdd:cd19132 213 WHVQLGVVPIPKSANPERQREN-LAIfdfELSDEDMAAIAA 252
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
19-295 |
2.92e-76 |
|
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: 234.08 E-value: 2.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLVPLA 98
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 99 LEKTLQDLNLEYIDAYLIHWPfallsgpeelprnekgeliYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLK 178
Cdd:cd19140 84 VEESLRKLRTDYVDLLLLHWP-------------------NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 179 IAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANARGEgiTPANIAISWA 258
Cdd:cd19140 145 LSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLAR---------GEVLKDPVLQEIGRKHGK--TPAQVALRWL 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19113635 259 V-KRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNI 295
Cdd:cd19140 214 LqQEGVAAIPKATNPERLEENLdiFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
21-292 |
3.33e-76 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 235.62 E-value: 3.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 21 DKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIR----ESGVPRTDIWVTSKLWCNAHRAGLVP 96
Cdd:cd19110 2 EDIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIRekikEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 97 LALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRV 176
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 177 LKIA--KVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNsdiskLIEHKTLVDIANARGEgiTPANIA 254
Cdd:cd19110 162 LNKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVD-----LIDDPVIQRIAKKHGK--SPAQIL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19113635 255 ISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAI 292
Cdd:cd19110 235 IRFQIQRNVIVIPKSVTPSRIKENIqvFDFELTEHDMDNL 274
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
15-295 |
1.96e-75 |
|
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: 233.67 E-value: 1.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 15 FTLPNGDKIPSIGLGTWRS--GKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRE-----SGVPRTDIWVTSKLWC 87
Cdd:cd19122 1 FTLNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 88 NAHRAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPR-NEKGE-LIYEDVP--IEETWQAMEELLETGKVRYI 163
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKyVILKDLTenPEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 164 GISNFNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNSDiSKLIEHKTLVDIANA 243
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTG-ERVSENPTLNEVAEK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 19113635 244 RGEgiTPANIAISWAVKRGTSVLPKSVNESRIVSNFLYIPLTDKEMEAINNI 295
Cdd:cd19122 240 GGY--SLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSDEDFEAINQV 289
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
20-301 |
9.74e-74 |
|
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: 228.27 E-value: 9.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGT---WRSGKDETKN-----AVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNahr 91
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIQrdlvdSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 92 AGLVPLALEKTLQDLNLEYIDAYLIHWPFallsgpeelprnekgeLIYEDVP-IEETWQAMEELLETGKVRYIGISNFNN 170
Cdd:cd19120 78 IKDPREALRKSLAKLGVDYVDLYLIHSPF----------------FAKEGGPtLAEAWAELEALKDAGLVRSIGVSNFRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 171 EYLDRVLKIAKVKPTIHQMELHPYL--PQTEYLEKHKKLQIHVSAYSPLANQNDAYNSDISKLIEhktlvDIANARgeGI 248
Cdd:cd19120 142 EDLEELLDTAKIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSPLSPLTRDAGGPLDPVLE-----KIAEKY--GV 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19113635 249 TPANIAISWAVKRGTSVLPKSVNESRIVS--NFLYIPLTDKEMEAINNIGVVRRF 301
Cdd:cd19120 215 TPAQVLLRWALQKGIVVVTTSSKEERMKEylEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
20-289 |
3.17e-73 |
|
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: 227.77 E-value: 3.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIR---ESG-VPRTDIWVTSKLWCNAHRAGLV 95
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PLALEKTLQDLNLEYIDAYLIHWPFALLSgpeelpRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDR 175
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVN------KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 176 VLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLAN---QNDAYNSDISKLIEHKTLVDIANARGEgiTPAN 252
Cdd:cd19111 155 ILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpgrANQSLWPDQPDLLEDPTVLAIAKELDK--TPAQ 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 19113635 253 IAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEM 289
Cdd:cd19111 233 VLLRFVLQRGTGVLPKSTNKERIEENFevFDFELTEEHF 271
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
19-295 |
3.36e-73 |
|
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: 227.54 E-value: 3.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRS--GKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRE---SGV--PRTDIWVTSKLWCNAHR 91
Cdd:cd19124 1 SGQTMPVIGMGTASDppSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGLvkSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 92 AGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEkgeliyEDVP---IEETWQAMEELLETGKVRYIGISNF 168
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEE------EDFLpfdIKGVWEAMEECQRLGLTKAIGVSNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 169 NNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNSDisKLIEHKTLVDIANARGEgi 248
Cdd:cd19124 155 SCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGSN--AVMESDVLKEIAAAKGK-- 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19113635 249 TPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNI 295
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLdiFDWELTEEDLEKISEI 279
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
16-301 |
3.43e-73 |
|
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: 227.02 E-value: 3.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRS-GKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWcNAHRAGL 94
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVqDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLW-NSDQGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 95 VPL-ALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnEKGELIyedvpieETWQAMEELLETGKVRYIGISNFNNEYL 173
Cdd:cd19156 81 STLaAFEESLEKLGLDYVDLYLIHWP-------------VKGKFK-------DTWKAFEKLYKEKKVRAIGVSNFHEHHL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 174 DRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANARGEgiTPANI 253
Cdd:cd19156 141 EELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQ---------GKLLSNPVLKAIGKKYGK--SAAQV 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19113635 254 AISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIGVVRRF 301
Cdd:cd19156 210 IIRWDIQHGIITIPKSVHEERIQENFdvFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
17-295 |
7.85e-73 |
|
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: 226.05 E-value: 7.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 17 LPNGDKIPSIGLGTWRSGKdETKNAVCAALK-AGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLV 95
Cdd:cd19135 7 LSNGVEMPILGLGTSHSGG-YSHEAVVYALKeCGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYEST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PLALEKTLQDLNLEYIDAYLIHWPFALLSGpeelprNEKGELIyedvpiEETWQAMEELLETGKVRYIGISNFNNEYLDR 175
Cdd:cd19135 86 KQAFEASLKRLGVDYLDLYLLHWPDCPSSG------KNVKETR------AETWRALEELYDEGLCRAIGVSNFLIEHLEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 176 VLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANARGEgiTPANIAI 255
Cdd:cd19135 154 LLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAK---------GKALEEPTVTELAKKYQK--TPAQILI 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19113635 256 SWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNI 295
Cdd:cd19135 223 RWSIQNGVVTIPKSTKEERIKENCqvFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
20-302 |
1.29e-72 |
|
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: 226.67 E-value: 1.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIR----ESGVPRTDIWVTSKLWCNAHRAGLV 95
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRkaiqEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PLALEKTLQDLNLEYIDAYLIHWPFAL--LSGPEELP----RNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFN 169
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAayVDPAENYPflwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 170 NEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQN----DAYNSDISKLIEHKTLVDIANArg 245
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVytkvTKHLKHFTNLLEHPVVKKLADK-- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19113635 246 EGITPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIGVVRRFS 302
Cdd:cd19114 239 HKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLdiTSYKLDEEDMEALYELEANARFN 297
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
12-296 |
8.96e-72 |
|
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: 224.30 E-value: 8.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 12 EAYFTLPNGDKIPSIGLGTWRSGKD--ETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIR----ESGVPRTDIWVTSKL 85
Cdd:cd19119 1 EISFKLNTGASIPALGLGTASPHEDraEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 86 WCNAHRAglVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPR-----NEKGELIYEDVPIE-ETWQAMEELLETGK 159
Cdd:cd19119 81 WPTFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSGKpftpvNDDGKTRYAASGDHiTTYKQLEKIYLDGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 160 VRYIGISNFNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDA--YNSDISKLiehktl 237
Cdd:cd19119 159 AKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPnlKNPLVKKI------ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19113635 238 vdianARGEGITPANIAISWAVKRGTSVLPKSVNESRIVSNFLYIPLTDKEMEAINNIG 296
Cdd:cd19119 233 -----AEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKEDLQKLDDIG 286
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
16-301 |
2.60e-70 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 221.14 E-value: 2.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEG----IRESGVPRTDIWVTSKLWCNAHR 91
Cdd:cd19115 6 KLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGvaraIKEGIVKREDLFIVSKLWNTFHD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 92 AGLVPLALEKTLQDLNLEYIDAYLIHWPFAL-LSGPE-ELP---RNEKGELIYEDVPIEETWQAMEELLETGKVRYIGIS 166
Cdd:cd19115 86 GERVEPICRKQLADWGIDYFDLFLIHFPIALkYVDPAvRYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLARSIGVS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 167 NFNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQ-----NDAYNSDISKLIEHKTLVDIA 241
Cdd:cd19115 166 NFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQsflelDLPGAKDTPPLFEHDVIKSIA 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113635 242 NARGEgiTPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIGVVRRF 301
Cdd:cd19115 246 EKHGK--TPAQVLLRWATQRGIAVIPKSNNPKRLAQNLdvTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
20-301 |
4.87e-70 |
|
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: 220.06 E-value: 4.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWRSG----KDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRES----GVPRTDIWVTSKLWCNAHR 91
Cdd:cd19109 1 GNSIPIIGLGTYSEPkttpKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 92 AGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNNE 171
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 172 YLDRVLKIA--KVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDA--YNSDISKLIEHKTLVDIANARGEg 247
Cdd:cd19109 161 QLELILNKPglKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPiwVNVSSPPLLEDPLLNSIGKKYNK- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19113635 248 iTPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIGVVRRF 301
Cdd:cd19109 240 -TAAQVVLRFNIQRGVVVIPKSFNPERIKENFqiFDFSLTEEEMKDIEALNKNVRY 294
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
16-279 |
1.00e-68 |
|
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: 217.01 E-value: 1.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRE---SG-VPRTDIWVTSKLWCNAHR 91
Cdd:cd19155 5 TFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLPPGGNR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 92 AGLVPLALEKTLQDLNLEYIDAYLIHWPFALLS-GPEELPRNEKGE-LIYEDVPIEETWQAMEELLETGKVRYIGISNFN 169
Cdd:cd19155 85 REKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSkEDDSGKLDPTGEhKQDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 170 NEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAY--------NSDISKLIEHKTLVDIA 241
Cdd:cd19155 165 REQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHfspgtgspSGSSPDLLQDPVVKAIA 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 19113635 242 NARGEgiTPANIAISWAVKRGTSVLPKSVNESRIVSNF 279
Cdd:cd19155 245 ERHGK--SPAQVLLRWLMQRGVVVIPKSTNAARIKENF 280
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
15-295 |
1.58e-67 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 213.89 E-value: 1.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 15 FTLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESG----VPRTDIWVTSKLWCNAH 90
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLWNSDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 91 raGLVPLALEKTLQDLNLEYIDAYLIHWPFAL----LSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGIS 166
Cdd:cd19112 83 --GHVIEACKDSLKKLQLDYLDLYLVHFPVATkhtgVGTTGSALGEDGVLDIDVTISLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 167 NFnNEYLDR-VLKIAKVKPTIHQMELHPYLpQTEYLEKH-KKLQIHVSAYSPL--ANQNDAYNSDISKLiEHKTLVDIAN 242
Cdd:cd19112 161 NY-DIFLTRdCLAYSKIKPAVNQIETHPYF-QRDSLVKFcQKHGISVTAHTPLggAAANAEWFGSVSPL-DDPVLKDLAK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19113635 243 ARGEgiTPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNI 295
Cdd:cd19112 238 KYGK--SAAQIVLRWGIQRNTAVIPKSSKPERLKENIdvFDFQLSKEDMKLIKSL 290
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
23-292 |
2.18e-67 |
|
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: 211.44 E-value: 2.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 23 IPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAG-LVPlALEK 101
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDkLLP-SLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 102 TLQDLNLEYIDAYLIHWPfallsgpeeLPRNEkgeliyedVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLKI-A 180
Cdd:cd19139 80 SLEKLRTDYVDLTLIHWP---------SPNDE--------VPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVvG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 181 KVKPTIHQMELHPYLpQTEYLEKHKKLQ-IHVSAYSPLAnqndaynsdISKLIEHKTLVDIANARgeGITPANIAISWAV 259
Cdd:cd19139 143 AGAIATNQIELSPYL-QNRKLVAHCKQHgIHVTSYMTLA---------YGKVLDDPVLAAIAERH--GATPAQIALAWAM 210
|
250 260 270
....*....|....*....|....*....|....*
gi 19113635 260 KRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAI 292
Cdd:cd19139 211 ARGYAVIPSSTKREHLRSNLlaLDLTLDADDMAAI 245
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
16-301 |
7.60e-65 |
|
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: 205.47 E-value: 7.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLV 95
Cdd:cd19134 4 TLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PLALEKTLQDLNLEYIDAYLIHWPfallsgpeeLPRNEKgeliYEDvpieeTWQAMEELLETGKVRYIGISNFNNEYLDR 175
Cdd:cd19134 84 QAACRASLERLGLDYVDLYLIHWP---------AGREGK----YVD-----SWGGLMKLREEGLARSIGVSNFTAEHLEN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 176 VLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLAnqndaynsdISKLIEHKTLVDIANARGEgiTPANIAI 255
Cdd:cd19134 146 LIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLG---------VGRLLDNPAVTAIAAAHGR--TPAQVLL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19113635 256 SWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIGVVRRF 301
Cdd:cd19134 215 RWSLQLGNVVISRSSNPERIASNLdvFDFELTADHMDALDGLDDGTRF 262
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
16-279 |
1.41e-63 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 202.61 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAglV 95
Cdd:PRK11565 8 KLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHKR--P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PLALEKTLQDLNLEYIDAYLIHWPfallsgpeeLPRNEKgeliyedvpIEETWQAMEELLETGKVRYIGISNFNNEYLDR 175
Cdd:PRK11565 86 REALEESLKKLQLDYVDLYLMHWP---------VPAIDH---------YVEAWKGMIELQKEGLIKSIGVCNFQIHHLQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 176 VLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAynsdiskLIEHKTLVDIANARGEgiTPANIAI 255
Cdd:PRK11565 148 LIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG-------VFDQKVIRDLADKYGK--TPAQIVI 218
|
250 260
....*....|....*....|....
gi 19113635 256 SWAVKRGTSVLPKSVNESRIVSNF 279
Cdd:PRK11565 219 RWHLDSGLVVIPKSVTPSRIAENF 242
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
16-293 |
3.57e-61 |
|
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: 195.90 E-value: 3.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLV 95
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PLALEKTLQDLNLEYIDAYLIHWPfallsgpeeLPrnEKGELIyedvpieETWQAMEELLETGKVRYIGISNFNNEYLDR 175
Cdd:cd19130 83 AAAFAESLAKLGLDQVDLYLVHWP---------TP--AAGNYV-------HTWEAMIELRAAGRTRSIGVSNFLPPHLER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 176 VLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANARGEgiTPANIAI 255
Cdd:cd19130 145 IVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQ---------GKLLGDPPVGAIAAAHGK--TPAQIVL 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19113635 256 SWAVKRGTSVLPKSVNESRIVSN--FLYIPLTDKEMEAIN 293
Cdd:cd19130 214 RWHLQKGHVVFPKSVRRERMEDNldVFDFDLTDTEIAAID 253
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
22-292 |
2.83e-60 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 193.70 E-value: 2.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 22 KIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAG-LVPlALE 100
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDkLIP-SLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 101 KTLQDLNLEYIDAYLIHWPfallsgpeeLPRNEkgeliyedVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVlkIA 180
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWP---------SPNDE--------VSVEEFMQALLEAKKQGLTREIGISNFTIALMKQA--IA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 181 KVKP---TIHQMELHPYLPQ---TEYLEKHkklQIHVSAYSPLAnqndaynsdISKLIEHKTLVDIANARgeGITPANIA 254
Cdd:PRK11172 142 AVGAeniATNQIELSPYLQNrkvVAFAKEH---GIHVTSYMTLA---------YGKVLKDPVIARIAAKH--NATPAQVI 207
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19113635 255 ISWAVKRGTSVLPKSVNESRIVSNFLY--IPLTDKEMEAI 292
Cdd:PRK11172 208 LAWAMQLGYSVIPSSTKRENLASNLLAqdLQLDAEDMAAI 247
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
26-295 |
3.34e-56 |
|
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: 184.05 E-value: 3.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 26 IGLGTWRSG-------KDETKNAVCAALKAGYRHIDTAHIYG---NEKEIGEGIRESGVPRTDIWVTSKLWCNAH----- 90
Cdd:pfam00248 1 IGLGTWQLGggwgpisKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVPDGDGpwpsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 91 --RAGLVPlALEKTLQDLNLEYIDAYLIHWPFallsgpeelprnekgeliyEDVPIEETWQAMEELLETGKVRYIGISNF 168
Cdd:pfam00248 81 gsKENIRK-SLEESLKRLGTDYIDLYYLHWPD-------------------PDTPIEETWDALEELKKEGKIRAIGVSNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 169 NNEYLDRVLKIAKVKPTIHQMELHPY--LPQTEYLEKHKKLQIHVSAYSPLAN--------QNDAYNSDISK------LI 232
Cdd:pfam00248 141 DAEQIEKALTKGKIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytRDPDKGPGERRrllkkgTP 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113635 233 EHKTLVDIAN--ARGEGITPANIAISWAVK--RGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNI 295
Cdd:pfam00248 221 LNLEALEALEeiAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLgaLEFPLSDEEVARIDEL 289
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
16-293 |
3.80e-51 |
|
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: 170.12 E-value: 3.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 16 TLPNGDKIPSIGLGTWRSGKD-----ETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESgvpRTDIWVTSKLW- 86
Cdd:cd19138 4 TLPDGTKVPALGQGTWYMGEDpakraQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 87 CNAHRAGLVpLALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnekgeliyEDVPIEETWQAMEELLETGKVRYIGIS 166
Cdd:cd19138 81 SNASRQGTV-RACERSLRRLGTDYLDLYLLHWR--------------------GGVPLAETVAAMEELKKEGKIRAWGVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 167 NFNN---EYLDRVLKIAKVkpTIHQMELH--------PYLPqteYLEKHKklqIHVSAYSPLANQNDAYnsdiSKLIEHK 235
Cdd:cd19138 140 NFDTddmEELWAVPGGGNC--AANQVLYNlgsrgieyDLLP---WCREHG---VPVMAYSPLAQGGLLR----RGLLENP 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113635 236 TLVDIANARgeGITPANIAISWAVKRG-TSVLPKSVNESRIVSNF--LYIPLTDKEMEAIN 293
Cdd:cd19138 208 TLKEIAARH--GATPAQVALAWVLRDGnVIAIPKSGSPEHARENAaaADLELTEEDLAELD 266
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
20-293 |
3.39e-49 |
|
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: 165.09 E-value: 3.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTW------RSGKDETKNAVCA---ALKAGYRHIDTAHIYGN---EKEIGEGIResGVPRTDIWVTSKLW- 86
Cdd:cd19072 1 GEEVPVLGLGTWgigggmSKDYSDDKKAIEAlryAIELGINLIDTAEMYGGghaEELVGKAIK--GFDREDLFITTKVSp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 87 CNAHRAGLVPlALEKTLQDLNLEYIDAYLIHWPfallsGPeelprnekgeliyeDVPIEETWQAMEELLETGKVRYIGIS 166
Cdd:cd19072 79 DHLKYDDVIK-AAKESLKRLGTDYIDLYLIHWP-----NP--------------SIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 167 NFNNEYLDRVLKIAKVKPTI-HQMELHPYLPQTE-----YLEKHKklqIHVSAYSPLAnqndayNSDISKLIEHKTLVDI 240
Cdd:cd19072 139 NFSLEELEEAQSYLKKGPIVaNQVEYNLFDREEEsgllpYCQKNG---IAIIAYSPLE------KGKLSNAKGSPLLDEI 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19113635 241 ANARgeGITPANIAISWAVKR-GTSVLPKSVNESRIVSNF--LYIPLTDKEMEAIN 293
Cdd:cd19072 210 AKKY--GKTPAQIALNWLISKpNVIAIPKASNIEHLEENAgaLGWELSEEDLQRLD 263
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
20-295 |
1.73e-44 |
|
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: 154.18 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTW-------RSGKDETKNAVCAALKAGYRHIDTAHIYG---NEKEIGEGIResGVPRTDIWVTSK----L 85
Cdd:COG0667 10 GLKVSRLGLGTMtfggpwgGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALK--GRPRDDVVIATKvgrrM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 86 WCNAHRAGLVPL----ALEKTLQDLNLEYIDAYLIHWPFAllsgpeelprnekgeliyeDVPIEETWQAMEELLETGKVR 161
Cdd:COG0667 88 GPGPNGRGLSREhirrAVEASLRRLGTDYIDLYQLHRPDP-------------------DTPIEETLGALDELVREGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 162 YIGISNFNNEYLDRVLKIAK--VKPTIHQMELHPY--LPQTEYLEKHKKLQIHVSAYSPLA------------------- 218
Cdd:COG0667 149 YIGVSNYSAEQLRRALAIAEglPPIVAVQNEYSLLdrSAEEELLPAARELGVGVLAYSPLAgglltgkyrrgatfpegdr 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 219 ---NQNDAYNSD-ISKLIEhkTLVDIANARgeGITPANIAISWAVKRG--TSVLPKSVNESRIVSNF--LYIPLTDKEME 290
Cdd:COG0667 229 aatNFVQGYLTErNLALVD--ALRAIAAEH--GVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLaaADLELSAEDLA 304
|
....*
gi 19113635 291 AINNI 295
Cdd:COG0667 305 ALDAA 309
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
23-296 |
1.60e-43 |
|
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: 151.20 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 23 IPSIGLGTWRSGKD---------ETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIREsgvPRTDIWVTSKLW-CNA 89
Cdd:cd19085 1 VSRLGLGCWQFGGGywwgdqddeESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSpDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 90 HRAGLVPlALEKTLQDLNLEYIDAYLIHWPFallsgpeelprnekgeliyEDVPIEETWQAMEELLETGKVRYIGISNFN 169
Cdd:cd19085 78 TPEDVRK-SCERSLKRLGTDYIDLYQIHWPS-------------------SDVPLEETMEALEKLKEEGKIRAIGVSNFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 170 NEYLDRVLKIAKVkpTIHQMelhPY-L----PQTEYLEKHKKLQIHVSAYSPLAnQ---NDAYNSDI--------SKLIE 233
Cdd:cd19085 138 PAQLEEALDAGRI--DSNQL---PYnLlwraIEYEILPFCREHGIGVLAYSPLA-QgllTGKFSSAEdfppgdarTRLFR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 234 H-------------KTLVDIANArgEGITPANIAISWAVKRG--TSVLPKSVNESRIVSNF--LYIPLTDKEMEAINNIG 296
Cdd:cd19085 212 HfepgaeeetfealEKLKEIADE--LGVTMAQLALAWVLQQPgvTSVIVGARNPEQLEENAaaVDLELSPSVLERLDEIS 289
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
20-293 |
6.32e-41 |
|
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: 143.48 E-value: 6.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWRSG---------KDETKNAVCAALKAGYRHIDTAHIYG---NEKEIGEGIREsgVPRTDIWVTSKLW- 86
Cdd:cd19137 1 GEKIPALGLGTWGIGgfltpdysrDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD--FPREDLFIVTKVWp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 87 CNAHRAGLVPlALEKTLQDLNLEYIDAYLIHWPfallsGPEelprnekgeliyedVPIEETWQAMEELLETGKVRYIGIS 166
Cdd:cd19137 79 TNLRYDDLLR-SLQNSLRRLDTDYIDLYLIHWP-----NPN--------------IPLEETLSAMAEGVRQGLIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 167 NFNNEYLDRVLKIAKVKPTIHQMELHPY---LPQTEYLEKHKKLQIHVSAYSPLANqndaynsdiSKLIEHKTLVDIANA 243
Cdd:cd19137 139 NFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRR---------GLEKTNRTLEEIAKN 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19113635 244 RGEgiTPANIAISWAVKRGTSV-LPKSVNESRIVSNF--LYIPLTDKEMEAIN 293
Cdd:cd19137 210 YGK--TIAQIALAWLIQKPNVVaIPKAGRVEHLKENLkaTEIKLSEEEMKLLD 260
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
24-279 |
2.14e-38 |
|
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: 136.11 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 24 PSIGLGTWRSG----KDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGVpRTDIWVTSKL----WCNAHRA 92
Cdd:cd06660 1 SRLGLGTMTFGgdgdEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-RDDVVIATKGghppGGDPSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 93 GLVP----LALEKTLQDLNLEYIDAYLIHWPFallsgpeelprnekgeliyEDVPIEETWQAMEELLETGKVRYIGISNF 168
Cdd:cd06660 80 RLSPehirRDLEESLRRLGTDYIDLYYLHRDD-------------------PSTPVEETLEALNELVREGKIRYIGVSNW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 169 NNEYLDRVLKIAK----VKPTIHQME---LHPYLPQTEYLEKHKKLQIHVSAYSPLanqndaynsdiskliehktlvdia 241
Cdd:cd06660 141 SAERLAEALAYAKahglPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPL------------------------ 196
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19113635 242 nARGegitPANIAISWAVKR--GTSVLPKSVNESRIVSNF 279
Cdd:cd06660 197 -ARG----PAQLALAWLLSQpfVTVPIVGARSPEQLEENL 231
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
22-293 |
1.67e-35 |
|
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: 130.04 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 22 KIPSIGLGTW-----------RSGKDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGvPRTDIWVTSKLWC 87
Cdd:cd19093 1 EVSPLGLGTWqwgdrlwwgygEYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG-DRDEVVIATKFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 88 NAHRAGL--VPLALEKTLQDLNLEYIDAYLIHWPFALLSgpeelprnekgeliyedvPIEETWQAMEELLETGKVRYIGI 165
Cdd:cd19093 80 LPWRLTRrsVVKALKASLERLGLDSIDLYQLHWPGPWYS------------------QIEALMDGLADAVEEGLVRAVGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 166 SNFNNEYLDRV---LKIAKVKPTIHQME---LHPYLPQTEYLEKHKKLQIHVSAYSPLA----------------NQNDA 223
Cdd:cd19093 142 SNYSADQLRRAhkaLKERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspenpppgGRRRL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113635 224 YNSDISKLIE--HKTLVDIANARGEgiTPANIAISWAVKRGTSVLPKSVNESRIVSNF--LYIPLTDKEMEAIN 293
Cdd:cd19093 222 FGRKNLEKVQplLDALEEIAEKYGK--TPAQVALNWLIAKGVVPIPGAKNAEQAEENAgaLGWRLSEEEVAELD 293
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
22-293 |
7.84e-34 |
|
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: 125.72 E-value: 7.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 22 KIPSIGLGTW-----RSGK---DETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESgvpRTDIWVTSK---LWC 87
Cdd:cd19084 3 KVSRIGLGTWaiggtWWGEvddQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKcglRWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 88 NAHRAG--LVP----LALEKTLQDLNLEYIDAYLIHWPFallsgpeelprnekgeliyEDVPIEETWQAMEELLETGKVR 161
Cdd:cd19084 80 GGKGVTkdLSPesirKEVEQSLRRLQTDYIDLYQIHWPD-------------------PNTPIEETAEALEKLKKEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 162 YIGISNFNNEYLDRVLKIAKVkpTIHQMELHPYLPQTE-----YLEKHKklqIHVSAYSPLAN--------------QND 222
Cdd:cd19084 141 YIGVSNFSVEQLEEARKYGPI--VSLQPPYSMLEREIEeellpYCRENG---IGVLPYGPLAQglltgkykkeptfpPDD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 223 AYNSD----------ISKLIEhkTLVDIANARgeGITPANIAISWAVKR--GTSVLPKSVNESRIVSN--FLYIPLTDKE 288
Cdd:cd19084 216 RRSRFpffrgenfekNLEIVD--KLKEIAEKY--GKSLAQLAIAWTLAQpgVTSAIVGAKNPEQLEENagALDWELTEEE 291
|
....*
gi 19113635 289 MEAIN 293
Cdd:cd19084 292 LKEID 296
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-293 |
2.56e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 119.31 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 23 IPSIGLGTWRSG----------KDETKN--AVCAALKAGYRHIDTAHIYG---NEKEIGEGIRESGvPRTDI-------W 80
Cdd:cd19102 1 LTTIGLGTWAIGgggwgggwgpQDDRDSiaAIRAALDLGINWIDTAAVYGlghSEEVVGRALKGLR-DRPIVatkcgllW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 81 VTSKLWCNAHRAGLVPLALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnekgeliYEDVPIEETWQAMEELLETGKV 160
Cdd:cd19102 80 DEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWP-------------------DPDEPIEEAWGALAELKEEGKV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 161 RYIGISNFNNEYLDRVLKI---AKVKP---TIHQMELHPYLPqteYLEKHKklqIHVSAYSPLAN--------------- 219
Cdd:cd19102 141 RAIGVSNFSVDQMKRCQAIhpiASLQPpysLLRRGIEAEILP---FCAEHG---IGVIVYSPMQSglltgkmtpervasl 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 220 -QND--AYNSDIS--KLIEHKTLVDIANARGE--GITPANIAISWAVKRG--TSVLPKSVNESRIVSNFLY--IPLTDKE 288
Cdd:cd19102 215 pADDwrRRSPFFQepNLARNLALVDALRPIAErhGRTVAQLAIAWVLRRPevTSAIVGARRPDQIDETVGAadLRLTPEE 294
|
....*
gi 19113635 289 MEAIN 293
Cdd:cd19102 295 LAEIE 299
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
19-292 |
1.87e-25 |
|
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: 103.45 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLG----TWRSGK---DETKNAVCAALKAGYRHIDTAHIYG---NEKEIGEGIREsgvPRTDIWVTSK---L 85
Cdd:cd19076 8 QGLEVSALGLGcmgmSAFYGPadeEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD---RRDEVVIATKfgiV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 86 WCNAH-------RAGLVPLALEKTLQDLNLEYIDAYLIHwpfallsgpeelpRnekgelIYEDVPIEETWQAMEELLETG 158
Cdd:cd19076 85 RDPGSgfrgvdgRPEYVRAACEASLKRLGTDVIDLYYQH-------------R------VDPNVPIEETVGAMAELVEEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 159 KVRYIGISNFNNEYLDRVlkiAKVKP-TIHQMElhpYLPQTEYLEKH-----KKLQIHVSAYSPL---------ANQNDA 223
Cdd:cd19076 146 KVRYIGLSEASADTIRRA---HAVHPiTAVQSE---YSLWTRDIEDEvlptcRELGIGFVAYSPLgrgfltgaiKSPEDL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 224 YNSDISKLI-----EH----KTLVDI--ANARGEGITPANIAISWAVKRGTSVLP----KSVneSRIVSNF--LYIPLTD 286
Cdd:cd19076 220 PEDDFRRNNprfqgENfdknLKLVEKleAIAAEKGCTPAQLALAWVLAQGDDIVPipgtKRI--KYLEENVgaLDVVLTP 297
|
....*.
gi 19113635 287 KEMEAI 292
Cdd:cd19076 298 EELAEI 303
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
19-295 |
9.88e-24 |
|
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: 99.05 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTW-------RSGKDETKNAVC-AALKAGYRHIDTAHIYG-NEKEIGEGIRESGVPRTDIWVTSKL-WCN 88
Cdd:cd19144 9 NGPSVPALGFGAMglsafygPPKPDEERFAVLdAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKFgIEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 89 AHRAGLVPL---------ALEKTLQDLNLEYIDAYLIHwpfallsgpeelprnekgeLIYEDVPIEETWQAMEELLETGK 159
Cdd:cd19144 89 NVETGEYSVdgspeyvkkACETSLKRLGVDYIDLYYQH-------------------RVDGKTPIEKTVAAMAELVQEGK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 160 VRYIGISNFNNEYLDRVLKIAKVkpTIHQMELHPYL-----PQTEYLEKHKKLQIHVSAYSPLANQ--NDAYNS------ 226
Cdd:cd19144 150 IKHIGLSECSAETLRRAHAVHPI--AAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRGflTGAIRSpddfee 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 227 -------------DISKLIEhktLVD----IANARgeGITPANIAISWAVKRGTSVL--PKSVNESRIVSNF--LYIPLT 285
Cdd:cd19144 228 gdfrrmaprfqaeNFPKNLE---LVDkikaIAKKK--NVTAGQLTLAWLLAQGDDIIpiPGTTKLKRLEENLgaLKVKLT 302
|
330
....*....|
gi 19113635 286 DKEMEAINNI 295
Cdd:cd19144 303 EEEEKEIREI 312
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
14-257 |
2.21e-23 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 97.53 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTLPNGD-KIPSIGLGTWRSG-----KDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGVPRTDIWVTSK 84
Cdd:COG4989 3 RIKLGASGlSVSRIVLGCMRLGewdlsPAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLSPSLREKIELQTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 85 lwC-----NAHRAGLVPL----------ALEKTLQDLNLEYIDAYLIHWPFALlsgpeelprnekgeliyedVPIEETWQ 149
Cdd:COG4989 83 --CgirlpSEARDNRVKHydtskehiiaSVEGSLRRLGTDYLDLLLLHRPDPL-------------------MDPEEVAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 150 AMEELLETGKVRYIGISNFN-------NEYLDRVLkiakvkpTIHQMELHPYlpQTEY-----LEKHKKLQIHVSAYSPL 217
Cdd:COG4989 142 AFDELKASGKVRHFGVSNFTpsqfellQSALDQPL-------VTNQIELSLL--HTDAfddgtLDYCQLNGITPMAWSPL 212
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19113635 218 ANQN--DAYNSDISKLieHKTLVDIANARGEgiTPANIAISW 257
Cdd:COG4989 213 AGGRlfGGFDEQFPRL--RAALDELAEKYGV--SPEAIALAW 250
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-178 |
8.11e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 94.96 E-value: 8.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWRSGKDETkNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIResGVPRTDIWVTSKLWCNAH---RAG 93
Cdd:cd19105 10 GLKVSRLGFGGGGLPRESP-ELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASPRLDkkdKAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 94 LVPlALEKTLQDLNLEYIDAYLIHwpfallsGPEELPRNEKGELIYEdvpieetwqAMEELLETGKVRYIGIS--NFNNE 171
Cdd:cd19105 87 LLK-SVEESLKRLQTDYIDIYQLH-------GVDTPEERLLNEELLE---------ALEKLKKEGKVRFIGFSthDNMAE 149
|
....*..
gi 19113635 172 YLDRVLK 178
Cdd:cd19105 150 VLQAAIE 156
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
20-257 |
1.10e-22 |
|
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: 95.74 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWR--SGKDETKNA---VCAALKAGYRHIDTAHIYGN---EKEIGEGIResGVPRTDIWVTSKL-W---C 87
Cdd:cd19074 1 GLKVSELSLGTWLtfGGQVDDEDAkacVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWptgP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 88 NAHRAGL----VPLALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnekgeliYEDVPIEETWQAMEELLETGKVRYI 163
Cdd:cd19074 79 GPNDRGLsrkhIFESIHASLKRLQLDYVDIYYCHRY-------------------DPETPLEETVRAMDDLIRQGKILYW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 164 GISNFNNEYLDRVLKIAK----VKPTIHQmelhpylPQTEYLEKHK---------KLQIHVSAYSPLA--------NQND 222
Cdd:cd19074 140 GTSEWSAEQIAEAHDLARqfglIPPVVEQ-------PQYNMLWREIeeeviplceKNGIGLVVWSPLAqglltgkyRDGI 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 19113635 223 -------AYNSDISKLI------EHKTLVD----IANArgEGITPANIAISW 257
Cdd:cd19074 213 pppsrsrATDEDNRDKKrrlltdENLEKVKklkpIADE--LGLTLAQLALAW 262
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
26-218 |
2.30e-22 |
|
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: 95.07 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 26 IGLGTWR------SGKDEtKNAVCAALKA---GYRHIDTAHIYG---NEKEIGEGIRESGvPRTDIWVTSKL-------- 85
Cdd:cd19148 7 IALGTWAiggwmwGGTDE-KEAIETIHKAldlGINLIDTAPVYGfglSEEIVGKALKEYG-KRDRVVIATKVglewdegg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 86 --WCNAHRAGLVPlALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnekgeliYEDVPIEETWQAMEELLETGKVRYI 163
Cdd:cd19148 85 evVRNSSPARIRK-EVEDSLRRLQTDYIDLYQVHWP-------------------DPLVPIEETAEALKELLDEGKIRAI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113635 164 GISNFNNEYLDRVLKIAkvkpTIHQMELhPY-----------LPqteYLEKHkklQIHVSAYSPLA 218
Cdd:cd19148 145 GVSNFSPEQMETFRKVA----PLHTVQP-PYnlfereiekdvLP---YARKH---NIVTLAYGALC 199
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
22-292 |
3.53e-22 |
|
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: 94.65 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 22 KIPSIGLGTW---------RSGKDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESgvpRTDIWVTSKLWCNA 89
Cdd:cd19149 10 EASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKCGLRW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 90 HRAG---------------LVPLAL----EKTLQDLNLEYIDAYLIHWPfallsgpeelprnekgeliyeDV--PIEETW 148
Cdd:cd19149 87 DREGgsfffvrdgvtvyknLSPESIreevEQSLKRLGTDYIDLYQTHWQ---------------------DVetPIEETM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 149 QAMEELLETGKVRYIGISNFNNEYLDRVLKIAKV-----KPTIHQMELhpylpQTEYLEKHKKLQIHVSAYSPLA----- 218
Cdd:cd19149 146 EALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLdiiqeKYSMLDRGI-----EKELLPYCKKNNIAFQAYSPLEqgllt 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 219 ---------NQNDAYNS----DISKLIEHKTLVD--IANARGEGITPANIAISWAVKRG--TSVLPKSVNESRIVSNF-- 279
Cdd:cd19149 221 gkitpdrefDAGDARSGipwfSPENREKVLALLEkwKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAka 300
|
330
....*....|...
gi 19113635 280 LYIPLTDKEMEAI 292
Cdd:cd19149 301 GDIRLSAEDIATM 313
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
35-294 |
8.68e-22 |
|
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: 93.45 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 35 KDETKNAVCAALKAGYRHIDTAHIYG---NEKEIGEGIREsgvPRTDIWVTSKLWCNAHRAGLVPL-----------ALE 100
Cdd:cd19078 24 KEEMIELIRKAVELGITFFDTAEVYGpytNEELVGEALKP---FRDQVVIATKFGFKIDGGKPGPLgldsrpehirkAVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 101 KTLQDLNLEYIDAYLIHwpfallsgpeelpRnekgelIYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDR---VL 177
Cdd:cd19078 101 GSLKRLQTDYIDLYYQH-------------R------VDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRahaVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 178 KIAKVKPTIHQMELHpylPQTEYLEKHKKLQIHVSAYSPLANQ--NDAYN-------SDISKLI---------EHKTLVD 239
Cdd:cd19078 162 PVTAVQSEYSMMWRE---PEKEVLPTLEELGIGFVPFSPLGKGflTGKIDentkfdeGDDRASLprftpealeANQALVD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113635 240 IAN--ARGEGITPANIAISWAVKRGTSV--LPKSVNESRIVSNF--LYIPLTDKEMEAINN 294
Cdd:cd19078 239 LLKefAEEKGATPAQIALAWLLAKKPWIvpIPGTTKLSRLEENIgaADIELTPEELREIED 299
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-257 |
1.30e-21 |
|
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: 92.62 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 18 PNGDKIPSIGLGTWRSGK-----DETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGVPRTDIWVTSKlwcna 89
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADwgesaEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 90 hrAGLVP--------------------LALEKTLQDLNLEYIDAYLIHWPFALLSgpeelprnekgeliyedvpIEETWQ 149
Cdd:cd19092 76 --CGIRLgddprpgrikhydtskehilASVEGSLKRLGTDYLDLLLLHRPDPLMD-------------------PEEVAE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 150 AMEELLETGKVRYIGISNFNN---EYLDRVLKIAKVkptIHQME---LHPYLPQTEYLEKHKKLQIHVSAYSPLANQNdA 223
Cdd:cd19092 135 AFDELVKSGKVRYFGVSNFTPsqiELLQSYLDQPLV---TNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLGGGR-L 210
|
250 260 270
....*....|....*....|....*....|....*
gi 19113635 224 YNSDISKLIE-HKTLVDIANARgeGITPANIAISW 257
Cdd:cd19092 211 FGGFDERFQRlRAALEELAEEY--GVTIEAIALAW 243
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
23-267 |
2.94e-21 |
|
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: 91.12 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 23 IPSIGLGTWR-SGK---------DETKNAVCAALKAGYRHIDTAHIYG---NEKEIGEGIRESGvprTDIWVTSKL---- 85
Cdd:cd19088 1 VSRLGYGAMRlTGPgiwgppadrEEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYP---DDVVIATKGglvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 86 -----WCNAHRAGLVPLALEKTLQDLNLEYIDAYLIHWPFAllsgpeelprnekgeliyeDVPIEETWQAMEELLETGKV 160
Cdd:cd19088 78 tgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDP-------------------KVPFEEQLGALAELQDEGLI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 161 RYIGISNFNNEYLDRVLKIAKVKPTihQMELHPYLPQTE----YLEKHkklQIHVSAYSPLANQNDAynsdiskliEHKT 236
Cdd:cd19088 139 RHIGLSNVTVAQIEEARAIVRIVSV--QNRYNLANRDDEgvldYCEAA---GIAFIPWFPLGGGDLA---------QPGG 204
|
250 260 270
....*....|....*....|....*....|.
gi 19113635 237 LVDiANARGEGITPANIAISWAVKRGTSVLP 267
Cdd:cd19088 205 LLA-EVAARLGATPAQVALAWLLARSPVMLP 234
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
22-295 |
3.45e-21 |
|
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: 91.71 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 22 KIPSIGLGTWRSG--------KDET-KNAVCAALKAGYRHIDTAHIYG---NEKEIGEGIRESGvpRTDIWVTSKlwcNA 89
Cdd:cd19083 10 DVNPIGLGTNAVGghnlypnlDEEEgKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYN--RNEVVIATK---GA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 90 HRAG-----------LVPLALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnekgeliYEDVPIEETWQAMEELLETG 158
Cdd:cd19083 85 HKFGgdgsvlnnspeFLRSAVEKSLKRLNTDYIDLYYIHFP-------------------DGETPKAEAVGALQELKDEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 159 KVRYIGISNFNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLA--------NQNDAYN-SDIS 229
Cdd:cd19083 146 KIRAIGVSNFSLEQLKEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLAsgllagkyTKDTKFPdNDLR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 230 KLIEH-------------KTLVDIANARgeGITPANIAISWAVKRG--TSVLPKSVNESRIVSNF--LYIPLTDKEMEAI 292
Cdd:cd19083 226 NDKPLfkgerfsenldkvDKLKSIADEK--GVTVAHLALAWYLTRPaiDVVIPGAKRAEQVIDNLkaLDVTLTEEEIAFI 303
|
...
gi 19113635 293 NNI 295
Cdd:cd19083 304 DAL 306
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
18-267 |
4.85e-21 |
|
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: 91.49 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 18 PNGDKIPSIGLGT----------WRSGKDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGvPRTDIWVTSK 84
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-PRDEVVIATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 85 LWCNAH----RAGL----VPLALEKTLQDLNLEYIDAYLIHWPFAllsgpeelprnekgeliyeDVPIEETWQAMEELLE 156
Cdd:cd19079 86 VYFPMGdgpnGRGLsrkhIMAEVDASLKRLGTDYIDLYQIHRWDY-------------------ETPIEETLEALHDVVK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 157 TGKVRYIGISNFNNEYLDRVLKIAKV----KPTIhqMELHPYLPQTE-------YLEKHKklqIHVSAYSPLA------- 218
Cdd:cd19079 147 SGKVRYIGASSMYAWQFAKALHLAEKngwtKFVS--MQNHYNLLYREeeremipLCEEEG---IGVIPWSPLArgrlarp 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113635 219 -NQNDAYNSDISKLIEHK-------------TLVDIANARgeGITPANIAISWAVKRGTSVLP 267
Cdd:cd19079 222 wGDTTERRRSTTDTAKLKydyfteadkeivdRVEEVAKER--GVSMAQVALAWLLSKPGVTAP 282
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
24-257 |
4.11e-20 |
|
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: 88.38 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 24 PSIGLGTWRSGKDETKNAVCAALKA----GYRHIDTAHIYGN-------EKEIGEGIRESGVpRTDIWVTSKLwcnAHRA 92
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAFALLDAfvelGGNFIDTARVYGDwvergasERVIGEWLKSRGN-RDKVVIATKG---GHPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 93 GLVPLA-----------LEKTLQDLNLEYIDAYLIHwpfallsgpeelpRNEkgeliyEDVPIEETWQAMEELLETGKVR 161
Cdd:cd19082 77 LEDMSRsrlspediradLEESLERLGTDYIDLYFLH-------------RDD------PSVPVGEIVDTLNELVRAGKIR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 162 YIGISNFN-------NEYLDrvlKIAKVKPTIHQ-------MELHPYLPQT------EYLEKHKKLQIHVSAYSPLAN-- 219
Cdd:cd19082 138 AFGASNWSteriaeaNAYAK---AHGLPGFAASSpqwslarPNEPPWPGPTlvamdeEMRAWHEENQLPVFAYSSQARgf 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19113635 220 --------------QNDAYNSDIS-KLIEH-KTLvdianARGEGITPANIAISW 257
Cdd:cd19082 215 fskraaggaeddseLRRVYYSEENfERLERaKEL-----AEEKGVSPTQIALAY 263
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
14-293 |
6.21e-20 |
|
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: 88.44 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTLPN-GDKIPSIGLGT-------------WRSGKDETKNAVCAALKAGYRHIDTAHIYGN-EKEI--GEGIRESgvpR 76
Cdd:cd19091 3 YRTLGRsGLKVSELALGTmtfgggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEgESEEilGKALKGR---R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 77 TDIWVTSKLW------CNAHRAGLVPL--ALEKTLQDLNLEYIDAYLIHWPFALlsgpeelprnekgeliyedVPIEETW 148
Cdd:cd19091 80 DDVLIATKVRgrmgegPNDVGLSRHHIirAVEASLKRLGTDYIDLYQLHGFDAL-------------------TPLEETL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 149 QAMEELLETGKVRYIGISNFNNEYLDRVLKIAK----VKPTIHQM-----------ELHPylpqteyLEKHKKLQIHVsa 213
Cdd:cd19091 141 RALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQAyysllgrdlehELMP-------LALDQGVGLLV-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 214 YSPLANQ----------------------------NDAYNSDIsklIEhkTLVDIANARgeGITPANIAISWAVKR--GT 263
Cdd:cd19091 212 WSPLAGGllsgkyrrgqpapegsrlrrtgfdfppvDRERGYDV---VD--ALREIAKET--GATPAQVALAWLLSRptVS 284
|
330 340 350
....*....|....*....|....*....|..
gi 19113635 264 SVLPKSVNESRIVSNF--LYIPLTDKEMEAIN 293
Cdd:cd19091 285 SVIIGARNEEQLEDNLgaAGLSLTPEEIARLD 316
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
14-166 |
3.47e-19 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 86.80 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTLPN-GDKIPSIGLGTWRSGKDETKNA---VCAALKAGYRHIDTAHIYGN-EKEIGEGIREsgvPRTDIWVTSKL--W 86
Cdd:COG1453 3 YRRLGKtGLEVSVLGFGGMRLPRKDEEEAealIRRAIDNGINYIDTARGYGDsEEFLGKALKG---PRDKVILATKLppW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 87 CNAhRAGLVPLaLEKTLQDLNLEYIDAYLIHWpfalLSGPEELPRNEKGELIYEdvpieetwqAMEELLETGKVRYIGIS 166
Cdd:COG1453 80 VRD-PEDMRKD-LEESLKRLQTDYIDLYLIHG----LNTEEDLEKVLKPGGALE---------ALEKAKAEGKIRHIGFS 144
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
19-261 |
1.11e-18 |
|
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: 84.57 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRSGKDETKNAVCAALKA----GYRHIDTAHIYGN----------EKEIGEGIRESGvPRTDIWVTSK 84
Cdd:cd19081 5 TGLSVSPLCLGTMVFGWTADEETSFALLDAfvdaGGNFIDTADVYSAwvpgnaggesETIIGRWLKSRG-KRDRVVIATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 85 L--WCNAHRAGLVP----LALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnekgeliYEDVPIEETWQAMEELLETG 158
Cdd:cd19081 84 VgfPMGPNGPGLSRkhirRAVEASLRRLQTDYIDLYQAHWD-------------------DPATPLEETLGALNDLIRQG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 159 KVRYIGISNFNNEYLDRVLKIAKvkptihQMELHPYL---PQ----------TEYLEKHKKLQIHVSAYSPLAN------ 219
Cdd:cd19081 145 KVRYIGASNYSAWRLQEALELSR------QHGLPRYVslqPEynlvdresfeGELLPLCREEGIGVIPYSPLAGgfltgk 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19113635 220 ---QNDAYNSDISKLIE-----------HKTLVDIANARgeGITPANIAISWAVKR 261
Cdd:cd19081 219 yrsEADLPGSTRRGEAAkrylnerglriLDALDEVAAEH--GATPAQVALAWLLAR 272
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
20-257 |
3.54e-18 |
|
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: 83.39 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTW----RSGKDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESgvpRTDIWVTSKL------W 86
Cdd:cd19087 10 GLKVSRLCLGTMnfggRTDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKVfgpmgdD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 87 CNAHraGL----VPLALEKTLQDLNLEYIDAYLIHWPFallsgpeelprnekgeliyEDVPIEETWQAMEELLETGKVRY 162
Cdd:cd19087 87 PNDR--GLsrrhIRRAVEASLRRLQTDYIDLYQMHHFD-------------------RDTPLEETLRALDDLVRQGKIRY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 163 IGISNFNNEYLDRVLKIAKVKptiHQM----ELHPY-----LPQTEYLEKHKKLQIHVSAYSPLA--------------- 218
Cdd:cd19087 146 IGVSNFAAWQIAKAQGIAARR---GLLrfvsEQPMYnllkrQAELEILPAARAYGLGVIPYSPLAgglltgkygkgkrpe 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19113635 219 ----NQNDAYNsdISKLIEHktLVDIAN-----ARGEGITPANIAISW 257
Cdd:cd19087 223 sgrlVERARYQ--ARYGLEE--YRDIAErfealAAEAGLTPASLALAW 266
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
22-219 |
1.01e-17 |
|
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: 80.60 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 22 KIPSIGLGTWRSG--------KDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIREsgvPRTDIWVTSKLWCNAH 90
Cdd:cd19086 2 EVSEIGFGTWGLGgdwwgdvdDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 91 RAGLVPL---------ALEKTLQDLNLEYIDAYLIH-WPfallsgpeelprnekgeliYEDVPIEETWQAMEELLETGKV 160
Cdd:cd19086 79 GGPERPQdfspeyireAVEASLKRLGTDYIDLYQLHnPP-------------------DEVLDNDELFEALEKLKQEGKI 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113635 161 RYIGISNFNNEYLDRVLKIAKVKpTIhQMELHPYLPQTEY--LEKHKKLQIHVSAYSPLAN 219
Cdd:cd19086 140 RAYGVSVGDPEEALAALRRGGID-VV-QVIYNLLDQRPEEelFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
19-293 |
1.25e-17 |
|
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: 81.52 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLG----TWRSGK--DETKNAVC-AALKAGYRHIDTAHIYG------NEKEIGEGIRESGVPRTDI------ 79
Cdd:cd19077 1 NGKLVGPIGLGlmglTWRPNPtpDEEAFETMkAALDAGSNLWNGGEFYGppdphaNLKLLARFFRKYPEYADKVvlsvkg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 80 -WVTSKLWCNAHRAGLVPlALEKTLQDLN-LEYIDAYlihwpfallsgpeELPRnekgelIYEDVPIEETWQAMEELLET 157
Cdd:cd19077 81 gLDPDTLRPDGSPEAVRK-SIENILRALGgTKKIDIF-------------EPAR------VDPNVPIEETIKALKELVKE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 158 GKVRYIGISNFNNEYLDRVLKIAKVkpTIHQMELHPY---LPQTEYLEKHKKLQIHVSAYSPLA---------NQNDAYN 225
Cdd:cd19077 141 GKIRGIGLSEVSAETIRRAHAVHPI--AAVEVEYSLFsreIEENGVLETCAELGIPIIAYSPLGrglltgrikSLADIPE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 226 SDISKL--------IEH-----KTLVDIANARgeGITPANIAISWAVKRGTSV---LPKSVNESRIVSNF--LYIPLTDK 287
Cdd:cd19077 219 GDFRRHldrfngenFEKnlklvDALQELAEKK--GCTPAQLALAWILAQSGPKiipIPGSTTLERVEENLkaANVELTDE 296
|
....*.
gi 19113635 288 EMEAIN 293
Cdd:cd19077 297 ELKEIN 302
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-178 |
1.32e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 80.60 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGT---WRSGKDETKNAVCAALKAGYRHIDTAHIYGN-EKEIGEGIREsgvPRTDIWVTSKLWcnAHRAGLV 95
Cdd:cd19100 8 GLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTG--ARDYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 96 PLALEKTLQDLNLEYIDAYLIHwpfaLLSGPEELPRNEKGELIYEdvpieetwqAMEELLETGKVRYIGISNFNNEYLDR 175
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLH----AVDTEEDLDQVFGPGGALE---------ALLEAKEEGKIRFIGISGHSPEVLLR 149
|
...
gi 19113635 176 VLK 178
Cdd:cd19100 150 ALE 152
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-266 |
2.76e-17 |
|
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: 80.76 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWR-----SGKDETKNAVCAALKAGYRHIDTAHIYGN-----EKEIGEGIRESGVPRTD-IWVTSKlwcn 88
Cdd:cd19089 8 GLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRPYRDeLVISTK---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 89 ahrAGLVPL---------------ALEKTLQDLNLEYIDAYLIHwpfallsgpeelpRNEKgeliyeDVPIEETWQAMEE 153
Cdd:cd19089 84 ---AGYGMWpgpygdggsrkyllaSLDQSLKRMGLDYVDIFYHH-------------RYDP------DTPLEETMTALAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 154 LLETGKVRYIGISNFNNEYLDRVLKI---AKVKPTIHQME---LHPYlPQTEYLEKHKKLQIHVSAYSPLAN-------- 219
Cdd:cd19089 142 AVRSGKALYVGISNYPGAKARRAIALlreLGVPLIIHQPRyslLDRW-AEDGLLEVLEEAGIGFIAFSPLAQglltdkyl 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113635 220 -----QNDAYNSDISKLIEHKT---------LVDIANARGEGItpANIAISWAVKRG--TSVL 266
Cdd:cd19089 221 ngippDSRRAAESKFLTEEALTpekleqlrkLNKIAAKRGQSL--AQLALSWVLRDPrvTSVL 281
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
26-267 |
2.98e-17 |
|
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: 79.59 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 26 IGLGTWRSG-------KDETKNAVCAALKAGYRHIDTAHIYGN-EKEIGEGIreSGVPRTDIWVTSKLWCnaHRAGLVPL 97
Cdd:cd19095 3 LGLGTSGIGrvwgvpsEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGT--HGEGGRDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 98 ----------ALEKTLQDLNLEYIDAYLIHwpfallSGPEELprnEKGELIyedvpieetwQAMEELLETGKVRYIGISN 167
Cdd:cd19095 79 kdfspaairaSIERSLRRLGTDYIDLLQLH------GPSDDE---LTGEVL----------ETLEDLKAAGKVRYIGVSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 168 FNNEyLDRVLKIAKVkpTIHQMELHPYLP-QTEYLEKHKKLQIHVSAYSPLANQNDAYNSDISKLIEHKTLVDIANARGE 246
Cdd:cd19095 140 DGEE-LEAAIASGVF--DVVQLPYNVLDReEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIG 216
|
250 260
....*....|....*....|...
gi 19113635 247 GITPANIAISWAV--KRGTSVLP 267
Cdd:cd19095 217 GATWAQAALRFVLshPGVSSAIV 239
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
28-293 |
5.93e-17 |
|
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: 79.96 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 28 LGT--------WRSGKDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESgvpRTDIWVTSKLWCNA------- 89
Cdd:cd19080 15 LGTmtfgtewgWGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKYTMNRrpgdpna 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 90 ---HRAGLVpLALEKTLQDLNLEYIDAYLIH-WPFAllsgpeelprnekgeliyedVPIEETWQAMEELLETGKVRYIGI 165
Cdd:cd19080 92 ggnHRKNLR-RSVEASLRRLQTDYIDLLYVHaWDFT--------------------TPVEEVMRALDDLVRAGKVLYVGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 166 SNFNNEYLDRVLKIAKVK----PTIHQME--LHPYLPQTEYLEKHKKLQIHVSAYSPLA----------------NQNDA 223
Cdd:cd19080 151 SDTPAWVVARANTLAELRgwspFVALQIEysLLERTPERELLPMARALGLGVTPWSPLGgglltgkyqrgeegraGEAKG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 224 YNSDISKLIEH-----KTLVDIANargE-GITPANIAISWAVKRGTSVLPkSVNESRI---VSNF--LYIPLTDKEMEAI 292
Cdd:cd19080 231 VTVGFGKLTERnwaivDVVAAVAE---ElGRSAAQVALAWVRQKPGVVIP-IIGARTLeqlKDNLgaLDLTLSPEQLARL 306
|
.
gi 19113635 293 N 293
Cdd:cd19080 307 D 307
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-258 |
5.03e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 76.41 E-value: 5.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 26 IGLGTW----------RSGK---DETKNAVCAALKAGYRHIDTAHIYGN-EKEIGEGIRESGVPRtdiwVTSKL----WC 87
Cdd:cd19097 3 LALGTAqfgldygianKSGKpseKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRLDKFK----IITKLpplkED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 88 NAHRAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELprnekgeliyedvpieetWQAMEELLETGKVRYIGISN 167
Cdd:cd19097 79 KKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKL------------------VEALLELKKEGLIRKIGVSV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 168 FNNEYLDRVLKiaKVKPTIHQMELHPY---LPQTEYLE--KHKKLQIHV-SAYspL-------ANQNDAYNSDISKLIEH 234
Cdd:cd19097 141 YSPEELEKALE--SFKIDIIQLPFNILdqrFLKSGLLAklKKKGIEIHArSVF--LqglllmePDKLPAKFAPAKPLLKK 216
|
250 260
....*....|....*....|....
gi 19113635 235 ktLVDIANArgEGITPANIAISWA 258
Cdd:cd19097 217 --LHELAKK--LGLSPLELALGFV 236
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
26-295 |
6.59e-16 |
|
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: 77.22 E-value: 6.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 26 IGLGTWRSGKDETKNAVCA----ALKAGYRHIDTAHIY---------G-NEKEIGEGIRESGvPRTDIWVTSK-----LW 86
Cdd:cd19094 4 ICLGTMTWGEQNTEAEAHEqldyAFDEGVNFIDTAEMYpvppspetqGrTEEIIGSWLKKKG-NRDKVVLATKvagpgEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 87 CNAHRAGLVPL-------ALEKTLQDLNLEYIDAYLIHWP---FALLSGPEELPRNEKgeliYEDVPIEETWQAMEELLE 156
Cdd:cd19094 83 ITWPRGGGTRLdrenireAVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEE----EDSVSFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 157 TGKVRYIGISNFNNEYLDRVLKIAKvkptihQMELHPYLP-QTEY-------LEKHKKLQIH--VS--AYSPLA------ 218
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAE------QLGLPRIVSiQNPYsllnrnfEEGLAEACHRenVGllAYSPLAggvltg 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 219 ----NQNDA--------------YNSdiSKLIEH-KTLVDIanARGEGITPANIAISWAVKRG--TSVL--PKSVNESRI 275
Cdd:cd19094 233 kyldGAARPeggrlnlfpgymarYRS--PQALEAvAEYVKL--ARKHGLSPAQLALAWVRSRPfvTSTIigATTLEQLKE 308
|
330 340
....*....|....*....|
gi 19113635 276 VSNFLYIPLTDKEMEAINNI 295
Cdd:cd19094 309 NIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
26-295 |
1.46e-15 |
|
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: 75.67 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 26 IGLGTWRSG-----KDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGiresGVPRTDIWVTSK---LWCNAHRAGL 94
Cdd:cd19075 5 LGTMTFGSQgrfttAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGEL----GLGERGFKIDTKanpGVGGGLSPEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 95 VPLALEKTLQDLNLEYIDAYLIHwpfallsGPEElprnekgeliyeDVPIEETWQAMEELLETGKVRYIGISNFNNEYLD 174
Cdd:cd19075 81 VRKQLETSLKRLKVDKVDVFYLH-------APDR------------STPLEETLAAIDELYKEGKFKEFGLSNYSAWEVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 175 RVLKIAK----VKPTIHQ-M----------ELHPYLpqteylekhKKLQIHVSAYSPLA--------------------- 218
Cdd:cd19075 142 EIVEICKengwVLPTVYQgMynaitrqvetELFPCL---------RKLGIRFYAYSPLAggfltgkykysedkagggrfd 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 219 ---NQNDAYNSDISKLIEHKTLVDIAN-ARGEGITPANIAISWAV-------KRGTSVLPKSVNESRIVSNFLYI---PL 284
Cdd:cd19075 213 pnnALGKLYRDRYWKPSYFEALEKVEEaAEKEGISLAEAALRWLYhhsaldgEKGDGVILGASSLEQLEENLAALekgPL 292
|
330
....*....|.
gi 19113635 285 TDKEMEAINNI 295
Cdd:cd19075 293 PEEVVKAIDEA 303
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-263 |
2.45e-15 |
|
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: 75.06 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 22 KIPSIGLGTWRSG---------------KDETKNAVCAALKAGYRHIDTAHIYG---NEKEIGEGIREsgVPRTDIWVTS 83
Cdd:cd19103 3 KLPKIALGTWSWGsggaggdqvfgnhldEDTLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR--YPREDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 84 KL--WCNAHRAGLVPLALEKTLQDLNLEYIDAYLIHwpfallsGPEELPRNEKgELIyedvpieetwqameELLETGKVR 161
Cdd:cd19103 81 KFtpQIAGQSADPVADMLEGSLARLGTDYIDIYWIH-------NPADVERWTP-ELI--------------PLLKSGKVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 162 YIGISNFN-------NEYLDRV-LKIAKVKPtiHQMELHPYLPQTEYLEKHKKLQIHVSAYSPL---------------- 217
Cdd:cd19103 139 HVGVSNHNlaeikraNEILAKAgVSLSAVQN--HYSLLYRSSEEAGILDYCKENGITFFAYMVLeqgalsgkydtkhplp 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19113635 218 --ANQNDAYNSDISKLIE-HKTLVDIANARgeGITPANIAISWAVKRGT 263
Cdd:cd19103 217 egSGRAETYNPLLPQLEElTAVMAEIGAKH--GASIAQVAIAWAIAKGT 263
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
20-295 |
3.84e-15 |
|
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: 74.94 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTW-----RSGKDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGVPRTDIWVTSKL-W---- 86
Cdd:cd19143 10 GLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWgggg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 87 --CNAH---RAGLVPlALEKTLQDLNLEYIDAYLIHWPFAllsgpeelprnekgeliyeDVPIEETWQAMEELLETGKVR 161
Cdd:cd19143 90 ppPNDRglsRKHIVE-GTKASLKRLQLDYVDLVFCHRPDP-------------------ATPIEETVRAMNDLIDQGKAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 162 YIGISNFNNEYLDRVLKIAK----VKPTIHQME---LHPYLPQTEYLEKHKKLQIHVSAYSPLANQ--NDAYNSDI---- 228
Cdd:cd19143 150 YWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQynlFHRERVEVEYAPLYEKYGLGTTTWSPLASGllTGKYNNGIpegs 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 229 -SKLIEHKTLVDIANARGE----------------GITPANIAISWAVK--RGTSVLPKSVNESRIVSNF----LYIPLT 285
Cdd:cd19143 230 rLALPGYEWLKDRKEELGQekiekvrklkpiaeelGCSLAQLAIAWCLKnpNVSTVITGATKVEQLEENLkaleVLPKLT 309
|
330
....*....|
gi 19113635 286 DKEMEAINNI 295
Cdd:cd19143 310 PEVMEKIEAI 319
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-166 |
4.49e-15 |
|
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: 74.66 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 25 SIGLGTWRSGKDET-----KNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRES----GVPRTDIWVTSKlwcnahrA 92
Cdd:cd19099 5 SLGLGTYRGDSDDEtdeeyREALKAALDSGINVIDTAINYRGgrsERLIGKALRELiekgGIKRDEVVIVTK-------A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 93 GLVP----------------------------------------LALEKTLQDLNLEYIDAYLIHWPFALLSgpeelprn 132
Cdd:cd19099 78 GYIPgdgdeplrplkyleeklgrglidvadsaglrhcispayleDQIERSLKRLGLDTIDLYLLHNPEEQLL-------- 149
|
170 180 190
....*....|....*....|....*....|....
gi 19113635 133 EKGELIYEDvPIEETWQAMEELLETGKVRYIGIS 166
Cdd:cd19099 150 ELGEEEFYD-RLEEAFEALEEAVAEGKIRYYGIS 182
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
14-183 |
6.94e-15 |
|
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: 73.74 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTLPNGD-KIPSIGLGT-------WRSGKDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIResGVPRTDIWVT 82
Cdd:cd19163 3 YRKLGKTGlKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALK--GIPRDSYYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 83 SKlwcnAHRAGLVPL------------ALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnEKGELIyeDVPIEETWQA 150
Cdd:cd19163 81 TK----VGRYGLDPDkmfdfsaeritkSVEESLKRLGLDYIDIIQVHDI-------------EFAPSL--DQILNETLPA 141
|
170 180 190
....*....|....*....|....*....|...
gi 19113635 151 MEELLETGKVRYIGISNFNNEYLDRVLKIAKVK 183
Cdd:cd19163 142 LQKLKEEGKVRFIGITGYPLDVLKEVLERSPVK 174
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
19-235 |
1.51e-14 |
|
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: 73.27 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRS---GKDETKNA--VCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGVPRTDIWVTSKL-WCN- 88
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstAISEEQAEeiVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIyWSYg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 89 AHRAGL----VPLALEKTLQDLNLEYIDAYLIHWPFALlsgpeelprnekgeliyedVPIEETWQAMEELLETGKVRYIG 164
Cdd:cd19142 89 SEERGLsrkhIIESVRASLRRLQLDYIDIVIIHKADPM-------------------CPMEEVVRAMSYLIDNGLIMYWG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 165 ISNFNNEYLDRVLKIAK----VKPTIHQMELHP--------YLPqteylEKHKKLQIHVSAYSPLANQNDAYNSDISKLI 232
Cdd:cd19142 150 TSRWSPVEIMEAFSIARqfncPTPICEQSEYHMfcrekmelYMP-----ELYNKVGVGLITWSPLSLGLDPGISEETRRL 224
|
...
gi 19113635 233 EHK 235
Cdd:cd19142 225 VTK 227
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
20-266 |
3.50e-14 |
|
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: 72.05 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWR--SGKDETKNA---VCAALKAGYRHIDTAHIYG-----NEKEIGEGIRESGVP-RTDIWVTSK---- 84
Cdd:cd19151 9 GLKLPAISLGLWHnfGDVDRYENSramLRRAFDLGITHFDLANNYGpppgsAEENFGRILKEDLKPyRDELIISTKagyt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 85 LWCNAH-----RAGLVPlALEKTLQDLNLEYIDAYLIHWPFAllsgpeelprnekgeliyeDVPIEETWQAMEELLETGK 159
Cdd:cd19151 89 MWPGPYgdwgsKKYLIA-SLDQSLKRMGLDYVDIFYHHRPDP-------------------ETPLEETMGALDQIVRQGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 160 VRYIGISNFNNEYLDRVLKIAKVKPT---IHQmelhpylPQTEYLEKH---------KKLQIHVSAYSPLANQ--NDAY- 224
Cdd:cd19151 149 ALYVGISNYPPEEAREAAAILKDLGTpclIHQ-------PKYSMFNRWveeglldvlEEEGIGCIAFSPLAQGllTDRYl 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113635 225 -----------------NSDIS--KLIEHKTLVDIANARGEgiTPANIAISWAVKRG--TSVL 266
Cdd:cd19151 222 ngipedsraakgssflkPEQITeeKLAKVRRLNEIAQARGQ--KLAQMALAWVLRNKrvTSVL 282
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
20-266 |
1.77e-13 |
|
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: 69.79 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWRS-GKD---ETKNAVC-AALKAGYRHIDTAHIYG-----NEKEIGEGIRESGVPRTD-IWVTSK---- 84
Cdd:cd19150 9 GLKLPALSLGLWHNfGDDtplETQRAILrTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAGYRDeLIISTKagyd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 85 LWCNAHRAG----LVPLALEKTLQDLNLEYIDAYLIHwpfallsgpeelpRNEkgeliyEDVPIEETWQAMEELLETGKV 160
Cdd:cd19150 89 MWPGPYGEWgsrkYLLASLDQSLKRMGLDYVDIFYSH-------------RFD------PDTPLEETMGALDHAVRSGKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 161 RYIGISNFNNEYLDR---VLKIAKVKPTIHQME---LHPYLPQTEYLEKHKKLQIHVSAYSPLANQ--NDAYNSDI---- 228
Cdd:cd19150 150 LYVGISSYSPERTREaaaILRELGTPLLIHQPSynmLNRWVEESGLLDTLQELGVGCIAFTPLAQGllTDKYLNGIpegs 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19113635 229 ---------SKLIEHKTLVDIAN----ARGEGITPANIAISWAVKRG--TSVL 266
Cdd:cd19150 230 raskerslsPKMLTEANLNSIRAlneiAQKRGQSLAQMALAWVLRDGrvTSAL 282
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
19-266 |
2.11e-13 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 70.02 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRS-----GKDETKNAVCAALKAGYRHIDTAHIYG-----NEKEIGEGIRESGVP-RTDIWVTSK--- 84
Cdd:PRK09912 21 SGLRLPALSLGLWHNfghvnALESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 85 -LWCNAHRAG----LVPLALEKTLQDLNLEYIDAYLIHwpfallsgpeelprnekgeLIYEDVPIEETWQAMEELLETGK 159
Cdd:PRK09912 101 dMWPGPYGSGgsrkYLLASLDQSLKRMGLEYVDIFYSH-------------------RVDENTPMEETASALAHAVQSGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 160 VRYIGISNFNNEYLDR---VLKIAKVKPTIHQME---LHPYLPQTEYLEKHKKLQIHVSAYSPLANQ--NDAYNSDI--- 228
Cdd:PRK09912 162 ALYVGISSYSPERTQKmveLLREWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGllTGKYLNGIpqd 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 229 --------------------SKLIEHKTLVDIANARGEgiTPANIAISWAVK--RGTSVL 266
Cdd:PRK09912 242 srmhregnkvrgltpkmlteANLNSLRLLNEMAQQRGQ--SMAQMALSWLLKdeRVTSVL 299
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
26-166 |
2.68e-13 |
|
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: 68.74 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 26 IGLGT------WRSGKDETKNA--VCAALKAGYRHIDTAHIYGN---EKEIGEGIREsgVPRTDIWVTSKL--WCNAHRA 92
Cdd:cd19096 3 LGFGTmrlpesDDDSIDEEKAIemIRYAIDAGINYFDTAYGYGGgksEEILGEALKE--GPREKFYLATKLppWSVKSAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113635 93 GLVPLaLEKTLQDLNLEYIDAYLIHWpfalLSGPEELPRNEKGELiyedvpieetWQAMEELLETGKVRYIGIS 166
Cdd:cd19096 81 DFRRI-LEESLKRLGVDYIDFYLLHG----LNSPEWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS 139
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
45-298 |
1.20e-12 |
|
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: 67.46 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 45 ALKAGYRHIDTAHIYG---NEKEIGEGIResGVPRTDIWVTSKLWCNAHRAG---------LVPLALEKTLQDLNLEYID 112
Cdd:cd19145 42 AFNSGVTFLDTSDIYGpntNEVLLGKALK--DGPREKVQLATKFGIHEIGGSgvevrgdpaYVRAACEASLKRLDVDYID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 113 AYLIHwpfallsgpeelprnekgeLIYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLKIAKVkpTIHQME-- 190
Cdd:cd19145 120 LYYQH-------------------RIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAVHPI--TAVQLEws 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 191 LHPYLPQTEYLEKHKKLQIHVSAYSPLAN-------------QNDAYNSDISKL----IEH-KTLVDIANARGE--GITP 250
Cdd:cd19145 179 LWTRDIEEEIIPTCRELGIGIVPYSPLGRgffagkakleellENSDVRKSHPRFqgenLEKnKVLYERVEALAKkkGCTP 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19113635 251 ANIAISWAVKRGTSVLPksvnesrivsnflyIPLTDKEMEAINNIGVV 298
Cdd:cd19145 259 AQLALAWVLHQGEDVVP--------------IPGTTKIKNLNQNIGAL 292
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-166 |
1.32e-12 |
|
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: 67.29 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTL-PNGDKIPSIGLG------TWRSGKDETK-NAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESgvpRTDIWVT 82
Cdd:cd19104 2 YRRFgRTGLKVSELTFGgggiggLMGRTTREEQiAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL---PAGPYIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 83 SKLwcnahRAGLVPL---------ALEKTLQDLNLEYIDAYLIHWPFallsGPEEL-PRNEKGELIYEDVPiEETWQAME 152
Cdd:cd19104 79 TKV-----RLDPDDLgdiggqierSVEKSLKRLKRDSVDLLQLHNRI----GDERDkPVGGTLSTTDVLGL-GGVADAFE 148
|
170
....*....|....
gi 19113635 153 ELLETGKVRYIGIS 166
Cdd:cd19104 149 RLRSEGKIRFIGIT 162
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-267 |
2.25e-12 |
|
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: 66.20 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 46 LKAGYRHIDTAHIY--------GNEKE--IGEGIRESGVpRTDIWVTSKLWCNAHRAGLVPL------------ALEKTL 103
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvGGESErlIGRWLKDRGN-RDDVVIATKVGAGPRDPDGGPEspeglsaetieqEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 104 QDLNLEYIDAYLIHWPFAllsgpeelprnekgeliyeDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLKIAKVK 183
Cdd:cd19752 106 RRLGTDYIDLYYAHVDDR-------------------DTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 184 ----PTIHQMElHPYL-P---------------QTEYLEKHKKLQIhvSAYSPLanQNDAYNSDISKLIEH--------- 234
Cdd:cd19752 167 gwaeFSAIQQR-HSYLrPrpgadfgvqrivtdeLLDYASSRPDLTL--LAYSPL--LSGAYTRPDRPLPEQydgpdsdar 241
|
250 260 270
....*....|....*....|....*....|....*
gi 19113635 235 -KTLVDIAnarGE-GITPANIAISWAVKRGTSVLP 267
Cdd:cd19752 242 lAVLEEVA---GElGATPNQVVLAWLLHRTPAIIP 273
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
24-166 |
6.89e-12 |
|
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: 64.88 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 24 PSIGLGT------WRS-GKDETKNAVCAALKAGYRHIDTAHIYGN-EKEIGEGIREsgVPRTDIWVTSKlwCNAHRAGLV 95
Cdd:cd19090 1 SALGLGTaglggvFGGvDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE--LPREPLVLSTK--VGRLPEDTA 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113635 96 PL-------ALEKTLQDLNLEYIDAYLIHwpfallsGPEELPrneKGELIYEDVPIEetwqAMEELLETGKVRYIGIS 166
Cdd:cd19090 77 DYsadrvrrSVEESLERLGRDRIDLLMIH-------DPERVP---WVDILAPGGALE----ALLELKEEGLIKHIGLG 140
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-167 |
9.20e-12 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 64.88 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 14 YFTLPNGD-KIPSIGLGTWRSGKDETKNAVCA----ALKAGYRHIDTAHIYG----------NEKEIGEGIRESGvPRTD 78
Cdd:PRK10625 3 YHRIPHSSlEVSTLGLGTMTFGEQNSEADAHAqldyAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 79 IWVTSKLW--CNAHRAGLVP----------LALEKTLQDLNLEYIDAYLIHWPfallsgpeELPRNEKGELIYE------ 140
Cdd:PRK10625 82 LIIASKVSgpSRNNDKGIRPnqaldrknirEALHDSLKRLQTDYLDLYQVHWP--------QRPTNCFGKLGYSwtdsap 153
|
170 180
....*....|....*....|....*..
gi 19113635 141 DVPIEETWQAMEELLETGKVRYIGISN 167
Cdd:PRK10625 154 AVSLLETLDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
24-182 |
6.36e-11 |
|
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: 61.99 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 24 PSIGLGT------WRSGKDETKNAVCAALKAGYRHIDTAHIYG---NEKEIGEGIResGVPRTDIWVTSKL--------- 85
Cdd:cd19162 1 PRLGLGAaslgnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 86 -WCNAHR------AGLVPLALEKTLQDLNLEYIDAYLIHwpfallsGPEElprnekgeliYEDVPIEETWQAMEELLETG 158
Cdd:cd19162 79 gRPAGADrrfdfsADGIRRSIEASLERLGLDRLDLVFLH-------DPDR----------HLLQALTDAFPALEELRAEG 141
|
170 180
....*....|....*....|....
gi 19113635 159 KVRYIGISNFNNEYLDRVLKIAKV 182
Cdd:cd19162 142 VVGAIGVGVTDWAALLRAARRADV 165
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
18-178 |
3.18e-10 |
|
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: 60.24 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 18 PNGDKIPSIGLGTWRSG--------KDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGVPRTDIWVTSKlw 86
Cdd:cd19153 7 IALGNVSPVGLGTAALGgvygdgleQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATK-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 87 CNAHRAG-------LVPLALEKTLQDLNLEYIDAYLIHwpfallsgpeelprneKGELIYEDVPIEETWQAMEELLETGK 159
Cdd:cd19153 85 VGRYRDSefdysaeRVRASVATSLERLHTTYLDVVYLH----------------DIEFVDYDTLVDEALPALRTLKDEGV 148
|
170
....*....|....*....
gi 19113635 160 VRYIGISNFNNEYLDRVLK 178
Cdd:cd19153 149 IKRIGIAGYPLDTLTRATR 167
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
20-176 |
7.15e-10 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 59.02 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWRSG-------KDETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGVPRTDIWVTSKlwCNA 89
Cdd:PLN02587 8 GLKVSSVGFGASPLGsvfgpvsEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTK--CGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 90 HRAGL------VPLALEKTLQDLNLEYIDAYLIHwpfallsgpeelpRNEKGELiyeDVPIEETWQAMEELLETGKVRYI 163
Cdd:PLN02587 86 YGEGFdfsaerVTKSVDESLARLQLDYVDILHCH-------------DIEFGSL---DQIVNETIPALQKLKESGKVRFI 149
|
170
....*....|....*..
gi 19113635 164 GIS----NFNNEYLDRV 176
Cdd:PLN02587 150 GITglplAIFTYVLDRV 166
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
19-295 |
1.48e-08 |
|
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: 55.43 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRSGKDETKNAVCAAL-----KAGYRHIDTAHIYGNEKE---IGEGIRESGVPRTDIWVTSKLWCNAH 90
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGQISDEVAERLmtiayESGVNLFDTAEVYAAGKAeviLGSIIKKKGWRRSSLVITTKLYWGGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 91 ---RAGL----VPLALEKTLQDLNLEYIDAYLIHWPFAllsgpeelprnekgeliyeDVPIEETWQAMEELLETGKVRYI 163
Cdd:cd19159 89 aetERGLsrkhIIEGLKGSLQRLQLEYVDVVFANRPDS-------------------NTPMEEIVRAMTHVINQGMAMYW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 164 GISNFNNEYLDRVLKIAK----VKPTIHQMELHpyLPQTEYLEK-----HKKLQIHVSAYSPLA-------NQNDAYNSD 227
Cdd:cd19159 150 GTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVEVqlpelYHKIGVGAMTWSPLAcgiisgkYGNGVPESS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 228 ISKLIEHKTLVD-IANARGE----------------GITPANIAISWAVKRG--TSVLPKSVNESRIVSNFLYI----PL 284
Cdd:cd19159 228 RASLKCYQWLKErIVSEEGRkqqnklkdlspiaerlGCTLPQLAVAWCLRNEgvSSVLLGSSTPEQLIENLGAIqvlpKM 307
|
330
....*....|.
gi 19113635 285 TDKEMEAINNI 295
Cdd:cd19159 308 TSHVVNEIDNI 318
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
19-218 |
1.10e-07 |
|
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: 52.68 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRSG----KDET-KNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIRESGVPRTDIWVTSKLWCNAH 90
Cdd:cd19160 11 SGLRVSCLGLGTWVTFgsqiSDETaEDLLTVAYEHGVNLFDTAEVYAAgkaERTLGNILKSKGWRRSSYVVTTKIYWGGQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 91 ---RAGL----VPLALEKTLQDLNLEYIDAYlihwpFALLSGPeelprnekgeliyeDVPIEETWQAMEELLETGKVRYI 163
Cdd:cd19160 91 aetERGLsrkhIIEGLRGSLDRLQLEYVDIV-----FANRSDP--------------NSPMEEIVRAMTYVINQGMAMYW 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113635 164 GISNFNNEYLDRVLKIAK----VKPTIHQMELHPYLP---QTEYLEKHKKLQIHVSAYSPLA 218
Cdd:cd19160 152 GTSRWSAMEIMEAYSVARqfnlIPPVCEQAEYHLFQRekvEMQLPELYHKIGVGSVTWSPLA 213
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
20-218 |
1.28e-06 |
|
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: 49.37 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 20 GDKIPSIGLGTWRS-----GKDETKNAVCAALKAGYRHIDTAHIYGNEK-EI--GEGIRESGVPRTDIWVTSKL-WcnAH 90
Cdd:cd19141 9 GLRVSCLGLGTWVTfgsqiSDEVAEELVTLAYENGINLFDTAEVYAAGKaEIvlGKILKKKGWRRSSYVITTKIfW--GG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 91 RA----GL----VPLALEKTLQDLNLEYIDAYlihwpFALLSGPeelprnekgeliyeDVPIEETWQAMEELLETGKVRY 162
Cdd:cd19141 87 KAeterGLsrkhIIEGLKASLERLQLEYVDIV-----FANRPDP--------------NTPMEEIVRAFTHVINQGMAMY 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113635 163 IGISNFNNEYLDRVLKIAK----VKPTIHQMELHpyLPQTEYLEKHK-----KLQIHVSAYSPLA 218
Cdd:cd19141 148 WGTSRWSAMEIMEAYSVARqfnlIPPIVEQAEYH--LFQREKVEMQLpelfhKIGVGAMTWSPLA 210
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
41-180 |
2.26e-06 |
|
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: 48.43 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 41 AVCAALKAGYRHIDTAHIYGNEKEI-GEGIR--ESGVPRTDIWVTSKlwcnAHRAGL---------VPLALEKTLQDLNL 108
Cdd:cd19164 39 IVRRALELGIRAFDTSPYYGPSEIIlGRALKalRDEFPRDTYFIITK----VGRYGPddfdyspewIRASVERSLRRLHT 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113635 109 EYIDAYLIHwpfallsgpeelprnekgelIYEDVPIEETWQAMEELLE---TGKVRYIGISNFNneyLDRVLKIA 180
Cdd:cd19164 115 DYLDLVYLH--------------------DVEFVADEEVLEALKELFKlkdEGKIRNVGISGYP---LPVLLRLA 166
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
19-218 |
4.60e-06 |
|
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: 47.77 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 19 NGDKIPSIGLGTWRS-----GKDETKNAVCAALKAGYRHIDTAHIYGNEKE---IGEGIRESGVPRTDIWVTSKLWCNAH 90
Cdd:cd19158 9 SGLRVSCLGLGTWVTfggqiTDEMAEHLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKKGWRRSSLVITTKIFWGGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 91 ---RAGL----VPLALEKTLQDLNLEYIDAYLIHWPfallsgpeelprnekgeliYEDVPIEETWQAMEELLETGKVRYI 163
Cdd:cd19158 89 aetERGLsrkhIIEGLKASLERLQLEYVDVVFANRP-------------------DPNTPMEETVRAMTHVINQGMAMYW 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113635 164 GISNFNNEYLDRVLKIAK----VKPTIHQMELHPYlpQTEYLEKH-----KKLQIHVSAYSPLA 218
Cdd:cd19158 150 GTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMF--QREKVEVQlpelfHKIGVGAMTWSPLA 211
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
24-213 |
1.70e-05 |
|
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: 45.68 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 24 PSIGLGT------WRSGKD-ETKNAVCAALKAGYRHIDTAHIYGN---EKEIGEGIREsgVPRTDIWVTSKLwcnahraG 93
Cdd:cd19152 1 PKLGFGTaplgnlYEAVSDeEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE--LGREDYVISTKV-------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 94 --LVPLA------------------------------LEKTLQDLNLEYIDAYLIHWPfallsgPEELPRNEKGELIYED 141
Cdd:cd19152 72 rlLVPLQeveptfepgfwnplpfdavfdysydgilrsIEDSLQRLGLSRIDLLSIHDP------DEDLAGAESDEHFAQA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 142 vpIEETWQAMEELLETGKVRYIGI-SN--------FNNEYLDRVLkIAKVKPTIHQMELHPYLPQteyLEKHkKLQIHVS 212
Cdd:cd19152 146 --IKGAFRALEELREEGVIKAIGLgVNdwevilriLEEADLDWVM-LAGRYTLLDHSAARELLPE---CEKR-GVKVVNA 218
|
.
gi 19113635 213 A 213
Cdd:cd19152 219 G 219
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
48-167 |
3.09e-05 |
|
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: 45.11 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 48 AGYRHIDTAHIY---GNEKEIGEGIRESGVpRTDIWVTSKLWCNAHRAGLVP--------------LALEKTLQDLNLEY 110
Cdd:cd19146 47 QGGNFIDTANNYqgeESERWVGEWMASRGN-RDEMVLATKYTTGYRRGGPIKiksnyqgnhakslrLSVEASLKKLQTSY 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 19113635 111 IDAYLIH-WPFAllsgpeelprnekgeliyedVPIEETWQAMEELLETGKVRYIGISN 167
Cdd:cd19146 126 IDILYVHwWDYT--------------------TSIPELMQSLNHLVAAGKVLYLGVSD 163
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
25-167 |
3.20e-04 |
|
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: 41.73 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 25 SIGlGTWRS-----GKDETKNAVCAALKAGYRHIDTAHIYGNEKE---IGEGIRESGVpRTDIWVTSKL----------- 85
Cdd:cd19147 19 SIG-DAWSGfmgsmDKEQAFELLDAFYEAGGNFIDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFttdykayevgk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113635 86 -----WCNAHRAGLVpLALEKTLQDLNLEYIDAYLIHWPFALLSgpeelprnekgeliyedvpIEETWQAMEELLETGKV 160
Cdd:cd19147 97 gkavnYCGNHKRSLH-VSVRDSLRKLQTDWIDILYVHWWDYTTS-------------------IEEVMDSLHILVQQGKV 156
|
....*..
gi 19113635 161 RYIGISN 167
Cdd:cd19147 157 LYLGVSD 163
|
|
| |
