|
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 ... |
14-303 |
5.87e-163 |
|
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: 455.27 E-value: 5.87e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 14 VHFTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESG----VPRKDIWVTSKLWCN 89
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 90 AHAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFpkdkdGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNF 169
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMP-----EPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 170 NDTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIYesKIPKLIEHETIQKIAKSKGEgv 249
Cdd:cd19125 156 SVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTW--VKKNVLKDPIVTKVAEKLGK-- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115800 250 TGATIAVSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSIGIRARFN 303
Cdd:cd19125 232 TPAQVALRWGLQRGTSVLPKSTNEERIKENIDVfdWSIPEEDFAKFSSIEQQRRVL 287
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
16-302 |
3.18e-126 |
|
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: 362.88 E-value: 3.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 16 FTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVG----DGIKESGVPRKDIWVTSKLWCNAH 91
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGaalaEVFKEGKVKREDLWITSKLWNNSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 APEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGEdKFPKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFND 171
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGV-GFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 172 TNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNT---IYESKIPKLIEHETIQKIAKSkgEG 248
Cdd:cd19123 163 KKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRpaaMKAEGEPVLLEDPVINKIAEK--HG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115800 249 VTGATIAVSWAITRGTSVIPKSVNEQRIKSNF--KYIPLTKEDMDEINSIGIRARF 302
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLeaAEVELDASDMATIAALDRHHRY 296
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
20-302 |
9.68e-122 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 349.74 E-value: 9.68e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 20 DGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAVPKA 99
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 100 LEKTLKDLKLDYLDEYLIHWPVSfktgedkfpkdkdgnliyekNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLERILK 179
Cdd:COG0656 81 FEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 180 VAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNqntiyeskiPKLIEHETIQKIAKSKgeGVTGATIAVSWA 259
Cdd:COG0656 141 ETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGR---------GKLLDDPVLAEIAEKH--GKTPAQVVLRWH 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 19115800 260 ITRGTSVIPKSVNEQRIKSNFK--YIPLTKEDMDEINSIGIRARF 302
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 ... |
24-294 |
1.69e-121 |
|
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: 349.09 E-value: 1.69e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 24 IPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAVPKALEKT 103
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 104 LKDLKLDYLDEYLIHWPVSFKTGEDkfpkdkdgnliyeKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLERILKVAKV 183
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVPGKEGGS-------------KEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 184 KPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNtiyeskiPKLIEHETIQKIAKSKgeGVTGATIAVSWAITRG 263
Cdd:cd19071 148 KPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGR-------RPLLDDPVLKEIAKKY--GKTPAQVLLRWALQRG 218
|
250 260 270
....*....|....*....|....*....|...
gi 19115800 264 TSVIPKSVNEQRIKSNFK--YIPLTKEDMDEIN 294
Cdd:cd19071 219 VVVIPKSSNPERIKENLDvfDFELSEEDMAAID 251
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
18-302 |
1.11e-118 |
|
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: 343.98 E-value: 1.11e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 18 LADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKES-----GVPRKDIWVTSKLWCNAHA 92
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 PEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFNDT 172
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 173 NLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIY-ESKIPKLIEHETIQKIAKSKGEgvTG 251
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWaKPDEPVLLEEPKVKALAKKYNK--SP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19115800 252 ATIAVSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSIGIRARF 302
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVfdFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
18-296 |
1.08e-111 |
|
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: 325.52 E-value: 1.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 18 LADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKES-----GVPRKDIWVTSKLWCNAHA 92
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 PEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGED---KFPKDKDGNLIY--EKNPIEETWKAMEKLLETGKVRHIGLS 167
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDlnpLTAVPTNGGEVDldLSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 168 NFNDTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNqNTIYEskiPKLIEHETIQKIAKSKge 247
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-NLAGL---PLLVQHPEVKAIAAKL-- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19115800 248 GVTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKYIPLTKEDMDEINSI 296
Cdd:cd19118 235 GKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVELSDDEFNAVTAL 283
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
16-297 |
1.20e-107 |
|
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: 315.21 E-value: 1.20e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 16 FTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHA-PE 94
Cdd:cd19117 6 FKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWHRrVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 95 AvpkALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKF-PKDKDGNLIYEKN-PIEETWKAMEKLLETGKVRHIGLSNFNDT 172
Cdd:cd19117 86 E---ALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFlFKKDDGTKDHEPDwDFIKTWELMQKLPATGKVKAIGVSNFSIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 173 NLERILK--VAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTiyeskipKLIEHETIQKIAKSKgeGVT 250
Cdd:cd19117 163 NLEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNA-------PLLKEPVIIKIAKKH--GKT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 19115800 251 GATIAVSWAITRGTSVIPKSVNEQRIKSNFKYIPLTKEDMDEINSIG 297
Cdd:cd19117 234 PAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFTLSDEEFKEIDELH 280
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
16-296 |
4.26e-101 |
|
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: 298.29 E-value: 4.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 16 FTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKES---GVPRKDIWVTSKLWCNAHa 92
Cdd:cd19121 4 FKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWSTYH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 pEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKT--GEDKFPKDKDG--NLIYEKNPIEeTWKAMEKLLETGKVRHIGLSN 168
Cdd:cd19121 83 -RRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGsrDLDWDWNHVD-TWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 169 FNDTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTiyeskipKLIEHETIQKIAKSKgeG 248
Cdd:cd19121 161 YSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGS-------PLISDEPVVEIAKKH--N 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19115800 249 VTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKYIPLTKEDMDEINSI 296
Cdd:cd19121 232 VGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLDDEDMNKLNDI 279
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
16-301 |
1.30e-99 |
|
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: 294.96 E-value: 1.30e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 16 FTLADGSKIPGLGLGTWRS-EPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDG----IKESGVPRKDIWVTSKLWCNA 90
Cdd:cd19116 3 IKLNDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 91 HAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKfpkDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFN 170
Cdd:cd19116 83 HEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDS---ESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 171 DTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIYESKIPKLIEHETIQKIAKSKGEgvT 250
Cdd:cd19116 160 SEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPRLDDPTLVAIAKKYGK--T 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115800 251 GATIAVSWAITRGTSVIPKSVNEQRIKSN-----FKyipLTKEDMDEINSIGIRAR 301
Cdd:cd19116 238 TAQIVLRYLIDRGVVPIPKSSNKKRIKENidifdFQ---LTPEEVAALNSFNTNQR 290
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
15-301 |
1.76e-96 |
|
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: 287.39 E-value: 1.76e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 15 HFTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKE---SGV-PRKDIWVTSKLWCNA 90
Cdd:cd19154 3 SITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 91 HAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFN 170
Cdd:cd19154 83 HAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 171 DTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGN------QNTIYESKIPKLIEHETIQKIAKS 244
Cdd:cd19154 163 NDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranfTKSTGVSPAPNLLQDPIVKAIAEK 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115800 245 KGEgvTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSIGIRAR 301
Cdd:cd19154 243 HGK--TPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIfdFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
21-295 |
5.92e-96 |
|
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: 286.24 E-value: 5.92e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGI----KESGVPRKDIWVTSKLWCNAHAPEAV 96
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLER 176
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 177 ILKVA--KVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIY-ESKIPKLIEHETIQKIAKSKGEgvTGAT 253
Cdd:cd19107 161 ILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWaKPEDPSLLEDPKIKEIAAKHNK--TTAQ 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19115800 254 IAVSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINS 295
Cdd:cd19107 239 VLIRFPIQRNLVVIPKSVTPERIAENFKVfdFELSSEDMATILS 282
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
17-296 |
6.66e-92 |
|
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: 273.86 E-value: 6.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 17 TLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAV 96
Cdd:cd19131 3 TLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVSfktGEDKFpkdkdgnliyeknpiEETWKAMEKLLETGKVRHIGLSNFNDTNLER 176
Cdd:cd19131 83 LRAFDESLRKLGLDYVDLYLIHWPVP---AQDKY---------------VETWKALIELKKEGRVKSIGVSNFTIEHLQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 177 ILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQntiyeskipKLIEHETIQKIAKSKGEgvTGATIAV 256
Cdd:cd19131 145 LIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQG---------GLLSDPVIGEIAEKHGK--TPAQVVI 213
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19115800 257 SWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19131 214 RWHLQNGLVVIPKSVTPSRIAENFDVfdFELDADDMQAIAGL 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
16-302 |
1.20e-91 |
|
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: 273.88 E-value: 1.20e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 16 FTLADGSKIPGLGLGTWRSEP-NQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPE 94
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 95 AVPKALEKTLKDLKLDYLDEYLIHWPVsfktgEDKFpkdkdgnliyeknpiEETWKAMEKLLETGKVRHIGLSNFNDTNL 174
Cdd:cd19157 82 STLKAFEASLERLGLDYLDLYLIHWPV-----KGKY---------------KETWKALEKLYKDGRVRAIGVSNFQVHHL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 175 ERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNtiyeskipkLIEHETIQKIAKSKGEgvTGATI 254
Cdd:cd19157 142 EDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ---------LLDNPVLKEIAEKYNK--SVAQV 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 19115800 255 AVSWAITRGTSVIPKSVNEQRIKSN---FKYiPLTKEDMDEINSIGIRARF 302
Cdd:cd19157 211 ILRWDLQNGVVTIPKSIKEHRIIENadvFDF-ELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
16-303 |
3.12e-89 |
|
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: 269.32 E-value: 3.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 16 FTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDG----IKESGVPRKDIWVTSKLWCNAH 91
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGvnraIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 APEAVPKALEKTLKDLKLDYLDEYLIHWPVSFK--TGEDKFPKD----KDGNLIYEKNPIEETWKAMEKLLETGKVRHIG 165
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPGfycgDGDNFVYEDVPILDTWKALEKLVDAGKIKSIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 166 LSNFNDTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTI-----YESKIPKLIEHETIQK 240
Cdd:cd19113 163 VSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVelnqgRALNTPTLFEHDTIKS 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115800 241 IAKSkgEGVTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKYIP--LTKEDMDEINSIGIRARFN 303
Cdd:cd19113 243 IAAK--HNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDfdLTKEDFEEIAKLDIGLRFN 305
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
24-296 |
5.53e-89 |
|
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: 266.80 E-value: 5.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 24 IPGLGLGTWR-SEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKES----GVPRKDIWVTSKLWCNAHAPEAVPK 98
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 99 ALEKTLKDLKLDYLDEYLIHWPvsfktGEDKFPKDKDGNLIYEKnpieETWKAMEKLLETGKVRHIGLSNFNDTNLERIL 178
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWP-----GVQGLKPSDPRNAELRR----ESWRALEDLYKEGKLRAIGVSNYTVRHLEELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 179 KVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNtiyeskiPKLIEHETIQKIAKSkgEGVTGATIAVSW 258
Cdd:cd19136 152 KYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD-------LRLLEDPTVLAIAKK--YGRTPAQVLLRW 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19115800 259 AITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19136 223 ALQQGIGVIPKSTNPERIAENIKVfdFELSEEDMAELNAL 262
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
24-294 |
1.50e-88 |
|
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: 264.90 E-value: 1.50e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 24 IPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAVPKALEKT 103
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 104 LKDLKLDYLDEYLIHWPVSfktgedkfpkdkdgnliyeKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLERILKVAKV 183
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNP-------------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 184 KPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQntiyeskipKLIEHETIQKIAKSKgeGVTGATIAVSWAITRG 263
Cdd:cd19073 142 PIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARG---------EVLRDPVIQEIAEKY--DKTPAQVALRWLVQKG 210
|
250 260 270
....*....|....*....|....*....|...
gi 19115800 264 TSVIPKSVNEQRIKSNFKY--IPLTKEDMDEIN 294
Cdd:cd19073 211 IVVIPKASSEDHLKENLAIfdWELTSEDVAKID 243
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
21-314 |
6.34e-88 |
|
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: 265.48 E-value: 6.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKE----SGVPRKDIWVTSKLWCNAHAPEAV 96
Cdd:cd19129 3 SGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHRPERV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEKN-PIEETWKAMEKLLETGKVRHIGLSNFNDTNLE 175
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDGvTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 176 RILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTiyeskiPKLIEHETIQKIAKSKGEgvTGATIA 255
Cdd:cd19129 163 EIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME------PKLLEDPVITAIARRVNK--TPAQVL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 256 VSWAITRGTSVIPKSVNEQRIKSNFKYIPLTKEDMDEINS-IGIRARFNQATFSNEPVFA 314
Cdd:cd19129 235 LAWAIQRGTALLTTSKTPSRIRENFDISTLPEDAMREINEgIKTRYRFNSVVETGVPGFI 294
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
17-296 |
1.01e-86 |
|
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: 260.58 E-value: 1.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 17 TLADGSKIPGLGLGTWR-SEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEA 95
Cdd:cd19133 2 TLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 96 VPKALEKTLKDLKLDYLDEYLIHWPVsfktgedkfpkdkdGNliyeknpIEETWKAMEKLLETGKVRHIGLSNFNDTNLE 175
Cdd:cd19133 82 AKKAFERSLKRLGLDYLDLYLIHQPF--------------GD-------VYGAWRAMEELYKEGKIRAIGVSNFYPDRLV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 176 RILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNtiyeskiPKLIEHETIQKIAKSKGEGVtgATIA 255
Cdd:cd19133 141 DLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGR-------NNLFENPVLTEIAEKYGKSV--AQVI 211
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 19115800 256 VSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19133 212 LRWLIQRGIVVIPKSVRPERIAENFDIfdFELSDEDMEAIAAL 254
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
21-302 |
5.30e-84 |
|
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: 255.12 E-value: 5.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIK---ESG-VPRKDIWVTSKLWCNAHAPEAV 96
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVSFKTgedkfpKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLER 176
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVN------KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 177 ILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGN---QNTIYESKIPKLIEHETIQKIAKSKGEgvTGAT 253
Cdd:cd19111 155 ILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpgrANQSLWPDQPDLLEDPTVLAIAKELDK--TPAQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 19115800 254 IAVSWAITRGTSVIPKSVNEQRIKSNFKYI--PLTKEDMDEINSIGIRARF 302
Cdd:cd19111 233 VLLRFVLQRGTGVLPKSTNKERIEENFEVFdfELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
18-305 |
5.41e-84 |
|
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: 255.62 E-value: 5.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 18 LADGSKIPGLGLGTWRSE---PNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIK---ESG-VPRKDIWVTSKLWCNA 90
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPEevpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRskiADGtVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 91 HAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFN 170
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 171 DTNLERILKVA--KVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIY--ESKIPKLIEHETIQKIAKSKG 246
Cdd:cd19108 165 RRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEwvDQNSPVLLEDPVLCALAKKHK 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115800 247 EgvTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKYI--PLTKEDMDEINSIGIRARFNQA 305
Cdd:cd19108 245 R--TPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFefQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
14-297 |
1.18e-83 |
|
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: 254.34 E-value: 1.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 14 VHFTLADGSKIPGLGLGTWRSEPN--QTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIK----ESGVPRKDIWVTSKLW 87
Cdd:cd19119 2 ISFKLNTGASIPALGLGTASPHEDraEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKVW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 88 CNAHapEAVPKALEKTLKDLKLDYLDEYLIHWPVSFK-----TGEDKFPKDKDGNLIYEKNPIE-ETWKAMEKLLETGKV 161
Cdd:cd19119 82 PTFY--DEVERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAASGDHiTTYKQLEKIYLDGRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 162 RHIGLSNFNDTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGnqntiyeSKIPKLIEHETIQKI 241
Cdd:cd19119 160 KAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLG-------SHGAPNLKNPLVKKI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115800 242 AKSkgEGVTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKYIPLTKEDMDEINSIG 297
Cdd:cd19119 233 AEK--YNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKEDLQKLDDIG 286
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
23-307 |
4.91e-83 |
|
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: 252.96 E-value: 4.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 23 KIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGI----KESGVPRKDIWVTSKLWCNAHAPEAVPK 98
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIrekiKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 99 ALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLERIL 178
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 179 KVA--KVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIYEskipkLIEHETIQKIAKSKGEgvTGATIAV 256
Cdd:cd19110 163 NKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVD-----LIDDPVIQRIAKKHGK--SPAQILI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19115800 257 SWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSIGIRARFnqATF 307
Cdd:cd19110 236 RFQIQRNVIVIPKSVTPSRIKENIQVfdFELTEHDMDNLLSLDRNLRL--ATF 286
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
17-297 |
9.59e-83 |
|
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: 251.17 E-value: 9.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 17 TLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAV 96
Cdd:cd19127 2 TLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVsfktgedkfPKDKDGNLiyeknpieETWKAMEKLLETGKVRHIGLSNFNDTNLER 176
Cdd:cd19127 82 LRGFDASLRRLGLDYVDLYLLHWPV---------PNDFDRTI--------QAYKALEKLLAEGRVRAIGVSNFTPEHLER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 177 ILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIYESKIP---KLIEHETIQKIAKSKGEgvTGAT 253
Cdd:cd19127 145 LIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGPTgpgDVLQDPTITGLAEKYGK--TPAQ 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19115800 254 IAVSWAITRGTSVIPKSVNEQRIKSNFKYI--PLTKEDMDEINSIG 297
Cdd:cd19127 223 IVLRWHLQNGVSAIPKSVHPERIAENIDIFdfALSAEDMAAIDALD 268
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
25-296 |
5.24e-82 |
|
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: 249.75 E-value: 5.24e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 25 PGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKE----SGVPRKDIWVTSKLWCNAHAPEAVPKAL 100
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 101 EKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLERILKV 180
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 181 AKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQntiYESKIPKLIEHETIQKIAKSKgeGVTGATIAVSWAI 260
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGS---YGDGNLTFLNDSELKALATKY--NTTPPQVIIAWHL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19115800 261 TRGT---SVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19128 237 QKWPknySVIPKSANKSRCQQNFDIndLALTKEDMDAINTL 277
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
21-304 |
2.50e-81 |
|
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: 248.63 E-value: 2.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIK----ESGVPRKDIWVTSKLWCNAHAPEAV 96
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRkaiqEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVSFK---TGEDKFPKDKDGNLI---YEKNPIEETWKAMEKLLETGKVRHIGLSNFN 170
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWKDKELKkfpLEQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 171 DTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGnqNTIYeSKIPK-------LIEHETIQKIAK 243
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFG--NAVY-TKVTKhlkhftnLLEHPVVKKLAD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115800 244 SkgEGVTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSIGIRARFNQ 304
Cdd:cd19114 238 K--HKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDItsYKLDEEDMEALYELEANARFND 298
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
17-296 |
2.92e-81 |
|
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: 246.97 E-value: 2.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 17 TLADGSKIPGLGLGTWRSEP-NQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEA 95
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 96 VPKALEKTLKDLKLDYLDEYLIHWPVsfktgedkfpKDKdgnliyeknpIEETWKAMEKLLETGKVRHIGLSNFNDTNLE 175
Cdd:cd19126 82 TEDAFQESLDRLGLDYVDLYLIHWPG----------KDK----------FIDTWKALEKLYASGKVKAIGVSNFQEHHLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 176 RILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQntiyeskipKLIEHETIQKIAKSKGEgvTGATIA 255
Cdd:cd19126 142 ELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG---------GLLSNPVLAAIGEKYGK--SAAQVV 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 19115800 256 VSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19126 211 LRWDIQHGVVTIPKSVHASRIKENADIfdFELSEDDMTAIDAL 253
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
16-296 |
3.77e-81 |
|
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: 247.92 E-value: 3.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 16 FTLADGSKIPGLGLGTWRSE--PNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKE-----SGVPRKDIWVTSKLWC 88
Cdd:cd19122 1 FTLNNGVKIPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 89 NAHAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPK-DKDGNLIYEK----NPiEETWKAMEKLLETGKVRH 163
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILKdlteNP-EPTWRAMEEIYESGKAKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 164 IGLSNFNDTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIyESKIPKLIEHETIQKIAK 243
Cdd:cd19122 160 IGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQV-PSTGERVSENPTLNEVAE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19115800 244 SKGEgvTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKYIPLTKEDMDEINSI 296
Cdd:cd19122 239 KGGY--SLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSDEDFEAINQV 289
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
20-296 |
8.83e-81 |
|
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: 246.41 E-value: 8.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 20 DGSKIPGLGLGTWRS--EPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKE---SGV--PRKDIWVTSKLWC-NAH 91
Cdd:cd19124 1 SGQTMPVIGMGTASDppSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGLvkSRDELFVTSKLWCsDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 APEAVPkALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEknpIEETWKAMEKLLETGKVRHIGLSNFND 171
Cdd:cd19124 81 PDLVLP-ALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPFD---IKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 172 TNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIYESKipKLIEHETIQKIAKSKGEgvTG 251
Cdd:cd19124 157 KKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGSN--AVMESDVLKEIAAAKGK--TV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 19115800 252 ATIAVSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19124 233 AQVSLRWVYEQGVSLVVKSFNKERMKQNLDIfdWELTEEDLEKISEI 279
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
21-302 |
2.27e-80 |
|
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: 246.63 E-value: 2.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWrSEPNQT-----KNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKES----GVPRKDIWVTSKLWCNAH 91
Cdd:cd19109 1 GNSIPIIGLGTY-SEPKTTpkgacAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKiaegKVKREDIFYCGKLWNTCH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 APEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFND 171
Cdd:cd19109 80 PPELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 172 TNLERILKVA--KVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGN--QNTIYESKIPKLIEHETIQKIAKSKGE 247
Cdd:cd19109 160 RQLELILNKPglKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTcrDPIWVNVSSPPLLEDPLLNSIGKKYNK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115800 248 gvTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSIGIRARF 302
Cdd:cd19109 240 --TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIfdFSLTEEEMKDIEALNKNVRY 294
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
17-304 |
2.55e-79 |
|
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: 243.87 E-value: 2.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 17 TLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDG----IKESGVPRKDIWVTSKLWCNAHA 92
Cdd:cd19115 6 KLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGvaraIKEGIVKREDLFIVSKLWNTFHD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 PEAVPKALEKTLKDLKLDYLDEYLIHWPVSFK--TGEDKFP---KDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLS 167
Cdd:cd19115 86 GERVEPICRKQLADWGIDYFDLFLIHFPIALKyvDPAVRYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLARSIGVS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 168 NFNDTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTI-----YESKIPKLIEHETIQKIA 242
Cdd:cd19115 166 NFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLeldlpGAKDTPPLFEHDVIKSIA 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115800 243 KSKGEgvTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKYIP--LTKEDMDEINSIGIRARFNQ 304
Cdd:cd19115 246 EKHGK--TPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGfdLEAEEIKAISALDIGLRFNN 307
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
21-302 |
3.21e-79 |
|
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: 242.14 E-value: 3.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGT---WRSEPNQTKN-----AVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAha 92
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIQrdlvdSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 pEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedKFPKDKDGNLiyeknpiEETWKAMEKLLETGKVRHIGLSNFNDT 172
Cdd:cd19120 79 -KDPREALRKSLAKLGVDYVDLYLIHSP--------FFAKEGGPTL-------AEAWAELEALKDAGLVRSIGVSNFRIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 173 NLERILKVAKVKPAVHQMELHPFL--PQTEFVEKHKKLGIHVTAYSPfgnQNTIYESKiPKLIEHeTIQKIAKSKgeGVT 250
Cdd:cd19120 143 DLEELLDTAKIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSP---LSPLTRDA-GGPLDP-VLEKIAEKY--GVT 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19115800 251 GATIAVSWAITRGTSVIPKSVNEQRIKS--NFKYIPLTKEDMDEINSIGIRARF 302
Cdd:cd19120 216 PAQVLLRWALQKGIVVVTTSSKEERMKEylEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
17-302 |
1.42e-78 |
|
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: 240.50 E-value: 1.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 17 TLADGSKIPGLGLGTWRSEP-NQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEA 95
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 96 VPKALEKTLKDLKLDYLDEYLIHWPvsfktGEDKFpkdkdgnliyeknpiEETWKAMEKLLETGKVRHIGLSNFNDTNLE 175
Cdd:cd19156 82 TLAAFEESLEKLGLDYVDLYLIHWP-----VKGKF---------------KDTWKAFEKLYKEKKVRAIGVSNFHEHHLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 176 RILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQntiyeskipKLIEHETIQKIAKSKGEgvTGATIA 255
Cdd:cd19156 142 ELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQG---------KLLSNPVLKAIGKKYGK--SAAQVI 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19115800 256 VSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSIGIRARF 302
Cdd:cd19156 211 IRWDIQHGIITIPKSVHEERIQENFDVfdFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
18-296 |
2.11e-78 |
|
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: 239.92 E-value: 2.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 18 LADGSKIPGLGLGTWRSEpNQTKNAVKTALQY-GYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAV 96
Cdd:cd19135 7 LSNGVEMPILGLGTSHSG-GYSHEAVVYALKEcGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYEST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKfpkdkdgnliyeKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLER 176
Cdd:cd19135 86 KQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNV------------KETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 177 ILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQntiyeskipKLIEHETIQKIAKSKGEgvTGATIAV 256
Cdd:cd19135 154 LLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKG---------KALEEPTVTELAKKYQK--TPAQILI 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19115800 257 SWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19135 223 RWSIQNGVVTIPKSTKEERIKENCQVfdFSLSEEDMATLDSL 264
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
15-301 |
3.57e-77 |
|
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: 238.19 E-value: 3.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 15 HFTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKE---SG-VPRKDIWVTSKLWCNA 90
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 91 HAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGED-KFPKDKDGN-LIYEKNPIEETWKAMEKLLETGKVRHIGLSN 168
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDdSGKLDPTGEhKQDYTTDLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 169 FNDTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQ--NTIY------ESKIPKLIEHETIQK 240
Cdd:cd19155 163 FNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPgaAHFSpgtgspSGSSPDLLQDPVVKA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115800 241 IAKSKGEgvTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSIGIRAR 301
Cdd:cd19155 243 IAERHGK--SPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVfdFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
21-296 |
8.27e-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: 232.92 E-value: 8.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAVPKAL 100
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLASV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 101 EKTLKDLKLDYLDEYLIHWPvsfktgedkfpkDKDGnliyeknPIEETWKAMEKLLETGKVRHIGLSNFNDTNLERILKV 180
Cdd:cd19140 85 EESLRKLRTDYVDLLLLHWP------------NKDV-------PLAETLGALNEAQEAGLARHIGVSNFTVALLREAVEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 181 AKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQntiyeskipKLIEHETIQKIAKSkgEGVTGATIAVSWAI 260
Cdd:cd19140 146 SEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARG---------EVLKDPVLQEIGRK--HGKTPAQVALRWLL 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 19115800 261 TR-GTSVIPKSVNEQRIKSNFKYI--PLTKEDMDEINSI 296
Cdd:cd19140 215 QQeGVAAIPKATNPERLEENLDIFdfTLSDEEMARIAAL 253
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
18-294 |
5.83e-74 |
|
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: 228.31 E-value: 5.83e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 18 LADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAVP 97
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 98 KALEKTLKDLKLDYLDEYLIHWPVsfktgedkfPKdkdgnliyeKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLERI 177
Cdd:cd19132 81 RTIEESLYRLGLDYVDLYLIHWPN---------PS---------RDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 178 LKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNtiyeskipKLIEHETIQKIAKSkgEGVTGATIAVS 257
Cdd:cd19132 143 IDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGS--------GLLDEPVIKAIAEK--HGKTPAQVVLR 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19115800 258 WAITRGTSVIPKSVNEQRIKSN---FKYiPLTKEDMDEIN 294
Cdd:cd19132 213 WHVQLGVVPIPKSANPERQRENlaiFDF-ELSDEDMAAIA 251
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
16-304 |
1.07e-72 |
|
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: 226.98 E-value: 1.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 16 FTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESG----VPRKDIWVTSKLWCNAH 91
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLWNSDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 apEAVPKALEKTLKDLKLDYLDEYLIHWPVSFK-TGEDK--FPKDKDGNL-IYEKNPIEETWKAMEKLLETGKVRHIGLS 167
Cdd:cd19112 83 --GHVIEACKDSLKKLQLDYLDLYLVHFPVATKhTGVGTtgSALGEDGVLdIDVTISLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 168 NFnDTNLER-ILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIYE---SKIPklIEHETIQKIAK 243
Cdd:cd19112 161 NY-DIFLTRdCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEwfgSVSP--LDDPVLKDLAK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115800 244 SKGEgvTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKYI--PLTKEDMDEINSIGIRARFNQ 304
Cdd:cd19112 238 KYGK--SAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFdfQLSKEDMKLIKSLDRKYRTNQ 298
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
17-293 |
2.14e-68 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 214.55 E-value: 2.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 17 TLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHApeAV 96
Cdd:PRK11565 8 KLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHK--RP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVSfktgedkfpkdkdgnliyEKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLER 176
Cdd:PRK11565 86 REALEESLKKLQLDYVDLYLMHWPVP------------------AIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 177 ILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPF--GNQNtiyeskipkLIEHETIQKIAKSKGEgvTGATI 254
Cdd:PRK11565 148 LIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLaqGGKG---------VFDQKVIRDLADKYGK--TPAQI 216
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19115800 255 AVSWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEI 293
Cdd:PRK11565 217 VIRWHLDSGLVVIPKSVTPSRIAENFDVfdFRLDKDELGEI 257
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
15-296 |
3.70e-68 |
|
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: 213.62 E-value: 3.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 15 HFTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPE 94
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 95 AVPKALEKTLKDLKLDYLDEYLIHWPVSFKtgedkfpkdkdGNLIyeknpieETWKAMEKLLETGKVRHIGLSNFNDTNL 174
Cdd:cd19130 81 EPAAAFAESLAKLGLDQVDLYLVHWPTPAA-----------GNYV-------HTWEAMIELRAAGRTRSIGVSNFLPPHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 175 ERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQntiyeskipKLIEHETIQKIAKSKGEgvTGATI 254
Cdd:cd19130 143 ERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG---------KLLGDPPVGAIAAAHGK--TPAQI 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 19115800 255 AVSWAITRGTSVIPKSVNEQRIKSN---FKYiPLTKEDMDEINSI 296
Cdd:cd19130 212 VLRWHLQKGHVVFPKSVRRERMEDNldvFDF-DLTDTEIAAIDAL 255
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
24-293 |
2.72e-66 |
|
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: 208.36 E-value: 2.72e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 24 IPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAVPKALEKT 103
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 104 LKDLKLDYLDEYLIHWPVsfktgedkfpkdkdgnlIYEKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLER-ILKVAK 182
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPS-----------------PNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEaIAVVGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 183 VKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGnqntiyeskIPKLIEHETIQKIAKSkgEGVTGATIAVSWAITR 262
Cdd:cd19139 144 GAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA---------YGKVLDDPVLAAIAER--HGATPAQIALAWAMAR 212
|
250 260 270
....*....|....*....|....*....|...
gi 19115800 263 GTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEI 293
Cdd:cd19139 213 GYAVIPSSTKREHLRSNLLAldLTLDADDMAAI 245
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
17-302 |
2.76e-64 |
|
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: 203.93 E-value: 2.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 17 TLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAV 96
Cdd:cd19134 4 TLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVSfktgedkfpkdKDGNLIyeknpieETWKAMEKLLETGKVRHIGLSNFNDTNLER 176
Cdd:cd19134 84 QAACRASLERLGLDYVDLYLIHWPAG-----------REGKYV-------DSWGGLMKLREEGLARSIGVSNFTAEHLEN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 177 ILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGnqntiyeskIPKLIEHETIQKIAKSKGEgvTGATIAV 256
Cdd:cd19134 146 LIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLG---------VGRLLDNPAVTAIAAAHGR--TPAQVLL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19115800 257 SWAITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSIGIRARF 302
Cdd:cd19134 215 RWSLQLGNVVISRSSNPERIASNLDVfdFELTADHMDALDGLDDGTRF 262
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
23-293 |
7.85e-60 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 192.55 E-value: 7.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 23 KIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAVPKALEK 102
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 103 TLKDLKLDYLDEYLIHWPVsfktgedkfPKDkdgnliyeKNPIEETwkaMEKLLET---GKVRHIGLSNFNDTNLER-IL 178
Cdd:PRK11172 82 SLQKLRTDYVDLTLIHWPS---------PND--------EVSVEEF---MQALLEAkkqGLTREIGISNFTIALMKQaIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 179 KVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGnqntiyeskIPKLIEHETIQKIAKSkgEGVTGATIAVSW 258
Cdd:PRK11172 142 AVGAENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA---------YGKVLKDPVIARIAAK--HNATPAQVILAW 210
|
250 260 270
....*....|....*....|....*....|....*..
gi 19115800 259 AITRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEI 293
Cdd:PRK11172 211 AMQLGYSVIPSSTKRENLASNLLAqdLQLDAEDMAAI 247
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
27-296 |
2.13e-58 |
|
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: 189.44 E-value: 2.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTW-------RSEPNQTKNAVKTALQYGYRHIDAAAIYG---NEDEVGDGIKESGVPRKDIWVTSKL------WCNA 90
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 91 HAPEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkdgnliYEKNPIEETWKAMEKLLETGKVRHIGLSNFN 170
Cdd:pfam00248 81 GSKENIRKSLEESLKRLGTDYIDLYYLHWP-------------------DPDTPIEETWDALEELKKEGKIRAIGVSNFD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 171 DTNLERILKVAKVKPAVHQMELHPF--LPQTEFVEKHKKLGIHVTAYSPFGNQ-----NTIYESKIPKLIEH-------- 235
Cdd:pfam00248 142 AEQIEKALTKGKIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGlltgkYTRDPDKGPGERRRllkkgtpl 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 236 -----ETIQKIAKSKgeGVTGATIAVSWAI--TRGTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:pfam00248 222 nlealEALEEIAKEH--GVSPAQVALRWALskPGVTIPIPGASNPEQLEDNLGAleFPLSDEEVARIDEL 289
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
17-294 |
4.91e-52 |
|
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: 172.43 E-value: 4.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 17 TLADGSKIPGLGLGTW-----RSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESgvpRKDIWVTSKLW- 87
Cdd:cd19138 4 TLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 88 CNAhAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFktgedkfpkdkdgnliyeknPIEETWKAMEKLLETGKVRHIGLS 167
Cdd:cd19138 81 SNA-SRQGTVRACERSLRRLGTDYLDLYLLHWRGGV--------------------PLAETVAAMEELKKEGKIRAWGVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 168 NFNDTNLERILKVAKVKP-AVHQMELHPFLPQTEF--VEKHKKLGIHVTAYSPFGNQNTIYESkipkLIEHETIQKIAKS 244
Cdd:cd19138 140 NFDTDDMEELWAVPGGGNcAANQVLYNLGSRGIEYdlLPWCREHGVPVMAYSPLAQGGLLRRG----LLENPTLKEIAAR 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19115800 245 kgEGVTGATIAVSWAITRG-TSVIPKSVNEQRIKSNFKY--IPLTKEDMDEIN 294
Cdd:cd19138 216 --HGATPAQVALAWVLRDGnVIAIPKSGSPEHARENAAAadLELTEEDLAELD 266
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
21-294 |
2.69e-50 |
|
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: 167.79 E-value: 2.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTW---------RSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKesGVPRKDIWVTSKLWC 88
Cdd:cd19072 1 GEEVPVLGLGTWgigggmskdYSDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK--GFDREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 89 NAHAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKtgedkfpkdkdgnliyeknPIEETWKAMEKLLETGKVRHIGLSN 168
Cdd:cd19072 79 DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSI-------------------PIEETLRAMEELVEEGKIRYIGVSN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 169 FNDTNLERILKVAK-VKPAVHQMELHPFLPQTE-----FVEKHkklGIHVTAYSPFGnqntiyESKIPKLIEHETIQKIA 242
Cdd:cd19072 140 FSLEELEEAQSYLKkGPIVANQVEYNLFDREEEsgllpYCQKN---GIAIIAYSPLE------KGKLSNAKGSPLLDEIA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19115800 243 KSKGEgvTGATIAVSWAITR-GTSVIPKSVNEQRIKSNFKY--IPLTKEDMDEIN 294
Cdd:cd19072 211 KKYGK--TPAQIALNWLISKpNVIAIPKASNIEHLEENAGAlgWELSEEDLQRLD 263
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
21-294 |
3.69e-43 |
|
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: 149.26 E-value: 3.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWR---------SEPNQTKNAVKTALQYGYRHIDAAAIYG---NEDEVGDGIKEsgVPRKDIWVTSKLWC 88
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 89 NAHAPEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkdgnliyEKN-PIEETWKAMEKLLETGKVRHIGLS 167
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP--------------------NPNiPLEETLSAMAEGVRQGLIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 168 NFNDTNLERILKVAKVKPAVHQMELHPF---LPQTEFVEKHKKLGIHVTAYSPFgnQNTIyeskipkLIEHETIQKIAKS 244
Cdd:cd19137 139 NFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL--RRGL-------EKTNRTLEEIAKN 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19115800 245 KGEgvTGATIAVSWAITRGTSV-IPKSVNEQRIKSNFKY--IPLTKEDMDEIN 294
Cdd:cd19137 210 YGK--TIAQIALAWLIQKPNVVaIPKAGRVEHLKENLKAteIKLSEEEMKLLD 260
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
24-297 |
2.21e-41 |
|
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: 145.42 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 24 IPGLGLGTWR---------SEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKEsgvPRKDIWVTSKLWCNAH 91
Cdd:cd19085 1 VSRLGLGCWQfgggywwgdQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 APEAVPKALEKTLKDLKLDYLDEYLIHWPVSFktgedkfpkdkdgnliyekNPIEETWKAMEKLLETGKVRHIGLSNFND 171
Cdd:cd19085 78 TPEDVRKSCERSLKRLGTDYIDLYQIHWPSSD-------------------VPLEETMEALEKLKEEGKIRAIGVSNFGP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 172 TNLERILKVAKVkpAVHQMELHPFL--PQTEFVEKHKKLGIHVTAYSPFG-------------NQNTIYESKIPKLIE-- 234
Cdd:cd19085 139 AQLEEALDAGRI--DSNQLPYNLLWraIEYEILPFCREHGIGVLAYSPLAqglltgkfssaedFPPGDARTRLFRHFEpg 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115800 235 -----HETIQKIAK-SKGEGVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFK--YIPLTKEDMDEINSIG 297
Cdd:cd19085 217 aeeetFEALEKLKEiADELGVTMAQLALAWVLQQPgvTSVIVGARNPEQLEENAAavDLELSPSVLERLDEIS 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
21-296 |
4.31e-40 |
|
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: 142.62 E-value: 4.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTW-------RSEPNQTKNAVKTALQYGYRHIDAAAIYG---NEDEVGDGIKesGVPRKDIWVTSKL---- 86
Cdd:COG0667 10 GLKVSRLGLGTMtfggpwgGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALK--GRPRDDVVIATKVgrrm 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 87 ----WCNAHAPEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDGNLiyeknPIEETWKAMEKLLETGKVR 162
Cdd:COG0667 88 gpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP--------------DPDT-----PIEETLGALDELVREGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 163 HIGLSNFNDTNLERILKVAK--VKPAVHQMELHPF--LPQTEFVEKHKKLGIHVTAYSPFGN------------------ 220
Cdd:COG0667 149 YIGVSNYSAEQLRRALAIAEglPPIVAVQNEYSLLdrSAEEELLPAARELGVGVLAYSPLAGglltgkyrrgatfpegdr 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 221 QNTIYESK--IPKLIEH-ETIQKIAKSKgeGVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFKY--IPLTKEDMDEI 293
Cdd:COG0667 229 AATNFVQGylTERNLALvDALRAIAAEH--GVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAadLELSAEDLAAL 306
|
...
gi 19115800 294 NSI 296
Cdd:COG0667 307 DAA 309
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
23-294 |
2.19e-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: 129.66 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 23 KIPGLGLGTW-----------RSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGvPRKDIWVTSKLWC 88
Cdd:cd19093 1 EVSPLGLGTWqwgdrlwwgygEYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG-DRDEVVIATKFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 89 NA--HAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFktgedkfpkdkdgnliyeKNPIEETWKAMEKLLETGKVRHIGL 166
Cdd:cd19093 80 LPwrLTRRSVVKALKASLERLGLDSIDLYQLHWPGPW------------------YSQIEALMDGLADAVEEGLVRAVGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 167 SNFNDTNLERI---LKVAKVKPAVHQME---LHPFLPQTEFVEKHKKLGIHVTAYSPF----------------GNQNTI 224
Cdd:cd19093 142 SNYSADQLRRAhkaLKERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLaqglltgkyspenpppGGRRRL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115800 225 YESKIPKLIE--HETIQKIAKSKgeGVTGATIAVSWAITRGTSVIPKSVNEQRIKSN-----FKyipLTKEDMDEIN 294
Cdd:cd19093 222 FGRKNLEKVQplLDALEEIAEKY--GKTPAQVALNWLIAKGVVPIPGAKNAEQAEENagalgWR---LSEEEVAELD 293
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
23-294 |
2.97e-35 |
|
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: 129.57 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 23 KIPGLGLGTW--------RSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESgvpRKDIWVTSK---LWC 88
Cdd:cd19084 3 KVSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKcglRWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 89 NAHA------PEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDGNLiyeknPIEETWKAMEKLLETGKVR 162
Cdd:cd19084 80 GGKGvtkdlsPESIRKEVEQSLRRLQTDYIDLYQIHWP--------------DPNT-----PIEETAEALEKLKKEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 163 HIGLSNFNDTNLERILKVAKVkpAVHQMELHPFLPQTE-----FVEKHkklGIHVTAYSPFG--------NQNTIYE--- 226
Cdd:cd19084 141 YIGVSNFSVEQLEEARKYGPI--VSLQPPYSMLEREIEeellpYCREN---GIGVLPYGPLAqglltgkyKKEPTFPpdd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 227 -------------SKIPKLIehETIQKIAKSKgeGVTGATIAVSWAITR--GTSVIPKSVNEQRIKSNFKY--IPLTKED 289
Cdd:cd19084 216 rrsrfpffrgenfEKNLEIV--DKLKEIAEKY--GKSLAQLAIAWTLAQpgVTSAIVGAKNPEQLEENAGAldWELTEEE 291
|
....*
gi 19115800 290 MDEIN 294
Cdd:cd19084 292 LKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
27-281 |
1.34e-33 |
|
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: 123.40 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTW----RSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGVpRKDIWVTSKL--------WCNAH 91
Cdd:cd06660 3 LGLGTMtfggDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-RDDVVIATKGghppggdpSRSRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 APEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDgnliyEKNPIEETWKAMEKLLETGKVRHIGLSNFND 171
Cdd:cd06660 82 SPEHIRRDLEESLRRLGTDYIDLYYLHRD--------------D-----PSTPVEETLEALNELVREGKIRYIGVSNWSA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 172 TNLERILKVAK----VKPAVHQMELHPFLPQ---TEFVEKHKKLGIHVTAYSPFGNqntiyeskipkliehetiqkiaks 244
Cdd:cd06660 143 ERLAEALAYAKahglPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLAR------------------------ 198
|
250 260 270
....*....|....*....|....*....|....*....
gi 19115800 245 kgeGVtgATIAVSWAITR--GTSVIPKSVNEQRIKSNFK 281
Cdd:cd06660 199 ---GP--AQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
20-296 |
2.22e-30 |
|
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: 117.16 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 20 DGSKIPGLGLGTW-------RSEPNQTKNAVKT-ALQYGYRHIDAAAIYG-NEDEVGDGIKESGVPRKDIWVTSK----- 85
Cdd:cd19144 9 NGPSVPALGFGAMglsafygPPKPDEERFAVLDaAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKfgiek 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 86 ------LWCNAhAPEAVPKALEKTLKDLKLDYLDEYLIHwpvsfktgedkfpkdkdgnLIYEKNPIEETWKAMEKLLETG 159
Cdd:cd19144 89 nvetgeYSVDG-SPEYVKKACETSLKRLGVDYIDLYYQH-------------------RVDGKTPIEKTVAAMAELVQEG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 160 KVRHIGLSnfnDTNLERILKVAKVKP--AVhQMELHPFL-----PQTEFVEKHKKLGIHVTAYSPFGN------------ 220
Cdd:cd19144 149 KIKHIGLS---ECSAETLRRAHAVHPiaAV-QIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRgfltgairspdd 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 221 -QNTIYESKIPKLIEH---------ETIQKIAKSKgeGVTGATIAVSWAITRGTSV--IPKSVNEQRIKSNFK--YIPLT 286
Cdd:cd19144 225 fEEGDFRRMAPRFQAEnfpknlelvDKIKAIAKKK--NVTAGQLTLAWLLAQGDDIipIPGTTKLKRLEENLGalKVKLT 302
|
330
....*....|
gi 19115800 287 KEDMDEINSI 296
Cdd:cd19144 303 EEEEKEIREI 312
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-296 |
8.26e-30 |
|
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: 115.08 E-value: 8.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTWRS---------EPNQTKNAVKT---ALQYGYRHIDAAAIYG---NEDEVGDGIKESgvpRKDIWVTSK---LW- 87
Cdd:cd19102 4 IGLGTWAIggggwgggwGPQDDRDSIAAiraALDLGINWIDTAAVYGlghSEEVVGRALKGL---RDRPIVATKcglLWd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 88 -----CNAHAPEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkdgnliYEKNPIEETWKAMEKLLETGKVR 162
Cdd:cd19102 81 eegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWP-------------------DPDEPIEEAWGALAELKEEGKVR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 163 HIGLSNFNDTNLERILK---VAKVKP---AVHQMELHPFLPqteFVEKHkklGIHVTAYSPFgnQNTIYESKI------- 229
Cdd:cd19102 142 AIGVSNFSVDQMKRCQAihpIASLQPpysLLRRGIEAEILP---FCAEH---GIGVIVYSPM--QSGLLTGKMtpervas 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 230 ---------------PKLIEH----ETIQKIAKSKgeGVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFKY--IPLT 286
Cdd:cd19102 214 lpaddwrrrspffqePNLARNlalvDALRPIAERH--GRTVAQLAIAWVLRRPevTSAIVGARRPDQIDETVGAadLRLT 291
|
330
....*....|
gi 19115800 287 KEDMDEINSI 296
Cdd:cd19102 292 PEELAEIEAL 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
20-293 |
4.96e-29 |
|
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: 113.08 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 20 DGSKIPGLGLG----TWRSEPNQTKNAVKT---ALQYGYRHIDAAAIYG---NEDEVGDGIKEsgvPRKDIWVTSK---L 86
Cdd:cd19076 8 QGLEVSALGLGcmgmSAFYGPADEEESIATlhrALELGVTFLDTADMYGpgtNEELLGKALKD---RRDEVVIATKfgiV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 87 WCNAHA-------PEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDGNLiyeknPIEETWKAMEKLLETG 159
Cdd:cd19076 85 RDPGSGfrgvdgrPEYVRAACEASLKRLGTDVIDLYYQHRV--------------DPNV-----PIEETVGAMAELVEEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 160 KVRHIGLSNFNDTNLERILKVAKVKpAVhQMELHPFL--PQTEFVEKHKKLGIHVTAYSPFGN-------------QNTI 224
Cdd:cd19076 146 KVRYIGLSEASADTIRRAHAVHPIT-AV-QSEYSLWTrdIEDEVLPTCRELGIGFVAYSPLGRgfltgaikspedlPEDD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 225 YESKIPKLI-EH--------ETIQKIAKSKgeGVTGATIAVSWAITRGTSVIP----KSVneQRIKSNFKY--IPLTKED 289
Cdd:cd19076 224 FRRNNPRFQgENfdknlklvEKLEAIAAEK--GCTPAQLALAWVLAQGDDIVPipgtKRI--KYLEENVGAldVVLTPEE 299
|
....
gi 19115800 290 MDEI 293
Cdd:cd19076 300 LAEI 303
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
28-289 |
1.16e-24 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 101.00 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 28 GLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGVPRKDIWVTSKlwC-----NAHAPEAVP-- 97
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLSPSLREKIELQTK--CgirlpSEARDNRVKhy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 98 --------KALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDgnliyeknP---IEETWKAMEKLLETGKVRHIGL 166
Cdd:COG4989 100 dtskehiiASVEGSLRRLGTDYLDLLLLHRP--------------D--------PlmdPEEVAEAFDELKASGKVRHFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 167 SNFNDTNLERILKVAKVKPAVHQMELHPFlpQTEFVEK-----HKKLGIHVTAYSPFGNQN--TIYESKIPKLieHETIQ 239
Cdd:COG4989 158 SNFTPSQFELLQSALDQPLVTNQIELSLL--HTDAFDDgtldyCQLNGITPMAWSPLAGGRlfGGFDEQFPRL--RAALD 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19115800 240 KIAKSKgeGVTGATIAVSWaITR---GTSVIPKSVNEQRIKSNFKY--IPLTKED 289
Cdd:COG4989 234 ELAEKY--GVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAAldIELTREE 285
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
28-296 |
1.89e-24 |
|
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: 100.46 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 28 GLGTWR--------SEPNQTKNAVKTALQYGYRHIDAAAIYG---NEDEVGDGIKESGvPRKDIWVTSKL---WCNAH-- 91
Cdd:cd19148 8 ALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKEYG-KRDRVVIATKVgleWDEGGev 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 ----APEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDgnliyEKNPIEETWKAMEKLLETGKVRHIGLS 167
Cdd:cd19148 87 vrnsSPARIRKEVEDSLRRLQTDYIDLYQVHWP--------------D-----PLVPIEETAEALKELLDEGKIRAIGVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 168 NFNDTNLERILKVAKVkpAVHQMELHPFLPQTE-----FVEKHkklGIHVTAYSPFG--------NQNTIYE-----SKI 229
Cdd:cd19148 148 NFSPEQMETFRKVAPL--HTVQPPYNLFEREIEkdvlpYARKH---NIVTLAYGALCrgllsgkmTKDTKFEgddlrRTD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 230 PKLIEH---------ETIQKIAKSKGeGVTGATIAVSWAITRGTSVI-------PKSVNEqrIKSNFKYiPLTKEDMDEI 293
Cdd:cd19148 223 PKFQEPrfsqylaavEELDKLAQERY-GKSVIHLAVRWLLDQPGVSIalwgarkPEQLDA--VDEVFGW-SLNDEDMKEI 298
|
...
gi 19115800 294 NSI 296
Cdd:cd19148 299 DAI 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
19-289 |
2.55e-23 |
|
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: 97.24 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 19 ADGSKIPGLGLGTWR-----SEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGVPRKDIWVTSK----- 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRladwgESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKcgirl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 86 -----LWCNAH---APEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDgnliYEKNPiEETWKAMEKLLE 157
Cdd:cd19092 81 gddprPGRIKHydtSKEHILASVEGSLKRLGTDYLDLLLLHRP--------------D----PLMDP-EEVAEAFDELVK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 158 TGKVRHIGLSNFNDTNLERILKVAKVKPAVHQME---LHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNtIYESKIPKLIE 234
Cdd:cd19092 142 SGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLGGGR-LFGGFDERFQR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115800 235 -HETIQKIAKSKgeGVTGATIAVSWaITR---GTSVIPKSVNEQRIKSNFK--YIPLTKED 289
Cdd:cd19092 221 lRAALEELAEEY--GVTIEAIALAW-LLRhpaRIQPILGTTNPERIRSAVKalDIELTREE 278
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
26-294 |
8.15e-23 |
|
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: 96.15 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 26 GLGLG--TWRSEPNQTKNA---VKTALQYGYRHIDAAAIYGNEDE------VGDGIKESGVPRKDIWVTSKLWCNAHA-- 92
Cdd:cd19077 9 GLGLMglTWRPNPTPDEEAfetMKAALDAGSNLWNGGEFYGPPDPhanlklLARFFRKYPEYADKVVLSVKGGLDPDTlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 ----PEAVPKALEKTLKDLK-LDYLDeylihwpvsfktgedkfpkdkdgnlIYE------KNPIEETWKAMEKLLETGKV 161
Cdd:cd19077 89 pdgsPEAVRKSIENILRALGgTKKID-------------------------IFEparvdpNVPIEETIKALKELVKEGKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 162 RHIGLSNFNDTNLERILKVAKVkpAVHQMELHPF---LPQTEFVEKHKKLGIHVTAYSPFG---------NQNTIYESKI 229
Cdd:cd19077 144 RGIGLSEVSAETIRRAHAVHPI--AAVEVEYSLFsreIEENGVLETCAELGIPIIAYSPLGrglltgrikSLADIPEGDF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 230 --------PKLIEH-----ETIQKIAKSKgeGVTGATIAVSWAITRGTSVI---PKSVNEQRIKSNFK--YIPLTKEDMD 291
Cdd:cd19077 222 rrhldrfnGENFEKnlklvDALQELAEKK--GCTPAQLALAWILAQSGPKIipiPGSTTLERVEENLKaaNVELTDEELK 299
|
...
gi 19115800 292 EIN 294
Cdd:cd19077 300 EIN 302
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
37-295 |
3.99e-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: 94.22 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 37 NQTKNAVKTALQYGYRHIDAAAIYG---NEDEVGDGIKEsgvPRKDIWVTSKL-WCNAH----------APEAVPKALEK 102
Cdd:cd19078 25 EEMIELIRKAVELGITFFDTAEVYGpytNEELVGEALKP---FRDQVVIATKFgFKIDGgkpgplgldsRPEHIRKAVEG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 103 TLKDLKLDYLDEYLIHWPvsfktgedkfpkDKDgnliyekNPIEETWKAMEKLLETGKVRHIGLSnfnDTNLERILKVAK 182
Cdd:cd19078 102 SLKRLQTDYIDLYYQHRV------------DPN-------VPIEEVAGTMKELIKEGKIRHWGLS---EAGVETIRRAHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 183 VKP--AVhQMELHPFL--PQTEFVEKHKKLGIHVTAYSPFG--------NQNTIYESK---------IPKLIEH-----E 236
Cdd:cd19078 160 VCPvtAV-QSEYSMMWrePEKEVLPTLEELGIGFVPFSPLGkgfltgkiDENTKFDEGddraslprfTPEALEAnqalvD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115800 237 TIQKIAKSKgeGVTGATIAVSWAITRGTSV--IPKSVNEQRIKSNFK--YIPLTKEDMDEINS 295
Cdd:cd19078 239 LLKEFAEEK--GATPAQIALAWLLAKKPWIvpIPGTTKLSRLEENIGaaDIELTPEELREIED 299
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
21-295 |
3.00e-20 |
|
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: 89.25 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTW---------RSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESgvpRKDIWVTSK--- 85
Cdd:cd19149 8 GIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKcgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 86 LWCNAH----------------APEAVPKALEKTLKDLKLDYLDEYLIHWP-VSFktgedkfpkdkdgnliyeknPIEET 148
Cdd:cd19149 85 RWDREGgsfffvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQdVET--------------------PIEET 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 149 WKAMEKLLETGKVRHIGLSNFNDTNLERILKVAKVkpAVHQME---LHPFLpQTEFVEKHKKLGIHVTAYSPFG------ 219
Cdd:cd19149 145 MEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQEKysmLDRGI-EKELLPYCKKNNIAFQAYSPLEqglltg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 220 --NQNTIYE-----SKIPkLIEHETIQKIAKSKGE--------GVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFK- 281
Cdd:cd19149 222 kiTPDREFDagdarSGIP-WFSPENREKVLALLEKwkplcekyGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKa 300
|
330
....*....|....*
gi 19115800 282 -YIPLTKEDMDEINS 295
Cdd:cd19149 301 gDIRLSAEDIATMRS 315
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-167 |
4.26e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 87.64 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQTkNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKesGVPRKDIWVTSKLWC--NAHAPEA 95
Cdd:cd19105 10 GLKVSRLGFGGGGLPRESP-ELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASPrlDKKDKAE 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115800 96 VPKALEKTLKDLKLDYLDEYLIHWPvsfkTGEDKFPKDkdgnliyeknpiEETWKAMEKLLETGKVRHIGLS 167
Cdd:cd19105 87 LLKSVEESLKRLQTDYIDIYQLHGV----DTPEERLLN------------EELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-219 |
4.82e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 87.15 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGT---WRSEPNQTKNAVKTALQYGYRHIDAAAIYGN-EDEVGDGIKEsgvPRKDIWVTSKLWcnAHAPEAV 96
Cdd:cd19100 8 GLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTG--ARDYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 97 PKALEKTLKDLKLDYLDEYLIHWPVSfktgedkfpkDKDGNLIYEKNPIeetWKAMEKLLETGKVRHIGLSNFNDTNLER 176
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHAVDT----------EEDLDQVFGPGGA---LEALLEAKEEGKIRFIGISGHSPEVLLR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19115800 177 ILKVAKVkpAVHQMELHPFLPQ-----TEFVEKHKKLGIHVTAYSPFG 219
Cdd:cd19100 150 ALETGEF--DVVLFPINPAGDHidsfrEELLPLAREKGVGVIAMKVLA 195
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
27-293 |
9.46e-20 |
|
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: 87.49 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTWRSEPNQTKNA---VKTALQYGYRHIDAAAIYG---NEDEVGDGIKesGVPRKDIWVTSKLWCNAHA-------- 92
Cdd:cd19145 20 MGLSGDYGAPKPEEEGialIHHAFNSGVTFLDTSDIYGpntNEVLLGKALK--DGPREKVQLATKFGIHEIGgsgvevrg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 -PEAVPKALEKTLKDLKLDYLDEYLIHwpvsfktgedkfpkdkdgnLIYEKNPIEETWKAMEKLLETGKVRHIGLSnfnD 171
Cdd:cd19145 98 dPAYVRAACEASLKRLDVDYIDLYYQH-------------------RIDTTVPIEITMGELKKLVEEGKIKYIGLS---E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 172 TNLERILKVAKVKP--AVhQME--LHPFLPQTEFVEKHKKLGIHVTAYSPFGN-------------QNTIYESKIPKL-- 232
Cdd:cd19145 156 ASADTIRRAHAVHPitAV-QLEwsLWTRDIEEEIIPTCRELGIGIVPYSPLGRgffagkakleellENSDVRKSHPRFqg 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115800 233 --IEH-----ETIQKIAKSKgeGVTGATIAVSWAITRGTSV--IPKSVNEQRIKSNFKYIP--LTKEDMDEI 293
Cdd:cd19145 235 enLEKnkvlyERVEALAKKK--GCTPAQLALAWVLHQGEDVvpIPGTTKIKNLNQNIGALSvkLTKEDLKEI 304
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
27-296 |
1.77e-19 |
|
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: 86.84 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTW-----RSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGdgikESGVPRKDIWVTSK---LWCNAHAPEA 95
Cdd:cd19075 5 LGTMTFgsqgrFTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLG----ELGLGERGFKIDTKanpGVGGGLSPEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 96 VPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDgnliyEKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLE 175
Cdd:cd19075 81 VRKQLETSLKRLKVDKVDVFYLHAP--------------D-----RSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 176 RILKVAK----VKPAVHQ-M----------ELHPFLpqtefvekhKKLGIHVTAYSP---------------------F- 218
Cdd:cd19075 142 EIVEICKengwVLPTVYQgMynaitrqvetELFPCL---------RKLGIRFYAYSPlaggfltgkykysedkagggrFd 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 219 --GNQNTIYESKIPKLIEHETIQKI-AKSKGEGVTGATIAVSWAI-------TRGTSVIPKSVNEQRIKSNFKYI---PL 285
Cdd:cd19075 213 pnNALGKLYRDRYWKPSYFEALEKVeEAAEKEGISLAEAALRWLYhhsaldgEKGDGVILGASSLEQLEENLAALekgPL 292
|
330
....*....|.
gi 19115800 286 TKEDMDEINSI 296
Cdd:cd19075 293 PEEVVKAIDEA 303
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
23-174 |
1.30e-18 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 85.26 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 23 KIPGLGLGTWRSEPNQTKNAVKT---ALQYGYRHIDAAAIYGN-EDEVGDGIKEsgvPRKDIWVTSKLWCNAHAPEAVPK 98
Cdd:COG1453 12 EVSVLGFGGMRLPRKDEEEAEALirrAIDNGINYIDTARGYGDsEEFLGKALKG---PRDKVILATKLPPWVRDPEDMRK 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115800 99 ALEKTLKDLKLDYLDEYLIHwpvSFKTGEDkFPKDKDGNLIYEknpieetwkAMEKLLETGKVRHIGLSNFNDTNL 174
Cdd:COG1453 89 DLEESLKRLQTDYIDLYLIH---GLNTEED-LEKVLKPGGALE---------ALEKAKAEGKIRHIGFSTHGSLEV 151
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
40-296 |
2.86e-18 |
|
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: 83.62 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 40 KNAVKTALQYGYRHIDAAAIYG---NEDEVGDGIKESGvpRKDIWVTSKlwcNAH-----------APEAVPKALEKTLK 105
Cdd:cd19083 36 KDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYN--RNEVVIATK---GAHkfggdgsvlnnSPEFLRSAVEKSLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 106 DLKLDYLDEYLIHWPvsfktgedkfpkdkDGNliyekNPIEETWKAMEKLLETGKVRHIGLSNFndtNLERiLKVAKVKP 185
Cdd:cd19083 111 RLNTDYIDLYYIHFP--------------DGE-----TPKAEAVGALQELKDEGKIRAIGVSNF---SLEQ-LKEANKDG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 186 AVHQMElHPF-LPQTEfVEKH-----KKLGIHVTAYSP--FG------NQNTIYE-----SKIPKLIEH---ETIQKIAK 243
Cdd:cd19083 168 YVDVLQ-GEYnLLQRE-AEEDilpycVENNISFIPYFPlaSGllagkyTKDTKFPdndlrNDKPLFKGErfsENLDKVDK 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115800 244 SK----GEGVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19083 246 LKsiadEKGVTVAHLALAWYLTRPaiDVVIPGAKRAEQVIDNLKAldVTLTEEEIAFIDAL 306
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
21-268 |
1.09e-17 |
|
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: 81.86 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGT----------WRSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGvPRKDIWVTSKLw 87
Cdd:cd19079 9 GLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-PRDEVVIATKV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 88 CNAHAP---------EAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkDKDgnliyekNPIEETWKAMEKLLET 158
Cdd:cd19079 87 YFPMGDgpngrglsrKHIMAEVDASLKRLGTDYIDLYQIHRW------------DYE-------TPIEETLEALHDVVKS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 159 GKVRHIGLSNFNDTNLERILKVAKV----KPAVhqMELHPFLPQTE-------FVEKHkklGIHVTAYSP---------- 217
Cdd:cd19079 148 GKVRYIGASSMYAWQFAKALHLAEKngwtKFVS--MQNHYNLLYREeeremipLCEEE---GIGVIPWSPlargrlarpw 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115800 218 -FGNQNTIYESKIPKLIEHET----------IQKIAKSKgeGVTGATIAVSWAITRGTSVIP 268
Cdd:cd19079 223 gDTTERRRSTTDTAKLKYDYFteadkeivdrVEEVAKER--GVSMAQVALAWLLSKPGVTAP 282
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
21-267 |
5.36e-17 |
|
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: 79.56 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRS-----EPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKesGVPRKDIWVTSKL------ 86
Cdd:cd19074 1 GLKVSELSLGTWLTfggqvDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfwptgp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 87 WCN------AHAPEAVpkalEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkdgnliYEKNPIEETWKAMEKLLETGK 160
Cdd:cd19074 79 GPNdrglsrKHIFESI----HASLKRLQLDYVDIYYCHRY-------------------DPETPLEETVRAMDDLIRQGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 161 VRHIGLSNFNDTNLERILKVAK----VKPAVHQMELHPFL--PQTEFVEKHKKLGIHVTAYSPFgNQNTI---YESKIP- 230
Cdd:cd19074 136 ILYWGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYNMLWreIEEEVIPLCEKNGIGLVVWSPL-AQGLLtgkYRDGIPp 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115800 231 -------------KLIEHETIQKIAKSKG-------EGVTGATIAVSWAITR--GTSVI 267
Cdd:cd19074 215 psrsratdednrdKKRRLLTDENLEKVKKlkpiadeLGLTLAQLALAWCLRNpaVSSAI 273
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
27-178 |
7.41e-17 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 78.76 E-value: 7.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTWR--------SEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKEsgVPRKDIWVTSKL-WCNAHAPE 94
Cdd:cd19096 3 LGFGTMRlpesdddsIDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE--GPREKFYLATKLpPWSVKSAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 95 AVPKALEKTLKDLKLDYLDEYLIHWPVSfktgEDKFPKDKDGNLiyeknpieetWKAMEKLLETGKVRHIGLSnFNDT-- 172
Cdd:cd19096 81 DFRRILEESLKRLGVDYIDFYLLHGLNS----PEWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS-FHDSpe 145
|
....*.
gi 19115800 173 NLERIL 178
Cdd:cd19096 146 LLKEIL 151
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
21-296 |
1.84e-16 |
|
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: 78.42 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGT-------------WRSEPNQTKNAVKTALQYGYRHIDAAAIY--------------GNEDEV------- 66
Cdd:cd19091 10 GLKVSELALGTmtfgggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYsegeseeilgkalkGRRDDVliatkvr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 67 ---GDGIKESGVPRKDIWvtsklwcnahapeavpKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDGnliyeKN 143
Cdd:cd19091 90 grmGEGPNDVGLSRHHII----------------RAVEASLKRLGTDYIDLYQLHGF--------------DA-----LT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 144 PIEETWKAMEKLLETGKVRHIGLSNFNDTNLERILKVAK----VKPAVHQM-----------ELHPFLpqtefveKHKKL 208
Cdd:cd19091 135 PLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQAyysllgrdlehELMPLA-------LDQGV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 209 GIHVtaYSPFGN--------------QNTIYESK----IPKLIEH-----ETIQKIAksKGEGVTGATIAVSWAITR--G 263
Cdd:cd19091 208 GLLV--WSPLAGgllsgkyrrgqpapEGSRLRRTgfdfPPVDRERgydvvDALREIA--KETGATPAQVALAWLLSRptV 283
|
330 340 350
....*....|....*....|....*....|....*
gi 19115800 264 TSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19091 284 SSVIIGARNEEQLEDNLGAagLSLTPEEIARLDKV 318
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
27-218 |
3.42e-16 |
|
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: 76.36 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTWR--------SEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKEsgvPRKDIWVTSKLWCNAHA--- 92
Cdd:cd19086 6 IGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFGNRFDGgpe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 ------PEAVPKALEKTLKDLKLDYLDEYLIH-WPVSFktgedkfpkdkdgnliyekNPIEETWKAMEKLLETGKVRHIG 165
Cdd:cd19086 83 rpqdfsPEYIREAVEASLKRLGTDYIDLYQLHnPPDEV-------------------LDNDELFEALEKLKQEGKIRAYG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115800 166 LSNFNDTNLERILKVAKVkpAVHQMELHPF--LPQTEFVEKHKKLGIHVTAYSPF 218
Cdd:cd19086 144 VSVGDPEEALAALRRGGI--DVVQVIYNLLdqRPEEELFPLAEEHGVGVIARVPL 196
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
44-296 |
4.21e-16 |
|
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: 77.23 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 44 KTALQYGYRHIDAAAIYGN---EDEVGDGIKESgvpRKDIWVTSKL------WCNAHAPEA--VPKALEKTLKDLKLDYL 112
Cdd:cd19087 37 DRALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKVfgpmgdDPNDRGLSRrhIRRAVEASLRRLQTDYI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 113 DEYLIHwpvsfktgedkfpkdkdgnLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLERILKVAKV----KPAVH 188
Cdd:cd19087 114 DLYQMH-------------------HFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARrgllRFVSE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 189 Q-----------MELHPfLPQTEfvekhkklGIHVTAYSPFG--------------NQNTIYESKIPKLIE-----HETI 238
Cdd:cd19087 175 QpmynllkrqaeLEILP-AARAY--------GLGVIPYSPLAgglltgkygkgkrpESGRLVERARYQARYgleeyRDIA 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115800 239 QKIAKSKGE-GVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19087 246 ERFEALAAEaGLTPASLALAWVLSHPavTSPIIGPRTLEQLEDSLAAleITLTPELLAEIDEL 308
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
22-296 |
4.36e-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: 77.61 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 22 SKIpGLGLGTWrSEPNQTKNAVKT---ALQYGYRHIDAAAIY---------GNEDE-VGDGIKESGvPRKDIWVTSKL-- 86
Cdd:cd19094 2 SEI-CLGTMTW-GEQNTEAEAHEQldyAFDEGVNFIDTAEMYpvppspetqGRTEEiIGSWLKKKG-NRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 87 ------WCN----AHAPEAVPKALEKTLKDLKLDYLDEYLIHWP---VSFKTGEDKFPKDKDGNLIyeknPIEETWKAME 153
Cdd:cd19094 79 pgegitWPRgggtRLDRENIREAVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEEEDSV----SFEEQLEALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 154 KLLETGKVRHIGLSNFNDTNLERILKVAKV----KPAVHQmelHPF-LPQTEFVEKHKKLGIHVT----AYSPFG----- 219
Cdd:cd19094 155 ELVKAGKIRHIGLSNETPWGVMKFLELAEQlglpRIVSIQ---NPYsLLNRNFEEGLAEACHRENvgllAYSPLAggvlt 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 220 -------NQNTI------------YESkiPKLIEH-ETIQKIAKSkgEGVTGATIAVSWAITR---GTSVIPKSVNEQrI 276
Cdd:cd19094 232 gkyldgaARPEGgrlnlfpgymarYRS--PQALEAvAEYVKLARK--HGLSPAQLALAWVRSRpfvTSTIIGATTLEQ-L 306
|
330 340
....*....|....*....|..
gi 19115800 277 KSNFKY--IPLTKEDMDEINSI 296
Cdd:cd19094 307 KENIDAfdVPLSDELLAEIDAV 328
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
21-296 |
1.43e-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: 76.10 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQT-----KNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGVPRKDIWVTSKLWCNAHA 92
Cdd:cd19143 10 GLKVSALSFGSWVTFGNQVdvdeaKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIFWGGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 PEA---------VPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkDKDGnliyeknPIEETWKAMEKLLETGKVRH 163
Cdd:cd19143 90 PPPndrglsrkhIVEGTKASLKRLQLDYVDLVFCHRP------------DPAT-------PIEETVRAMNDLIDQGKAFY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 164 IGLSNFNDTNLERILKVAK----VKPAVHQMELHPFlpQTEFVEK-----HKKLGIHVTAYSP----------------- 217
Cdd:cd19143 151 WGTSEWSAQQIEEAHEIADrlglIPPVMEQPQYNLF--HRERVEVeyaplYEKYGLGTTTWSPlasglltgkynngipeg 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 218 --FGNQNTIYESKIPKLIEHETIQKIAK----SKGEGVTGATIAVSWAIT--RGTSVIPKSVNEQRIKSNFKYIP----L 285
Cdd:cd19143 229 srLALPGYEWLKDRKEELGQEKIEKVRKlkpiAEELGCSLAQLAIAWCLKnpNVSTVITGATKVEQLEENLKALEvlpkL 308
|
330
....*....|.
gi 19115800 286 TKEDMDEINSI 296
Cdd:cd19143 309 TPEVMEKIEAI 319
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
24-281 |
4.96e-15 |
|
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: 73.41 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 24 IPGLGLGTWR----------SEPNQTKNAVKTALQYGYRHIDAAAIYG---NEDEVGDGIKESGvprKDIWVTSKL---- 86
Cdd:cd19088 1 VSRLGYGAMRltgpgiwgppADREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYP---DDVVIATKGglvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 87 -----WCNAHAPEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkDKDGnliyeknPIEETWKAMEKLLETGKV 161
Cdd:cd19088 78 tgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI------------DPKV-------PFEEQLGALAELQDEGLI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 162 RHIGLSNFNDTNLERILKVAKVkpAVHQMELHPFLPQTEFV-EKHKKLGIHVTAYSPFGNQntiyeskiPKLIEHETIQK 240
Cdd:cd19088 139 RHIGLSNVTVAQIEEARAIVRI--VSVQNRYNLANRDDEGVlDYCEAAGIAFIPWFPLGGG--------DLAQPGGLLAE 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 19115800 241 IAKSKgeGVTGATIAVSWAITRGTSV--IPKSVNEQRIKSNFK 281
Cdd:cd19088 209 VAARL--GATPAQVALAWLLARSPVMlpIPGTSSVEHLEENLA 249
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
25-279 |
1.28e-14 |
|
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: 72.27 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 25 PGLGLGTWR--------SEPnQTKNAVKTALQYGYRHIDAAAIYGN-EDEVGDGIkeSGVPRKDIWVTSKLWCN------ 89
Cdd:cd19095 1 SVLGLGTSGigrvwgvpSEA-EAARLLNTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGTHgeggrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 90 --AHAPEAVPKALEKTLKDLKLDYLDEYLIHWPVsfktgedkfPKDKDGNLIyeknpieetwKAMEKLLETGKVRHIGLS 167
Cdd:cd19095 78 rkDFSPAAIRASIERSLRRLGTDYIDLLQLHGPS---------DDELTGEVL----------ETLEDLKAAGKVRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 168 NFNDtNLERILKVAKVkpAVHQMELHPFLPQTEFV-EKHKKLGIHVTAYSPFGNQNTIYESKIPKLIEHETIQKIAKSKG 246
Cdd:cd19095 139 GDGE-ELEAAIASGVF--DVVQLPYNVLDREEEELlPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEI 215
|
250 260 270
....*....|....*....|....*....|....*
gi 19115800 247 EGVTGATIAVSWAITRG--TSVIPKSVNEQRIKSN 279
Cdd:cd19095 216 GGATWAQAALRFVLSHPgvSSAIVGTTNPEHLEEN 250
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
21-294 |
2.37e-14 |
|
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: 72.25 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGT----WRSEPNQTKNAVKTALQYGYRHIDAAAIYGN----------EDEVGDGIKESGvPRKDIWVTSKL 86
Cdd:cd19081 6 GLSVSPLCLGTmvfgWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKSRG-KRDRVVIATKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 87 WCNAHA------PEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDGNLiyeknPIEETWKAMEKLLETGK 160
Cdd:cd19081 85 GFPMGPngpglsRKHIRRAVEASLRRLQTDYIDLYQAHWD--------------DPAT-----PLEETLGALNDLIRQGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 161 VRHIGLSNFNDTNLERILKVAKvkpavhQMELHPFL---PQTEFVEKH----------KKLGIHVTAYSPF------GNQ 221
Cdd:cd19081 146 VRYIGASNYSAWRLQEALELSR------QHGLPRYVslqPEYNLVDREsfegellplcREEGIGVIPYSPLaggfltGKY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 222 NTiyESKIPKLIE----------------HETIQKIAKSKgeGVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFKY- 282
Cdd:cd19081 220 RS--EADLPGSTRrgeaakrylnerglriLDALDEVAAEH--GATPAQVALAWLLARPgvTAPIAGARTVEQLEDLLAAa 295
|
330
....*....|...
gi 19115800 283 -IPLTKEDMDEIN 294
Cdd:cd19081 296 gLRLTDEEVARLD 308
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
21-294 |
1.01e-13 |
|
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: 70.36 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWR-----SEPNQTKNAVKTALQYGYRHIDAAAIYGN-----EDEVGDGIKESGVPRKD-IWVTSK---- 85
Cdd:cd19089 8 GLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRPYRDeLVISTKagyg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 86 LWCNAHAPEAVPK----ALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkDKDgnliyekNPIEETWKAMEKLLETGKV 161
Cdd:cd19089 88 MWPGPYGDGGSRKyllaSLDQSLKRMGLDYVDIFYHHRY------------DPD-------TPLEETMTALADAVRSGKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 162 RHIGLSNFNDTNLERILKV---AKVKPAVHQMELHPFLPQTE--FVEKHKKLGIHVTAYSP------------------- 217
Cdd:cd19089 149 LYVGISNYPGAKARRAIALlreLGVPLIIHQPRYSLLDRWAEdgLLEVLEEAGIGFIAFSPlaqglltdkylngippdsr 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 218 ------FGNQNTIYESKIPKLiehETIQKIAKSKGEgvTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFKYIPLTKED 289
Cdd:cd19089 229 raaeskFLTEEALTPEKLEQL---RKLNKIAAKRGQ--SLAQLALSWVLRDPrvTSVLIGASSPSQLEDNVAALKNLDFS 303
|
....*
gi 19115800 290 MDEIN 294
Cdd:cd19089 304 EEELA 308
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-297 |
1.39e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 66.97 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 23 KIPGLGLGTW---------------RSEPNQTKNAVKTALQYGYRHIDAAAIYG---NEDEVGDGIKEsgVPRKDIWVTS 84
Cdd:cd19103 3 KLPKIALGTWswgsggaggdqvfgnHLDEDTLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR--YPREDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 85 KL--WCNAHAPEAVPKALEKTLKDLKLDYLDEYLIHWPVsfktgedkfpkDKDGNLIYeknpieetwkaMEKLLETGKVR 162
Cdd:cd19103 81 KFtpQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPA-----------DVERWTPE-----------LIPLLKSGKVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 163 HIGLSNFNDTNLER---ILKVAKVK-PAV--HQMELHPFLPQTEFVEKHKKLGIHVTAY---------SPFGNQNTI--- 224
Cdd:cd19103 139 HVGVSNHNLAEIKRaneILAKAGVSlSAVqnHYSLLYRSSEEAGILDYCKENGITFFAYmvleqgalsGKYDTKHPLpeg 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 225 ------YESKIPKLIE-HETIQKIAKSKgeGVTGATIAVSWAITRGTSVI-----PKSVNE-QRIKSnfkyIPLTKEDMD 291
Cdd:cd19103 219 sgraetYNPLLPQLEElTAVMAEIGAKH--GASIAQVAIAWAIAKGTTPIigvtkPHHVEDaARAAS----ITLTDDEIK 292
|
....*.
gi 19115800 292 EINSIG 297
Cdd:cd19103 293 ELEQLA 298
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-219 |
3.42e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 66.19 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTWRSEPNQT-----KNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKES----GVPRKDIWVTSK--------- 85
Cdd:cd19099 6 LGLGTYRGDSDDEtdeeyREALKAALDSGINVIDTAINYRGgrsERLIGKALRELiekgGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 86 ---------LWCNAHAPEAV-----------PK----ALEKTLKDLKLDYLDEYLIHWPVSF--KTGEDKFpkdkdgnli 139
Cdd:cd19099 86 eplrplkylEEKLGRGLIDVadsaglrhcisPAyledQIERSLKRLGLDTIDLYLLHNPEEQllELGEEEF--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 140 YEKnpIEETWKAMEKLLETGKVRHIGLSNFN----DTNLERILKVAKVKPAVH------------QMELHPFLPQ----- 198
Cdd:cd19099 157 YDR--LEEAFEALEEAVAEGKIRYYGISTWDgfraPPALPGHLSLEKLVAAAEevggdnhhfkviQLPLNLLEPEaltek 234
|
250 260
....*....|....*....|....*...
gi 19115800 199 -------TEFVEKHKKLGIHVTAYSPFG 219
Cdd:cd19099 235 ntvkgeaLSLLEAAKELGLGVIASRPLN 262
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-218 |
4.62e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 65.24 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTW-------------RSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVgdgIKESGVPRKDIWVTSKL----WCN 89
Cdd:cd19097 3 LALGTAqfgldygianksgKPSEKEAKKILEYALKAGINTLDTAPAYGDSEKV---LGKFLKRLDKFKIITKLpplkEDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 90 AHAPEAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkdgNLIYEKNPieETWKAMEKLLETGKVRHIGLSNF 169
Cdd:cd19097 80 KEDEAAIEASVEASLKRLKVDSLDGLLLHNP----------------DDLLKHGG--KLVEALLELKKEGLIRKIGVSVY 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115800 170 NDTNLERILKvaKVKPAVHQMELHPF---LPQTEFVEKHKKLGIHVTAYSPF 218
Cdd:cd19097 142 SPEELEKALE--SFKIDIIQLPFNILdqrFLKSGLLAKLKKKGIEIHARSVF 191
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
27-294 |
6.14e-12 |
|
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: 65.32 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGT--------WRSEPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESgvpRKDIWVTSKLWCNAHAP-- 93
Cdd:cd19080 13 LALGTmtfgtewgWGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKYTMNRRPGdp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 94 -------EAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDGNliyekNPIEETWKAMEKLLETGKVRHIGL 166
Cdd:cd19080 90 naggnhrKNLRRSVEASLRRLQTDYIDLLYVHAW--------------DFT-----TPVEEVMRALDDLVRAGKVLYVGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 167 SNFNDTNLERILKVAKVK----PAVHQMELHpfL----PQTEFVEKHKKLGIHVTAYSPFG----------------NQN 222
Cdd:cd19080 151 SDTPAWVVARANTLAELRgwspFVALQIEYS--LlertPERELLPMARALGLGVTPWSPLGgglltgkyqrgeegraGEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 223 TIYESKIPKLIEH-----ETIQKIAKSKgeGVTGATIAVSWAITRGTSVIP---KSVNEQrIKSNFKY--IPLTKEDMDE 292
Cdd:cd19080 229 KGVTVGFGKLTERnwaivDVVAAVAEEL--GRSAAQVALAWVRQKPGVVIPiigARTLEQ-LKDNLGAldLTLSPEQLAR 305
|
..
gi 19115800 293 IN 294
Cdd:cd19080 306 LD 307
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
21-232 |
3.28e-11 |
|
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: 63.25 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRS-----EPNQTKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGVPRKDIWVTSKLWCNAHA 92
Cdd:cd19142 10 GLRVSNVGLGTWSTfstaiSEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIYWSYGS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 PEA------VPKALEKTLKDLKLDYLDEYLIHwpvsfktgedkfpkdkdgnliyeKN----PIEETWKAMEKLLETGKVR 162
Cdd:cd19142 90 EERglsrkhIIESVRASLRRLQLDYIDIVIIH-----------------------KAdpmcPMEEVVRAMSYLIDNGLIM 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115800 163 HIGLSNFNDTNLERILKVAK----VKPAVHQMELHPFLPQT---EFVEKHKKLGIHVTAYSPF--GNQNTIYESKIPKL 232
Cdd:cd19142 147 YWGTSRWSPVEIMEAFSIARqfncPTPICEQSEYHMFCREKmelYMPELYNKVGVGLITWSPLslGLDPGISEETRRLV 225
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-167 |
5.24e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 62.67 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLG------TW-RSEPNQTKNAVKTALQYGYRHIDAAAIYGN-EDEVGDGIKESGVPrKDIWVTSKLWCNAHA 92
Cdd:cd19104 9 GLKVSELTFGgggiggLMgRTTREEQIAAVRRALDLGINFFDTAPSYGDgKSEENLGRALKGLP-AGPYITTKVRLDPDD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 PEAVP----KALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKF----PKDKDGnliyeknpIEETWKAMEKLLETGKVRHI 164
Cdd:cd19104 88 LGDIGgqieRSVEKSLKRLKRDSVDLLQLHNRIGDERDKPVGgtlsTTDVLG--------LGGVADAFERLRSEGKIRFI 159
|
...
gi 19115800 165 GLS 167
Cdd:cd19104 160 GIT 162
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-182 |
1.03e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 61.58 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTW----RSEPNQTKNAVKTALQYGYRHIDAAAIY--------GNEDE--VGDGIKESGVpRKDIWVTSKlwCNAH- 91
Cdd:cd19752 3 LCLGTMyfgtRTDEETSFAILDRYVAAGGNFLDTANNYafwteggvGGESErlIGRWLKDRGN-RDDVVIATK--VGAGp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 -------------APEAVPKALEKTLKDLKLDYLDEYLIHwpvsfktgedkfpkdkdgnlIYEKN-PIEETWKAMEKLLE 157
Cdd:cd19752 80 rdpdggpespeglSAETIEQEIDKSLRRLGTDYIDLYYAH--------------------VDDRDtPLEETLEAFNELVK 139
|
170 180
....*....|....*....|....*
gi 19115800 158 TGKVRHIGLSNFNDTNLERILKVAK 182
Cdd:cd19752 140 AGKVRAIGASNFAAWRLERARQIAR 164
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
8-296 |
1.95e-10 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 61.16 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 8 FENAQnVHFTLADGSKIPGLGLGTWRS----EPNQTKNAV-KTALQYGYRHIDAAAIYG-----NEDEVGDGIKESGVPR 77
Cdd:PRK09912 10 YGQMQ-YRYCGKSGLRLPALSLGLWHNfghvNALESQRAIlRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 78 KDIWVTS-----KLWCNAHAPEAVPK----ALEKTLKDLKLDYLDEYLIHwpvsfktgedkfpkdkdgnLIYEKNPIEET 148
Cdd:PRK09912 89 RDELIIStkagyDMWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSH-------------------RVDENTPMEET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 149 WKAMEKLLETGKVRHIGLSNFNDTNLER---ILKVAKVKPAVHQME---LHPFLPQTEFVEKHKKLGIHVTAYSPFGNQ- 221
Cdd:PRK09912 150 ASALAHAVQSGKALYVGISSYSPERTQKmveLLREWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 222 ------NTIYE--------SKIPKLIEH----------ETIQKIAKSKGEgvTGATIAVSWAI--TRGTSVIPKSVNEQR 275
Cdd:PRK09912 230 ltgkylNGIPQdsrmhregNKVRGLTPKmlteanlnslRLLNEMAQQRGQ--SMAQMALSWLLkdERVTSVLIGASRAEQ 307
|
330 340
....*....|....*....|.
gi 19115800 276 IKSNFKYIPLTKEDMDEINSI 296
Cdd:PRK09912 308 LEENVQALNNLTFSTEELAQI 328
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
21-267 |
3.74e-10 |
|
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: 59.72 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWR--SEPNQTKNA---VKTALQYGYRHIDAAAIYG-----NEDEVGDGIKESGVP-RKDIWVTSK---- 85
Cdd:cd19151 9 GLKLPAISLGLWHnfGDVDRYENSramLRRAFDLGITHFDLANNYGpppgsAEENFGRILKEDLKPyRDELIISTKagyt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 86 LWCNAHAPEAVPK----ALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkDKDgnliyekNPIEETWKAMEKLLETGKV 161
Cdd:cd19151 89 MWPGPYGDWGSKKyliaSLDQSLKRMGLDYVDIFYHHRP------------DPE-------TPLEETMGALDQIVRQGKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 162 RHIGLSNFNDTNLE---RILKVAKVKPAVHQmelhpflPQTEFVEKH---------KKLGIHVTAYSP------------ 217
Cdd:cd19151 150 LYVGISNYPPEEAReaaAILKDLGTPCLIHQ-------PKYSMFNRWveeglldvlEEEGIGCIAFSPlaqglltdryln 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115800 218 -------------FGNQNTIYESKIPKLiehETIQKIAKSKGEgvTGATIAVSWAITRG--TSVI 267
Cdd:cd19151 223 gipedsraakgssFLKPEQITEEKLAKV---RRLNEIAQARGQ--KLAQMALAWVLRNKrvTSVL 282
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
21-296 |
4.89e-10 |
|
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: 59.67 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQTKNAV-----KTALQYGYRHIDAAAIYG---NEDEVGDGIKESGVPRKDIWVTSKLWCNAHA 92
Cdd:cd19159 10 GLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYAagkAEVILGSIIKKKGWRRSSLVITTKLYWGGKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 P-------EAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDGNliyekNPIEETWKAMEKLLETGKVRHIG 165
Cdd:cd19159 90 EterglsrKHIIEGLKGSLQRLQLEYVDVVFANRP--------------DSN-----TPMEEIVRAMTHVINQGMAMYWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 166 LSNFNDTNLERILKVAK----VKPAVHQMELHPFlpQTEFVEK-----HKKLGIHVTAYSPF--GNQNTIYESKIP---- 230
Cdd:cd19159 151 TSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF--QREKVEVqlpelYHKIGVGAMTWSPLacGIISGKYGNGVPessr 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 231 -----------KLIEHETIQKIAKSKG-------EGVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFKYI----PLT 286
Cdd:cd19159 229 aslkcyqwlkeRIVSEEGRKQQNKLKDlspiaerLGCTLPQLAVAWCLRNEgvSSVLLGSSTPEQLIENLGAIqvlpKMT 308
|
330
....*....|
gi 19115800 287 KEDMDEINSI 296
Cdd:cd19159 309 SHVVNEIDNI 318
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
21-169 |
5.47e-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: 59.47 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGT------WRSEPNQTK--NAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGVPRKDIWVTSKLwCN 89
Cdd:cd19153 9 LGNVSPVGLGTaalggvYGDGLEQDEavAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKV-GR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 90 AHAP------EAVPKALEKTLKDLKLDYLDEYLIHwPVSFKtgeDKFPKdkdgnliyeknpIEETWKAMEKLLETGKVRH 163
Cdd:cd19153 88 YRDSefdysaERVRASVATSLERLHTTYLDVVYLH-DIEFV---DYDTL------------VDEALPALRTLKDEGVIKR 151
|
....*.
gi 19115800 164 IGLSNF 169
Cdd:cd19153 152 IGIAGY 157
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
27-167 |
1.20e-09 |
|
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: 57.95 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGT------WRSEPN-QTKNAVKTALQYGYRHIDAAAIYGN-EDEVGDGIKEsgVPRKDIWVTSKLWCN--AHA---P 93
Cdd:cd19090 3 LGLGTaglggvFGGVDDdEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE--LPREPLVLSTKVGRLpeDTAdysA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115800 94 EAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfPKDKDGNLIYEKNPIEetwkAMEKLLETGKVRHIGLS 167
Cdd:cd19090 81 DRVRRSVEESLERLGRDRIDLLMIHDP----------ERVPWVDILAPGGALE----ALLELKEEGLIKHIGLG 140
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
42-167 |
1.59e-09 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 58.25 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 42 AVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGVPRKDIWVTSKlwCNAHA------PEAVPKALEKTLKDLKLDYL 112
Cdd:PLN02587 36 SVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTK--CGRYGegfdfsAERVTKSVDESLARLQLDYV 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19115800 113 DEYLIHwPVSFktgedkfpkdkdGNLiyeKNPIEETWKAMEKLLETGKVRHIGLS 167
Cdd:PLN02587 114 DILHCH-DIEF------------GSL---DQIVNETIPALQKLKESGKVRFIGIT 152
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
27-244 |
1.88e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 57.94 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 27 LGLGTWR-SEPNQTKNA---VKTALQYGYRHIDAAAIYG----------NEDEVGDGIKESGvPRKDIWVTSKLWCNAHA 92
Cdd:PRK10625 16 LGLGTMTfGEQNSEADAhaqLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVSGPSRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 PEA------------VPKALEKTLKDLKLDYLDEYLIHWPvsfktgedKFPKDKDGNLIY---EKNPIE---ETWKAMEK 154
Cdd:PRK10625 95 NDKgirpnqaldrknIREALHDSLKRLQTDYLDLYQVHWP--------QRPTNCFGKLGYswtDSAPAVsllETLDALAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 155 LLETGKVRHIGLSNFNDTNLERILKVAkvkpavhqmelhpflpqtefvEKHKKLGIhVTAYSPFGNQNTIYESKIPKLIE 234
Cdd:PRK10625 167 QQRAGKIRYIGVSNETAFGVMRYLHLA---------------------EKHDLPRI-VTIQNPYSLLNRSFEVGLAEVSQ 224
|
250
....*....|
gi 19115800 235 HETIQKIAKS 244
Cdd:PRK10625 225 YEGVELLAYS 234
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
42-181 |
5.46e-09 |
|
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: 56.13 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 42 AVKTALQYGYRHIDAAAIYGNEDEV-GDGIK--ESGVPRKDIWVTSK-----LWCNAHAPEAVPKALEKTLKDLKLDYLD 113
Cdd:cd19164 39 IVRRALELGIRAFDTSPYYGPSEIIlGRALKalRDEFPRDTYFIITKvgrygPDDFDYSPEWIRASVERSLRRLHTDYLD 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115800 114 EYLIHwPVSFKTGEDkfpkdkdgnliyeknpIEETWKAMEKLLETGKVRHIGLSNFndtNLERILKVA 181
Cdd:cd19164 119 LVYLH-DVEFVADEE----------------VLEALKELFKLKDEGKIRNVGISGY---PLPVLLRLA 166
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
21-281 |
6.32e-09 |
|
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: 56.31 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRS----EPNQTKNAV-KTALQYGYRHIDAAAIYG-----NEDEVGDGIKESGVPRKD-IWVTSK---- 85
Cdd:cd19150 9 GLKLPALSLGLWHNfgddTPLETQRAIlRTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAGYRDeLIISTKagyd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 86 LWCNAHAPEAVPK----ALEKTLKDLKLDYLDEYLIHwpvsfktgedKFPKDkdgnliyekNPIEETWKAMEKLLETGKV 161
Cdd:cd19150 89 MWPGPYGEWGSRKyllaSLDQSLKRMGLDYVDIFYSH----------RFDPD---------TPLEETMGALDHAVRSGKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 162 RHIGLSNFNDTNLER---ILKVAKVKPAVHQME---LHPFLPQTEFVEKHKKLGIHVTAYSPF---------------GN 220
Cdd:cd19150 150 LYVGISSYSPERTREaaaILRELGTPLLIHQPSynmLNRWVEESGLLDTLQELGVGCIAFTPLaqglltdkylngipeGS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115800 221 QNTIYESKIPKLIEHETIQKI----AKSKGEGVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFK 281
Cdd:cd19150 230 RASKERSLSPKMLTEANLNSIralnEIAQKRGQSLAQMALAWVLRDGrvTSALIGASRPEQLEENVG 296
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
42-184 |
6.34e-09 |
|
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: 56.02 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 42 AVKTALQYGYRHIDAAAIYGN---EDEVGDGIKesGVPRKDIWVTSK-----LWCNAH---APEAVPKALEKTLKDLKLD 110
Cdd:cd19163 38 TVHEALDSGINYIDTAPWYGQgrsETVLGKALK--GIPRDSYYLATKvgrygLDPDKMfdfSAERITKSVEESLKRLGLD 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115800 111 YLDEYLIHwPVSFKtgedkfpkdKDGNLIyeknpIEETWKAMEKLLETGKVRHIGLSNFNDTNLERILKVAKVK 184
Cdd:cd19163 116 YIDIIQVH-DIEFA---------PSLDQI-----LNETLPALQKLKEEGKVRFIGITGYPLDVLKEVLERSPVK 174
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
21-296 |
1.09e-08 |
|
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: 55.76 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQ-----TKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGVPRKDIWVTSKLWCNAHA 92
Cdd:cd19160 12 GLRVSCLGLGTWVTFGSQisdetAEDLLTVAYEHGVNLFDTAEVYAAgkaERTLGNILKSKGWRRSSYVVTTKIYWGGQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 P-------EAVPKALEKTLKDLKLDYLDEYlihwpvsfktgedkFPKDKDGNliyekNPIEETWKAMEKLLETGKVRHIG 165
Cdd:cd19160 92 EterglsrKHIIEGLRGSLDRLQLEYVDIV--------------FANRSDPN-----SPMEEIVRAMTYVINQGMAMYWG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 166 LSNFNDTNLERILKVAK----VKPAVHQMELHPFLP---QTEFVEKHKKLGIHVTAYSPF--GNQNTIYESKIP------ 230
Cdd:cd19160 153 TSRWSAMEIMEAYSVARqfnlIPPVCEQAEYHLFQRekvEMQLPELYHKIGVGSVTWSPLacGLITGKYDGRVPdtcraa 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 231 ---------KLIEHETIQKIAKSKG-------EGVTGATIAVSWAI-TRGTSVIPKSVN--EQRIKS--NFKYIP-LTKE 288
Cdd:cd19160 233 vkgyqwlkeKVQSEEGKKQQAKVKElhpiadrLGCTVAQLAIAWCLrSEGVSSVLLGVSsaEQLIENlgSIQVLSqLTPQ 312
|
....*...
gi 19115800 289 DMDEINSI 296
Cdd:cd19160 313 TVMEIDAL 320
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-296 |
9.47e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 52.60 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 24 IPGLGLGTWR-SEP----NQTKNAVKTALQY---GYRHIDAAAIYGN-EDEVGDGIKESG---------------VPRKD 79
Cdd:cd19101 2 ISRVINGMWQlSGGhggiRDEDAAVRAMAAYvdaGLTTFDCADIYGPaEELIGEFRKRLRrerdaaddvqihtkwVPDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 80 IWVTSKlwcnahapEAVPKALEKTLKDLKLDYLDEYLIHWpvsfktgEDkfpkdkdgnliYEKNPIEETWKAMEKLLETG 159
Cdd:cd19101 82 ELTMTR--------AYVEAAIDRSLKRLGVDRLDLVQFHW-------WD-----------YSDPGYLDAAKHLAELQEEG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 160 KVRHIGLSNFNDTNLERILKvAKVKPAVHQMEL-----HPFLPQTEFVEKHkklGIHVTAY----------------SPF 218
Cdd:cd19101 136 KIRHLGLTNFDTERLREILD-AGVPIVSNQVQYslldrRPENGMAALCEDH---GIKLLAYgtlaggllsekylgvpEPT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 219 GNQNTIYESKIPKLIEHE------------TIQKIAKSKgeGVTGATIAVSWAITR--GTSVIPKSVNEQRIKSN----- 279
Cdd:cd19101 212 GPALETRSLQKYKLMIDEwggwdlfqellrTLKAIADKH--GVSIANVAVRWVLDQpgVAGVIVGARNSEHIDDNvrafs 289
|
330
....*....|....*..
gi 19115800 280 FKyipLTKEDMDEINSI 296
Cdd:cd19101 290 FR---LDDEDRAAIDAV 303
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
21-296 |
1.57e-07 |
|
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: 52.01 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQ-----TKNAVKTALQYGYRHIDAAAIYGN---EDEVGDGIKESGVPRKDIWVTSKLWCNAHA 92
Cdd:cd19158 10 GLRVSCLGLGTWVTFGGQitdemAEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIFWGGKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 P-------EAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDGNliyekNPIEETWKAMEKLLETGKVRHIG 165
Cdd:cd19158 90 EterglsrKHIIEGLKASLERLQLEYVDVVFANRP--------------DPN-----TPMEETVRAMTHVINQGMAMYWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 166 LSNFNDTNLERILKVAK----VKPAVHQMELHPFlpQTEFVEKH-----KKLGIHVTAYSPF--GNQNTIYESKIP---- 230
Cdd:cd19158 151 TSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMF--QREKVEVQlpelfHKIGVGAMTWSPLacGIVSGKYDSGIPpysr 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 231 -----------KLIEHETIQKIAKSKG-------EGVTGATIAVSWAITRG--TSVIPKSVNEQRIKSNFKYI----PLT 286
Cdd:cd19158 229 aslkgyqwlkdKILSEEGRRQQAKLKElqaiaerLGCTLPQLAIAWCLRNEgvSSVLLGASNAEQLMENIGAIqvlpKLS 308
|
330
....*....|
gi 19115800 287 KEDMDEINSI 296
Cdd:cd19158 309 SSIVHEIDSI 318
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
21-230 |
2.57e-07 |
|
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: 51.29 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 21 GSKIPGLGLGTWRSEPNQ-----TKNAVKTALQYGYRHIDAAAIY-GNEDEV--GDGIKESGVPRKDIWVTSKLWCNAHA 92
Cdd:cd19141 9 GLRVSCLGLGTWVTFGSQisdevAEELVTLAYENGINLFDTAEVYaAGKAEIvlGKILKKKGWRRSSYVITTKIFWGGKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 93 P-------EAVPKALEKTLKDLKLDYLDEYLIHWPvsfktgedkfpkdkDGNliyekNPIEETWKAMEKLLETGKVRHIG 165
Cdd:cd19141 89 EterglsrKHIIEGLKASLERLQLEYVDIVFANRP--------------DPN-----TPMEEIVRAFTHVINQGMAMYWG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115800 166 LSNFNDTNLERILKVAK----VKPAVHQMELHPFlpQTEFVEKHK-----KLGIHVTAYSP--FGNQNTIYESKIP 230
Cdd:cd19141 150 TSRWSAMEIMEAYSVARqfnlIPPIVEQAEYHLF--QREKVEMQLpelfhKIGVGAMTWSPlaCGILSGKYDDGVP 223
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
25-167 |
1.88e-05 |
|
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: 45.43 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 25 PGLGLGT------WRSEPNQTKNAVKTALQYGYRHIDAAAIYG---NEDEVGDGIKesGVPRKDIWVTSKLWCNAHAPEA 95
Cdd:cd19162 1 PRLGLGAaslgnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA--RHPRAEYVVSTKVGRLLEPGAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 96 VPKA----------------LEKTLKDLKLDYLDEYLIHwpvsfktgedkfpkDKDGnliYEKNPIEETWKAMEKLLETG 159
Cdd:cd19162 79 GRPAgadrrfdfsadgirrsIEASLERLGLDRLDLVFLH--------------DPDR---HLLQALTDAFPALEELRAEG 141
|
....*...
gi 19115800 160 KVRHIGLS 167
Cdd:cd19162 142 VVGAIGVG 149
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
46-168 |
7.99e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 43.42 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 46 ALQYGYRHIDAAAIYG----NEDevgdgIKESGVP-RKDIWVTSKL---------WCNAHAPEAVPKALEKTLKDLKLDY 111
Cdd:PRK10376 49 AVALGVNHIDTSDFYGphvtNQL-----IREALHPyPDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLRNLGLDV 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115800 112 LDeylihwPVSFKTGEDKF-PKDkdgnliyekNPIEETWKAMEKLLETGKVRHIGLSN 168
Cdd:PRK10376 124 LD------VVNLRLMGDGHgPAE---------GSIEEPLTVLAELQRQGLVRHIGLSN 166
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
25-166 |
4.05e-03 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 38.46 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 25 PGLGLGT------WRSEPNQTKNAV-KTALQYGYRHIDAAAIYGN---EDEVGDGIKEsgVPRKDIWVTSK---LWCNAH 91
Cdd:cd19161 1 SELGLGTaglgnlYTAVSNADADATlDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKvgrLLKPAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115800 92 APEAVP----------------------KALEKTLKDLKLDYLDEYLIHwPVSFKTGEDKFPKDKDGNLiyeknpIEETW 149
Cdd:cd19161 79 EGSVPDpngfvdplpfeivydysydgimRSFEDSLQRLGLNRIDILYVH-DIGVYTHGDRKERHHFAQL------MSGGF 151
|
170
....*....|....*..
gi 19115800 150 KAMEKLLETGKVRHIGL 166
Cdd:cd19161 152 KALEELKKAGVIKAFGL 168
|
|
| |
