|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-313 |
0e+00 |
|
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: 609.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKGIRREDVFVTSKLWNTKHH 88
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 89 PDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSR 168
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 169 QIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAWKHPDEPVLLEEPAIAALAKKYNKTPAQ 248
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSPAQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528482668 249 IIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIVPTITVDGKSVPR 313
Cdd:cd19106 241 ILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVPMITVDGKRVPR 305
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
9-300 |
1.14e-132 |
|
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: 379.45 E-value: 1.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKgIRREDVFVTSKLWNTKHH 88
Cdd:cd19123 6 LSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGK-VKREDLWITSKLWNNSHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 89 PDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGdTPFPRKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSR 168
Cdd:cd19123 85 PEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSVK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 169 QIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDR--AWKHPDEPVLLEEPAIAALAKKYNKTP 246
Cdd:cd19123 164 KLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRpaAMKAEGEPVLLEDPVINKIAEKHGASP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 528482668 247 AQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYI 300
Cdd:cd19123 244 AQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
12-326 |
1.29e-131 |
|
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: 377.14 E-value: 1.29e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMgPDKGIRREDVFVTSKLWNTKHHPDD 91
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKI-KEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 92 VEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSRQID 171
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 172 DILSVASIK--PTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAWKHPDEPVLLEEPAIAALAKKYNKTPAQI 249
Cdd:cd19107 160 RILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528482668 250 IIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIvptitvdgkSVPRDAGHPHYPFNDSY 326
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRAC---------ALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
9-300 |
5.67e-127 |
|
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: 364.68 E-value: 5.67e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKS-EPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGpDKGIRREDVFVTSKLWNTKH 87
Cdd:cd19116 5 LNDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIA-EGVVKREDLFITTKLWNSYH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 HPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPfprKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNS 167
Cdd:cd19116 84 EREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDS---ESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 168 RQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAwKHPDEPVLLEEPAIAALAKKYNKTPA 247
Cdd:cd19116 161 EQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPR-GQTNPPPRLDDPTLVAIAKKYGKTTA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528482668 248 QIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYI 300
Cdd:cd19116 240 QIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-287 |
9.50e-126 |
|
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: 359.87 E-value: 9.50e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 15 MPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQEtmgpdKGIRREDVFVTSKLWNTKHHPDDVEP 94
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRE-----SGVPREELFITTKLWPTDHGYERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 95 SLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEdgtllyddidyklTWAAMEKLVGKGLVRAIGLSNFNSRQIDDIL 174
Cdd:cd19071 76 ALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEARLE-------------TWRALEELVDEGLVRSIGVSNFNVEHLEELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 175 SVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRawkhpdepVLLEEPAIAALAKKYNKTPAQIIIRWQ 254
Cdd:cd19071 143 AAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR--------PLLDDPVLKEIAKKYGKTPAQVLLRWA 214
|
250 260 270
....*....|....*....|....*....|...
gi 528482668 255 TQRGVVTIPKSITQSRIKENIQVFDFTLESEEM 287
Cdd:cd19071 215 LQRGVVVIPKSSNPERIKENLDVFDFELSEEDM 247
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-302 |
4.60e-122 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 350.89 E-value: 4.60e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKHHPDD 91
Cdd:COG0656 2 GVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS-----GVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 92 VEPSLLKTLKDLKLEYLDLYLIHWPYafqrgdtpfprkedgtllydDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSRQID 171
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPG--------------------PGPYVETWRALEELYEEGLIRAIGVSNFDPEHLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 172 DILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDrawkhpdepvLLEEPAIAALAKKYNKTPAQIII 251
Cdd:COG0656 137 ELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQVVL 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 528482668 252 RWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIVP 302
Cdd:COG0656 207 RWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLGPD 257
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
5-290 |
6.69e-119 |
|
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: 343.94 E-value: 6.69e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 5 DFAVLSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGpDKGIRREDVFVTSKLWN 84
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFE-DGVVKREDLFITSKLWC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 85 TKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEdgtllYDDIDYKLTWAAMEKLVGKGLVRAIGLSN 164
Cdd:cd19125 80 TDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEE-----VLPPDIPSTWKAMEKLVDSGKVRAIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 165 FNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAWKHPDepvLLEEPAIAALAKKYNK 244
Cdd:cd19125 155 FSVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKLGK 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 528482668 245 TPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQV 290
Cdd:cd19125 232 TPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKF 277
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-298 |
4.01e-118 |
|
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: 342.47 E-value: 4.01e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKGiRREDVFVTSKLWNTKHH 88
Cdd:cd19154 6 LSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVV-KREDLFITTKLWTHEHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 89 PDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSR 168
Cdd:cd19154 85 PEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 169 QIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAWKHPD-----EPVLLEEPAIAALAKKYN 243
Cdd:cd19154 165 QIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKStgvspAPNLLQDPIVKAIAEKHG 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 528482668 244 KTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWR 298
Cdd:cd19154 245 KTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
9-300 |
7.60e-114 |
|
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: 331.89 E-value: 7.60e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSE---PGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGpDKGIRREDVFVTSKLWNT 85
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPEevpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIA-DGTVKREDIFYTSKLWCT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 86 KHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNF 165
Cdd:cd19108 84 FHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGVSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 166 NSRQIDDILSVASIK--PTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSP-DRAWKHPDEPVLLEEPAIAALAKKY 242
Cdd:cd19108 164 NRRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALAKKH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 243 NKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYI 300
Cdd:cd19108 244 KRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
9-293 |
2.15e-108 |
|
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: 317.05 E-value: 2.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKGIRREDVFVTSKLWNTKHH 88
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 89 PDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTP---FPRKEDGTLLYDDIDYKL--TWAAMEKLVGKGLVRAIGLS 163
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLnplTAVPTNGGEVDLDLSVSLvdTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 164 NFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSpDRAwkhpDEPVLLEEPAIAALAKKYN 243
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-NLA----GLPLLVQHPEVKAIAAKLG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 528482668 244 KTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQvfDFTLESEEMSQVTAL 293
Cdd:cd19118 236 KTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
12-322 |
1.09e-107 |
|
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: 316.36 E-value: 1.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTW----KSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKgIRREDVFVTSKLWNTKH 87
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGK-VKREDIFYCGKLWNTCH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 HPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNS 167
Cdd:cd19109 80 PPELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 168 RQIDDILSVASIK--PTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSP-DRAWKHPDEPVLLEEPAIAALAKKYNK 244
Cdd:cd19109 160 RQLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 245 TPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIVPTITVDgksvprdagHPHYPF 322
Cdd:cd19109 240 TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRD---------HPEYPF 308
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-301 |
2.09e-101 |
|
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: 299.41 E-value: 2.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKgIRREDVFVTSKLWNTKHHPDD 91
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGK-LKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 92 VEPSLLKTLKDLKLEYLDLYLIHWPYAFQRgdtpfprKEDGTLLyDDIDYKL--TWAAMEKLVGKGLVRAIGLSNFNSRQ 169
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVN-------KKDKGER-ELASSDVtsVWRAMEALVSEGKVKSIGLSNFNPRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 170 IDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRA--WKHPDEPVLLEEPAIAALAKKYNKTPA 247
Cdd:cd19111 152 INKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 528482668 248 QIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIV 301
Cdd:cd19111 232 QVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFD 285
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
14-326 |
6.28e-98 |
|
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: 291.09 E-value: 6.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 14 KMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMgpDKG-IRREDVFVTSKLWNTKHHPDDV 92
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKI--KEGvVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 93 EPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSRQIDD 172
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 173 ILSVAS--IKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAWKhpdepvLLEEPAIAALAKKYNKTPAQII 250
Cdd:cd19110 161 LLNKPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVD------LIDDPVIQRIAKKHGKSPAQIL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528482668 251 IRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYivptitvdgKSVPRDAGHPHYPFNDSY 326
Cdd:cd19110 235 IRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRL---------ATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
6-299 |
1.27e-97 |
|
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: 289.29 E-value: 1.27e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 6 FAVLSTGRKMPLLGLGTWKSEPG-LVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWN 84
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGsEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKES-----GIPREELFITSKVWN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 85 TKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgdtpfprKEDgtllyddiDYKLTWAAMEKLVGKGLVRAIGLSN 164
Cdd:cd19157 76 ADQGYDSTLKAFEASLERLGLDYLDLYLIHWP------------VKG--------KYKETWKALEKLYKDGRVRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 165 FNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDrawkhpdepvLLEEPAIAALAKKYNK 244
Cdd:cd19157 136 FQVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEKYNK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 528482668 245 TPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRY 299
Cdd:cd19157 206 SVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-298 |
8.38e-97 |
|
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: 288.66 E-value: 8.38e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 5 DFAVLSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKgIRREDVFVTSKLWN 84
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGK-VKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 85 TKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQ-RGDTPFPRKEDGTLLYD-DIDYKLTWAAMEKLVGKGLVRAIGL 162
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 163 SNFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAWKHP-------DEPVLLEEPAI 235
Cdd:cd19155 161 SNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528482668 236 AALAKKYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWR 298
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
12-290 |
5.58e-96 |
|
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: 285.89 E-value: 5.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKgIRREDVFVTSKLWNTKHHPDD 91
Cdd:cd19129 3 SGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGK-IRREDLFVTTKLWNTNHRPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 92 VEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLLYDD-IDYKLTWAAMEKLVGKGLVRAIGLSNFNSRQI 170
Cdd:cd19129 82 VKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 171 DDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGspdrawkHPDEPVLLEEPAIAALAKKYNKTPAQII 250
Cdd:cd19129 162 REIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG-------HGMEPKLLEDPVITAIARRVNKTPAQVL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 528482668 251 IRWQTQRGVVTIPKSITQSRIKENiqvFDF-TLESEEMSQV 290
Cdd:cd19129 235 LAWAIQRGTALLTTSKTPSRIREN---FDIsTLPEDAMREI 272
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
15-293 |
5.15e-95 |
|
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: 282.21 E-value: 5.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 15 MPLLGLGTWK---SEpgLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQEtMGPDKGIRREDVFVTSKLWNTKHHPDD 91
Cdd:cd19136 1 MPILGLGTFRlrgEE--EVRQAVDAALKAGYRLIDTASVYRNEADIGKALRD-LLPKYGLSREDIFITSKLAPKDQGYEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 92 VEPSLLKTLKDLKLEYLDLYLIHWPYAfqrgdtpfprkeDGTLLYDDIDYKL---TWAAMEKLVGKGLVRAIGLSNFNSR 168
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHWPGV------------QGLKPSDPRNAELrreSWRALEDLYKEGKLRAIGVSNYTVR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 169 QIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDrawkhpdePVLLEEPAIAALAKKYNKTPAQ 248
Cdd:cd19136 146 HLEELLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD--------LRLLEDPTVLAIAKKYGRTPAQ 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 528482668 249 IIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19136 218 VLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
3-294 |
2.39e-93 |
|
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: 278.05 E-value: 2.39e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 3 MNDFAVLSTGRKMPLLGLGTWKSEpGLVKQAVIWAL-ESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSK 81
Cdd:cd19135 1 GTPTVRLSNGVEMPILGLGTSHSG-GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKES-----GVPREDLFLTTK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 82 LWNTKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgDTPFPRKEDGTLLYDdidyklTWAAMEKLVGKGLVRAIG 161
Cdd:cd19135 75 LWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWP------DCPSSGKNVKETRAE------TWRALEELYDEGLCRAIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 162 LSNFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSpdraWKhpdepvLLEEPAIAALAKK 241
Cdd:cd19135 143 VSNFLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAK----GK------ALEEPTVTELAKK 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528482668 242 YNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALH 294
Cdd:cd19135 213 YQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSLH 265
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-295 |
1.87e-91 |
|
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: 273.99 E-value: 1.87e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQetmgpDKGIRREDVFVTSKLWNTKHH 88
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK-----DSGVPREEIFITTKLWCTWHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 89 pdDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLL--YDDIDYKLTWAAMEKLVGKGLVRAIGLSNFN 166
Cdd:cd19117 83 --RVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKdhEPDWDFIKTWELMQKLPATGKVKAIGVSNFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 167 SRQIDDILSVASIK--PTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAwkhpdepvLLEEPAIAALAKKYNK 244
Cdd:cd19117 161 IKNLEKLLASPSAKivPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 528482668 245 TPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVfdFTLESEEMSQVTALHR 295
Cdd:cd19117 233 TPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-302 |
2.28e-91 |
|
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: 274.75 E-value: 2.28e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMgpDKG-IRREDVFVTSKLWNTKH 87
Cdd:cd19112 5 LNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAF--KTGlVKREDLFITTKLWNSDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 hpDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQR---GDTPFPRKEDGTLLYD-DIDYKLTWAAMEKLVGKGLVRAIGLS 163
Cdd:cd19112 83 --GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLDIDvTISLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 164 NFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLG--SPDRAWKHPDEPvlLEEPAIAALAKK 241
Cdd:cd19112 161 NYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWFGSVSP--LDDPVLKDLAKK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528482668 242 YNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIVP 302
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQP 299
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
9-293 |
5.68e-91 |
|
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: 271.62 E-value: 5.68e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPG-LVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKH 87
Cdd:cd19126 3 LNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRES-----GVPREELFVTTKLWNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 HPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAfqrgdtpfprkeDGtllyddidYKLTWAAMEKLVGKGLVRAIGLSNFNS 167
Cdd:cd19126 78 RARRTEDAFQESLDRLGLDYVDLYLIHWPGK------------DK--------FIDTWKALEKLYASGKVKAIGVSNFQE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 168 RQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGspdrawkhpdEPVLLEEPAIAALAKKYNKTPA 247
Cdd:cd19126 138 HHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLG----------QGGLLSNPVLAAIGEKYGKSAA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 528482668 248 QIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19126 208 QVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
9-303 |
1.82e-90 |
|
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: 272.76 E-value: 1.82e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMgpDKGI-RREDVFVTSKLWNTKH 87
Cdd:cd19115 7 LNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAI--KEGIvKREDLFIVSKLWNTFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 HPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGD--TPFP---RKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGL 162
Cdd:cd19115 85 DGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDpaVRYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLARSIGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 163 SNFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLG-------SPDRAwkhPDEPVLLEEPAI 235
Cdd:cd19115 165 SNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsflelDLPGA---KDTPPLFEHDVI 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 236 AALAKKYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIVPT 303
Cdd:cd19115 242 KSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFNNPL 309
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-293 |
2.30e-90 |
|
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: 271.06 E-value: 2.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTWKS--EPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMgpDKG--IRREDVFVTSKLWNTK 86
Cdd:cd19124 1 SGQTMPVIGMGTASDppSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEAL--RLGlvKSRDELFVTSKLWCSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 87 HHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLlydDIDYKLTWAAMEKLVGKGLVRAIGLSNFN 166
Cdd:cd19124 79 AHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFL---PFDIKGVWEAMEECQRLGLTKAIGVSNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 167 SRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAWkhpDEPVLLEEPAIAALAKKYNKTP 246
Cdd:cd19124 156 CKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKW---GSNAVMESDVLKEIAAAKGKTV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 528482668 247 AQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19124 233 AQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-290 |
5.65e-90 |
|
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: 268.76 E-value: 5.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 15 MPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKHHPDDVEP 94
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES-----GVPREDLFITTKVWRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 95 SLLKTLKDLKLEYLDLYLIHWPyafqRGDTPFPRkedgtllyddidyklTWAAMEKLVGKGLVRAIGLSNFNSRQIDDIL 174
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLIHWP----NPTVPLEE---------------TLGALKELKEAGKVKSIGVSNFTIELLEEAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 175 SVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDrawkhpdepvLLEEPAIAALAKKYNKTPAQIIIRWQ 254
Cdd:cd19073 137 DISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE----------VLRDPVIQEIAEKYDKTPAQVALRWL 206
|
250 260 270
....*....|....*....|....*....|....*.
gi 528482668 255 TQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQV 290
Cdd:cd19073 207 VQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
9-293 |
9.35e-89 |
|
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: 265.98 E-value: 9.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWK-SEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLW---- 83
Cdd:cd19133 3 LNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKS-----GIPREELFITTKLWiqda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 84 NTKHHPDDVEPSLLKTLKdlklEYLDLYLIHWPYAfqrgdtpfprkedgtllyddiDYKLTWAAMEKLVGKGLVRAIGLS 163
Cdd:cd19133 78 GYEKAKKAFERSLKRLGL----DYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 164 NFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAwkhpdepvLLEEPAIAALAKKYN 243
Cdd:cd19133 133 NFYPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN--------LFENPVLTEIAEKYG 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 528482668 244 KTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19133 205 KSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
3-287 |
7.62e-87 |
|
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: 262.08 E-value: 7.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 3 MNDFAvLSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMgpDKGIRREDVFVTSKL 82
Cdd:cd19121 1 MTSFK-LNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI--AGGVKREDLFVTTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 83 WNTKHhpDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQ-RGDTP-FPRKEDGTLLYD-DIDYKLTWAAMEKLVGKGLVRA 159
Cdd:cd19121 78 WSTYH--RRVELCLDRSLKSLGLDYVDLYLVHWPVLLNpNGNHDlFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 160 IGLSNFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAwkhpdepvLLEEPAIAALA 239
Cdd:cd19121 156 IGVSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEIA 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 528482668 240 KKYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTleSEEM 287
Cdd:cd19121 228 KKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDM 273
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
9-299 |
1.94e-86 |
|
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: 260.53 E-value: 1.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQ-AVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKH 87
Cdd:cd19156 3 LANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES-----GVPREEVFVTTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 HPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQrgdtpfprkedgtllyddidYKLTWAAMEKLVGKGLVRAIGLSNFNS 167
Cdd:cd19156 78 GYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK--------------------FKDTWKAFEKLYKEKKVRAIGVSNFHE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 168 RQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDrawkhpdepvLLEEPAIAALAKKYNKTPA 247
Cdd:cd19156 138 HHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKYGKSAA 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 528482668 248 QIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRY 299
Cdd:cd19156 208 QVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
9-293 |
1.06e-85 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 258.46 E-value: 1.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQetmgpDKGIRREDVFVTSKLWNTKHH 88
Cdd:cd19131 4 LNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR-----ASGVPREELFITTKLWNSDQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 89 PDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgdtpFPRKEDgtllyddidYKLTWAAMEKLVGKGLVRAIGLSNFNSR 168
Cdd:cd19131 79 YDSTLRAFDESLRKLGLDYVDLYLIHWP---------VPAQDK---------YVETWKALIELKKEGRVKSIGVSNFTIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 169 QIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDrawkhpdepvLLEEPAIAALAKKYNKTPAQ 248
Cdd:cd19131 141 HLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG----------LLSDPVIGEIAEKHGKTPAQ 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 528482668 249 IIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19131 211 VVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-299 |
2.74e-85 |
|
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: 259.30 E-value: 2.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMgpDKGI-RREDVFVTSKLWNTKH 87
Cdd:cd19113 5 LNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAI--DEGLvKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 HPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRgdTPFPRK--------EDGTLLYDDIDYKLTWAAMEKLVGKGLVRA 159
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKF--VPIEEKyppgfycgDGDNFVYEDVPILDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 160 IGLSNFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGsPDR--AWKHP---DEPVLLEEPA 234
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFG-PQSfvELNQGralNTPTLFEHDT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528482668 235 IAALAKKYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRY 299
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-287 |
1.88e-84 |
|
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: 255.91 E-value: 1.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 16 PLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGpDKGIRREDVFVTSKLWNTKHHPDDVEPS 95
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFK-DGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 96 LLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILS 175
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 176 VASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRawkhPDEPVLLEEPAIAALAKKYNKTPAQIIIRWQT 255
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYG----DGNLTFLNDSELKALATKYNTTPPQVIIAWHL 236
|
250 260 270
....*....|....*....|....*....|....*
gi 528482668 256 QRGVVT---IPKSITQSRIKENIQVFDFTLESEEM 287
Cdd:cd19128 237 QKWPKNysvIPKSANKSRCQQNFDINDLALTKEDM 271
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-293 |
1.73e-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: 253.10 E-value: 1.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 8 VLSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKH 87
Cdd:cd19127 2 TLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS-----GVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 HPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgdTPfprkedgTLLYDDIDyklTWAAMEKLVGKGLVRAIGLSNFNS 167
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWP-------VP-------NDFDRTIQ---AYKALEKLLAEGRVRAIGVSNFTP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 168 RQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAWK-HPDEPV-LLEEPAIAALAKKYNKT 245
Cdd:cd19127 140 EHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGAsGPTGPGdVLQDPTITGLAEKYGKT 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 528482668 246 PAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19127 220 PAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
12-293 |
5.35e-83 |
|
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: 251.41 E-value: 5.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKHHPDD 91
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAAS-----GVPRDELFLTTKVWPDNYSPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 92 VEPSLLKTLKDLKLEYLDLYLIHWPYAfqrgDTPFPRkedgtllyddidyklTWAAMEKLVGKGLVRAIGLSNFNSRQID 171
Cdd:cd19140 80 FLASVEESLRKLRTDYVDLLLLHWPNK----DVPLAE---------------TLGALNEAQEAGLARHIGVSNFTVALLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 172 DILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDrawkhpdepvLLEEPAIAALAKKYNKTPAQIII 251
Cdd:cd19140 141 EAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE----------VLKDPVLQEIGRKHGKTPAQVAL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 528482668 252 RWQTQR-GVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19140 211 RWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-292 |
2.68e-78 |
|
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: 239.83 E-value: 2.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGT----WKSEPGLVKQ----AVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPdkgirREDVFVTSKLW 83
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRdlvdSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVP-----REDLFITTKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 84 ntkHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRkedgtllyddidyklTWAAMEKLVGKGLVRAIGLS 163
Cdd:cd19120 76 ---PGIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGPTLAE---------------AWAELEALKDAGLVRSIGVS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 164 NFNSRQIDDILSVASIKPTVLQVESHPYLA--QVELLSHCRDRGLVMTAYSPLgSPdrAWKHPDEPVlleEPAIAALAKK 241
Cdd:cd19120 138 NFRIEDLEELLDTAKIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPL-SP--LTRDAGGPL---DPVLEKIAEK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 528482668 242 YNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTA 292
Cdd:cd19120 212 YGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-298 |
7.25e-76 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 234.20 E-value: 7.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 1 MSMNDFAVLSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTS 80
Cdd:PRK11565 1 MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA-----SVAREELFITT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 81 KLWNTKHHpdDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQrgDTpfprkedgtllyddidYKLTWAAMEKLVGKGLVRAI 160
Cdd:PRK11565 76 KLWNDDHK--RPREALEESLKKLQLDYVDLYLMHWPVPAI--DH----------------YVEAWKGMIELQKEGLIKSI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 161 GLSNFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAwkhpdepvLLEEPAIAALAK 240
Cdd:PRK11565 136 GVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG--------VFDQKVIRDLAD 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 241 KYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWR 298
Cdd:PRK11565 208 KYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
9-295 |
1.05e-75 |
|
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: 232.93 E-value: 1.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKHH 88
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRS-----GVPREELFVTTKLPGRHHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 89 PDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgdtpFPRKEdgtlLYDDidyklTWAAMEKLVGKGLVRAIGLSNFNSR 168
Cdd:cd19132 76 YEEALRTIEESLYRLGLDYVDLYLIHWP---------NPSRD----LYVE-----AWQALIEAREEGLVRSIGVSNFLPE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 169 QIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRawkhpdepvLLEEPAIAALAKKYNKTPAQ 248
Cdd:cd19132 138 HLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 528482668 249 IIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHR 295
Cdd:cd19132 209 VVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-304 |
1.44e-74 |
|
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: 231.68 E-value: 1.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMgpDKGI-RREDVFVTSKLWNTKHHPD 90
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAI--QEGLvKREDLFIVTKLWNNFHGKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 91 DVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGD--TPFP----RKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSN 164
Cdd:cd19114 79 HVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaENYPflwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 165 FNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSP--DRAWKHPDEPV-LLEEPAIAALAKK 241
Cdd:cd19114 159 FNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvyTKVTKHLKHFTnLLEHPVVKKLADK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528482668 242 YNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIVPTI 304
Cdd:cd19114 239 HKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPVV 301
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-283 |
4.35e-69 |
|
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: 217.36 E-value: 4.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTW--KSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMgpDKG-IRREDVFVTSKLWNT 85
Cdd:cd19119 6 LNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAI--DDGsIKREELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 86 KHhpDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTP-----FPRKEDGTLLYD-DIDYKLTWAAMEKLVGKGLVRA 159
Cdd:cd19119 84 FY--DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDsgkpfTPVNDDGKTRYAaSGDHITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 160 IGLSNFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPdrawKHPdepvLLEEPAIAALA 239
Cdd:cd19119 162 IGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSH----GAP----NLKNPLVKKIA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 528482668 240 KKYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLE 283
Cdd:cd19119 234 EKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKE 277
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-293 |
6.89e-69 |
|
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: 215.54 E-value: 6.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 8 VLSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKH 87
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAAS-----GIPRDELFVTTKLWNDRH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 HPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgdtpFPRKEDgtllyddidYKLTWAAMEKLVGKGLVRAIGLSNFNS 167
Cdd:cd19130 78 DGDEPAAAFAESLAKLGLDQVDLYLVHWP---------TPAAGN---------YVHTWEAMIELRAAGRTRSIGVSNFLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 168 RQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGspdrawkhpdEPVLLEEPAIAALAKKYNKTPA 247
Cdd:cd19130 140 PHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLG----------QGKLLGDPPVGAIAAAHGKTPA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 528482668 248 QIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19130 210 QIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-299 |
4.71e-68 |
|
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: 213.56 E-value: 4.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 8 VLSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKH 87
Cdd:cd19134 4 TLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS-----GIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 HPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQrgdtpfprkedGTllyddidYKLTWAAMEKLVGKGLVRAIGLSNFNS 167
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWPAGRE-----------GK-------YVDSWGGLMKLREEGLARSIGVSNFTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 168 RQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDrawkhpdepvLLEEPAIAALAKKYNKTPA 247
Cdd:cd19134 141 EHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR----------LLDNPAVTAIAAAHGRTPA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 528482668 248 QIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRY 299
Cdd:cd19134 211 QVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-292 |
3.49e-67 |
|
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: 212.48 E-value: 3.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSE--PGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKGIRREDVFVTSKLWNTK 86
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENPSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 87 HHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPR-KEDGT-LLYDDI--DYKLTWAAMEKLVGKGLVRAIGL 162
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKyVILKDLteNPEPTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 163 SNFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGS----PDRAWKHPDEPVLLEepaiaaL 238
Cdd:cd19122 163 SNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqnqvPSTGERVSENPTLNE------V 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 528482668 239 AKKYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTA 292
Cdd:cd19122 237 AEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSDEDFEAINQVA 290
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
15-293 |
1.27e-61 |
|
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: 196.42 E-value: 1.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 15 MPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKHHPDDVEP 94
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAES-----GVPRDELFITTKIWIDNLSKDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 95 SLLKTLKDLKLEYLDLYLIHWPyafqrgdTPfprkedgtllYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSRQIDDIL 174
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHWP-------SP----------NDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 175 SVASIKPTVL-QVESHPYLAQVELLSHCRDRGLVMTAYSPLGspdrawkhpdEPVLLEEPAIAALAKKYNKTPAQIIIRW 253
Cdd:cd19139 139 AVVGAGAIATnQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA----------YGKVLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 528482668 254 QTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-289 |
4.14e-56 |
|
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: 182.81 E-value: 4.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTWK---------SEPGLVKQAVIWALESGYRHIDCAPIYAN---EPEIGEAFqetmgpdKGIRREDVFVT 79
Cdd:cd19072 1 GEEVPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI-------KGFDREDLFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 80 SKLWNTKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgdtpfprkedgtllYDDIDYKLTWAAMEKLVGKGLVRA 159
Cdd:cd19072 74 TKVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP-------------------NPSIPIEETLRAMEELVEEGKIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 160 IGLSNFNSRQIDDILSVAS-IKPTVLQVESHPYL--AQVELLSHCRDRGLVMTAYSPLGSPDRAWKHPDEpvLLEEpaia 236
Cdd:cd19072 135 IGVSNFSLEELEEAQSYLKkGPIVANQVEYNLFDreEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSP--LLDE---- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 528482668 237 aLAKKYNKTPAQIIIRWQTQR-GVVTIPKSITQSRIKENIQVFDFTLESEEMSQ 289
Cdd:cd19072 209 -IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQR 261
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
14-302 |
3.19e-54 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 178.29 E-value: 3.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 14 KMPLLGLGTWKsepgLVKQAVI----WALESGYRHIDCAPIYANEPEIGEAFQETmgpdkGIRREDVFVTSKLWNTKHHP 89
Cdd:PRK11172 2 SIPAFGLGTFR----LKDQVVIdsvkTALELGYRAIDTAQIYDNEAAVGQAIAES-----GVPRDELFITTKIWIDNLAK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 90 DDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgdTPfprkedgtllYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFN--- 166
Cdd:PRK11172 73 DKLIPSLKESLQKLRTDYVDLTLIHWP-------SP----------NDEVSVEEFMQALLEAKKQGLTREIGISNFTial 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 167 SRQIDDILSVASIKPTvlQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDrawkhpdepvLLEEPAIAALAKKYNKTP 246
Cdd:PRK11172 136 MKQAIAAVGAENIATN--QIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK----------VLKDPVIARIAAKHNATP 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 528482668 247 AQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIVP 302
Cdd:PRK11172 204 AQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSP 259
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
18-293 |
2.13e-52 |
|
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: 174.04 E-value: 2.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTW-------KSEPGLVKQAVIWALESGYRHIDCAPIY---ANEPEIGEAFQETMGPdkgirREDVFVTSKL----- 82
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVK-----RDKVVIATKVpdgdg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 83 -WNTKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgDTPFPRKEdgtllyddidyklTWAAMEKLVGKGLVRAIG 161
Cdd:pfam00248 76 pWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP------DPDTPIEE-------------TWDALEELKKEGKIRAIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 162 LSNFNSRQIDDILSVASIKPTVLQVESHPY--LAQVELLSHCRDRGLVMTAYSPLGS-----------------PDRAWK 222
Cdd:pfam00248 137 VSNFDAEQIEKALTKGKIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgeRRRLLK 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528482668 223 HPDEPVLLEEPAIAALAKKYNKTPAQIIIRW--QTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTAL 293
Cdd:pfam00248 217 KGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-289 |
4.61e-46 |
|
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: 157.03 E-value: 4.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 9 LSTGRKMPLLGLGTWKSEPGLVK-----QAVIWALESGYRHIDCAPIYAN---EPEIGEAFQEtmgpdkgiRREDVFVTS 80
Cdd:cd19138 5 LPDGTKVPALGQGTWYMGEDPAKraqeiEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG--------RRDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 81 KLWNTKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWpyafqRGDTPFprkedgtllyddidyKLTWAAMEKLVGKGLVRAI 160
Cdd:cd19138 77 KVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHW-----RGGVPL---------------AETVAAMEELKKEGKIRAW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 161 GLSNFNSRQIDDILSVASIKP-TVLQVESHpyLAQ----VELLSHCRDRGLVMTAYSPLGSPDRAWKHpdepvLLEEPAI 235
Cdd:cd19138 137 GVSNFDTDDMEELWAVPGGGNcAANQVLYN--LGSrgieYDLLPWCREHGVPVMAYSPLAQGGLLRRG-----LLENPTL 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 528482668 236 AALAKKYNKTPAQIIIRWQT-QRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQ 289
Cdd:cd19138 210 KEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAE 264
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-287 |
2.46e-44 |
|
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: 152.34 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTWK---------SEPGLVKQAVIWALESGYRHIDCAPIYA---NEPEIGEAFqetmgpdKGIRREDVFVT 79
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAI-------KDFPREDLFIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 80 SKLWNTKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAfqrgdtpfprkedgtllydDIDYKLTWAAMEKLVGKGLVRA 159
Cdd:cd19137 74 TKVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNP-------------------NIPLEETLSAMAEGVRQGLIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 160 IGLSNFNSRQIDDILSVASIKPTVLQVESHPYLAQVE---LLSHCRDRGLVMTAYSPLgspdrawkhpDEPVLLEEPAIA 236
Cdd:cd19137 135 IGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEDRDPErdgLLEYCQKNGITVVAYSPL----------RRGLEKTNRTLE 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 528482668 237 ALAKKYNKTPAQIIIRWQTQR-GVVTIPKSITQSRIKENIQVFDFTLESEEM 287
Cdd:cd19137 205 EIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEM 256
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
10-298 |
1.03e-36 |
|
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: 133.77 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 10 STGRKMPLLGLGTW-------KSEPGLVKQAVIWALESGYRHIDCAPIY---ANEPEIGEAFqetmgpdKGIRREDVFVT 79
Cdd:COG0667 8 RSGLKVSRLGLGTMtfggpwgGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEAL-------KGRPRDDVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 80 SKL-WNTKHHPDDVEPSLLKTLKDLKL-------EYLDLYLIHWPYAfqrgDTPFprkEDgtllyddidyklTWAAMEKL 151
Cdd:COG0667 81 TKVgRRMGPGPNGRGLSREHIRRAVEAslrrlgtDYIDLYQLHRPDP----DTPI---EE------------TLGALDEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 152 VGKGLVRAIGLSNFNSRQIDDILSVAS--IKPTVLQVEshpY-----LAQVELLSHCRDRGLVMTAYSPLGS-------- 216
Cdd:COG0667 142 VREGKIRYIGVSNYSAEQLRRALAIAEglPPIVAVQNE---YslldrSAEEELLPAARELGVGVLAYSPLAGglltgkyr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 217 -------PDRAWKHPDEPVLLEE-----PAIAALAKKYNKTPAQIIIRWQTQRGVVTIP----KSITQsrIKENIQVFDF 280
Cdd:COG0667 219 rgatfpeGDRAATNFVQGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSVipgaRSPEQ--LEENLAAADL 296
|
330
....*....|....*...
gi 528482668 281 TLESEEMSQVTALHRGWR 298
Cdd:COG0667 297 ELSAEDLAALDAALAAVP 314
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
18-288 |
3.85e-36 |
|
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: 131.97 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTWK-----------SEPGLVKQAVIWALESGYRHIDCAPIYAN---EPEIGEAFQETMgpdkgiRREDVFVTSKLW 83
Cdd:cd19093 5 LGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG------DRDEVVIATKFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 84 NT--KHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFprkedgtllyddidykltWAAMEKLVGKGLVRAIG 161
Cdd:cd19093 79 PLpwRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLVRAVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 162 LSNFNSRQI---DDILSVASIKPTVLQVE---SHPYLAQVELLSHCRDRGLVMTAYSPLG---------------SPDRA 220
Cdd:cd19093 141 VSNYSADQLrraHKALKERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspenpppGGRRR 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528482668 221 W-----KHPDEPVLLeepAIAALAKKYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMS 288
Cdd:cd19093 221 LfgrknLEKVQPLLD---ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVA 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
18-288 |
5.40e-34 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 126.10 E-value: 5.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTW--------KSEPGLVKQAVIWALESGYRHIDCAPIYAN---EPEIGEAFQEtmgpdkgiRREDVFVTSK---LW 83
Cdd:cd19084 7 IGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG--------RRDDVVIATKcglRW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 84 NTKHH------PD----DVEPSLLKTLKdlklEYLDLYLIHWPyafqRGDTPFprkEDgtllyddidyklTWAAMEKLVG 153
Cdd:cd19084 79 DGGKGvtkdlsPEsirkEVEQSLRRLQT----DYIDLYQIHWP----DPNTPI---EE------------TAEALEKLKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 154 KGLVRAIGLSNFNSRQIDDILSVASIkpTVLQVeshPY-----LAQVELLSHCRDRGLVMTAYSPLG------------- 215
Cdd:cd19084 136 EGKIRYIGVSNFSVEQLEEARKYGPI--VSLQP---PYsmlerEIEEELLPYCRENGIGVLPYGPLAqglltgkykkept 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 216 --SPDRAWKHPD--EPVLLEEPAIAA----LAKKYNKTPAQIIIRWQTQR-GVVTI---PKSITQsrIKENIQVFDFTLE 283
Cdd:cd19084 211 fpPDDRRSRFPFfrGENFEKNLEIVDklkeIAEKYGKSLAQLAIAWTLAQpGVTSAivgAKNPEQ--LEENAGALDWELT 288
|
....*
gi 528482668 284 SEEMS 288
Cdd:cd19084 289 EEELK 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
18-292 |
1.03e-33 |
|
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: 125.39 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTW---------KSEPGLVKQAVIWALESGYRHIDCAPIYAN---EPEIGEAFQEtmgpdkgiRREDVFVTSKLWNT 85
Cdd:cd19085 4 LGLGCWqfgggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG--------RRDDVVIATKVSPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 86 KHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgDTPFPRKEdgtllyddidyklTWAAMEKLVGKGLVRAIGLSNF 165
Cdd:cd19085 76 NLTPEDVRKSCERSLKRLGTDYIDLYQIHWP------SSDVPLEE-------------TMEALEKLKEEGKIRAIGVSNF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 166 NSRQIDDILSVASIkpTVLQVeshPY-L----AQVELLSHCRDRGLVMTAYSPL------GSPDRAWKHPD--------- 225
Cdd:cd19085 137 GPAQLEEALDAGRI--DSNQL---PYnLlwraIEYEILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPgdartrlfr 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 226 --EPVLLEE--PAIAAL---AKKYNKTPAQIIIRWQTQRGVVTIPksITQSR----IKENIQVFDFTLESEEMSQVTA 292
Cdd:cd19085 212 hfEPGAEEEtfEALEKLkeiADELGVTMAQLALAWVLQQPGVTSV--IVGARnpeqLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
18-276 |
2.44e-25 |
|
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: 101.44 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTWK-SEPGLVKQA---VIWALESGYRHIDCAPIYAN---EPEIGEAFQETmgpdkgIRREDVFVTSKLWNTKH--- 87
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAfalLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGR------GNRDDVVIATKGGHPPGgdp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 88 -----HPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgDTPFPRKEdgtllyddidyklTWAAMEKLVGKGLVRAIGL 162
Cdd:cd06660 77 srsrlSPEHIRRDLEESLRRLGTDYIDLYYLHRD------DPSTPVEE-------------TLEALNELVREGKIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 163 SNFNSRQIDDILSVAS----IKPTVLQVE-S--HPYLAQVELLSHCRDRGLVMTAYSPLGSpdrawkhpdepvlleepai 235
Cdd:cd06660 138 SNWSAERLAEALAYAKahglPGFAAVQPQySllDRSPMEEELLDWAEENGLPLLAYSPLAR------------------- 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 528482668 236 aalakkynkTPAQIIIRWQTQRGVVTIP----KSITQsrIKENIQ 276
Cdd:cd06660 199 ---------GPAQLALAWLLSQPFVTVPivgaRSPEQ--LEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-293 |
1.42e-22 |
|
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: 95.43 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTWKS-----EPGLVKQ-------AVIWALESGYRHIDCAPIYA---NEPEIGEAFQEtmgpdkgiRREDVFVTSK- 81
Cdd:cd19102 4 IGLGTWAIggggwGGGWGPQddrdsiaAIRAALDLGINWIDTAAVYGlghSEEVVGRALKG--------LRDRPIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 82 --LWNTKHH------PDDVEPSLLKTLKDLKLEYLDLYLIHWPYafqrGDTPFprkEDGtllyddidykltWAAMEKLVG 153
Cdd:cd19102 76 glLWDEEGRirrslkPASIRAECEASLRRLGVDVIDLYQIHWPD----PDEPI---EEA------------WGALAELKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 154 KGLVRAIGLSNFNSRQIDDILSVASIkpTVLQVeshPYLA-----QVELLSHCRDRGLVMTAYSPLGS--------PDRA 220
Cdd:cd19102 137 EGKVRAIGVSNFSVDQMKRCQAIHPI--ASLQP---PYSLlrrgiEAEILPFCAEHGIGVIVYSPMQSglltgkmtPERV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 221 WKHPDEPV-----LLEEPAIA----------ALAKKYNKTPAQIIIRWQTQRGVVT--IPKSITQSRIKENIQVFDFTLE 283
Cdd:cd19102 212 ASLPADDWrrrspFFQEPNLArnlalvdalrPIAERHGRTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGAADLRLT 291
|
330
....*....|
gi 528482668 284 SEEMSQVTAL 293
Cdd:cd19102 292 PEELAEIEAL 301
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
12-290 |
1.61e-22 |
|
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: 95.59 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 12 GRKMPLLGLGTW-------KSEPGLVKQAVI-WALESGYRHIDCAPIYA-NEPEIGEAFQETMGpdkgiRREDVFVTSKL 82
Cdd:cd19144 10 GPSVPALGFGAMglsafygPPKPDEERFAVLdAAFELGCTFWDTADIYGdSEELIGRWFKQNPG-----KREKIFLATKF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 83 WNTKH----------HPDDVEPSLLKTLKDLKLEYLDLYLIHwpyafqRGDTPFPrkedgtllyddidYKLTWAAMEKLV 152
Cdd:cd19144 85 GIEKNvetgeysvdgSPEYVKKACETSLKRLGVDYIDLYYQH------RVDGKTP-------------IEKTVAAMAELV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 153 GKGLVRAIGLSNFNSRQIDDILSVASIkpTVLQVESHPYL-----AQVELLSHCRDRGLVMTAYSPLG---------SPD 218
Cdd:cd19144 146 QEGKIKHIGLSECSAETLRRAHAVHPI--AAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGrgfltgairSPD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 219 ---------RAWKHPDE--PVLLE-EPAIAALAKKYNKTPAQIIIRWQTQRG--VVTIPKSITQSRIKENIQVFDFTLES 284
Cdd:cd19144 224 dfeegdfrrMAPRFQAEnfPKNLElVDKIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTE 303
|
....*.
gi 528482668 285 EEMSQV 290
Cdd:cd19144 304 EEEKEI 309
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-283 |
7.74e-19 |
|
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: 84.19 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 15 MPLLGLGTWkSEPGLVKQAVI---WALESGYRHIDCAPIYA---NEPEIGEAfqetMGPdkgiRREDVFVTSKLWNTKHH 88
Cdd:cd19088 9 MRLTGPGIW-GPPADREEAIAvlrRALELGVNFIDTADSYGpdvNERLIAEA----LHP----YPDDVVIATKGGLVRTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 89 PDDVEPsllktlkDLKLEYL----------------DLYLIHWPyafqrgDTPFPRKEdgtllyddidyklTWAAMEKLV 152
Cdd:cd19088 80 PGWWGP-------DGSPEYLrqaveaslrrlgldriDLYQLHRI------DPKVPFEE-------------QLGALAELQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 153 GKGLVRAIGLSNFNSRQIDDILSVASIkptvLQVESHPYLAQ---VELLSHCRDRGLVMTAYSPLGSpdrawkhpdEPVL 229
Cdd:cd19088 134 DEGLIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLANrddEGVLDYCEAAGIAFIPWFPLGG---------GDLA 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 528482668 230 LEEPAIAALAKKYNKTPAQIIIRWQTQRG--VVTIPKSITQSRIKENIQVFDFTLE 283
Cdd:cd19088 201 QPGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
11-286 |
3.04e-18 |
|
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: 83.48 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTW---------KSEPGLVKQAVIWALESGYRHIDCAPIY---ANEPEIGEAFqetmgpdKGiRREDVFV 78
Cdd:cd19149 7 SGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAI-------KG-RRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 79 TSK---LWNTK---HHP-----------------DDVEPSLLKTLKdlklEYLDLYLIHWPyafqrgDTPFPRKEdgtll 135
Cdd:cd19149 79 ATKcglRWDREggsFFFvrdgvtvyknlspesirEEVEQSLKRLGT----DYIDLYQTHWQ------DVETPIEE----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 136 yddidyklTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASIkpTVLQvESHPYL---AQVELLSHCRDRGLVMTAYS 212
Cdd:cd19149 144 --------TMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQ-EKYSMLdrgIEKELLPYCKKNNIAFQAYS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 213 PLGS--------PD--------RAWKHPDEP-------VLLEepAIAALAKKYNKTPAQIIIRWQTQRG--VVTIPKSIT 267
Cdd:cd19149 213 PLEQglltgkitPDrefdagdaRSGIPWFSPenrekvlALLE--KWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARK 290
|
330
....*....|....*....
gi 528482668 268 QSRIKENIQVFDFTLESEE 286
Cdd:cd19149 291 PEQAEENAKAGDIRLSAED 309
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
10-287 |
2.07e-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: 81.09 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 10 STGRKMPLLGLGTW-----KSEPGLVKQAVIW-----ALESGYRHIDCAPIYAN---EPEIGEAFQETmgpdkgIRREDV 76
Cdd:cd19079 7 NSGLKVSRLCLGCMsfgdpKWRPWVLDEEESRpiikrALDLGINFFDTANVYSGgasEEILGRALKEF------APRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 77 FVTSKLWNT------------KHHPDDVEPSLLKTLKdlklEYLDLYLIH-WPYafqrgDTPFprkEDgtllyddidykl 143
Cdd:cd19079 81 VIATKVYFPmgdgpngrglsrKHIMAEVDASLKRLGT----DYIDLYQIHrWDY-----ETPI---EE------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 144 TWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASI----KPTVLQveSHPYLAQVE----LLSHCRDRGLVMTAYSPL- 214
Cdd:cd19079 137 TLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKngwtKFVSMQ--NHYNLLYREeereMIPLCEEEGIGVIPWSPLa 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 215 -GSPDRAWKHP---------------------DEPVLLeepAIAALAKKYNKTPAQIIIRWQTQRGVVTIPksI----TQ 268
Cdd:cd19079 215 rGRLARPWGDTterrrsttdtaklkydyfteaDKEIVD---RVEEVAKERGVSMAQVALAWLLSKPGVTAP--IvgatKL 289
|
330
....*....|....*....
gi 528482668 269 SRIKENIQVFDFTLESEEM 287
Cdd:cd19079 290 EHLEDAVAALDIKLSEEEI 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-293 |
3.66e-17 |
|
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: 80.74 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGT--------WKSEPGLVKQA-----VIWALESGYRHIDCAPIYAN-EPEI--GEAFqetmgpdKGiRRE 74
Cdd:cd19091 9 SGLKVSELALGTmtfgggggFFGAWGGVDQEeadrlVDIALDAGINFFDTADVYSEgESEEilGKAL-------KG-RRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 75 DVFVTSKLWN-----------TKHH-PDDVEPSLLKTLKdlklEYLDLYLIHWPYAFqrgdTPFprkeDGTLlyddidyk 142
Cdd:cd19091 81 DVLIATKVRGrmgegpndvglSRHHiIRAVEASLKRLGT----DYIDLYQLHGFDAL----TPL----EETL-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 143 ltwAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVAS----IKPTVLQVeshpYLAQV------ELLSHCRDRGLVMTAYS 212
Cdd:cd19091 141 ---RALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQA----YYSLLgrdlehELMPLALDQGVGLLVWS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 213 PL------GSPDRAWKHP----------DEPVLLEE---PAIAAL---AKKYNKTPAQIIIRW-QTQRGVVTI---PKSI 266
Cdd:cd19091 214 PLaggllsGKYRRGQPAPegsrlrrtgfDFPPVDRErgyDVVDALreiAKETGATPAQVALAWlLSRPTVSSViigARNE 293
|
330 340
....*....|....*....|....*..
gi 528482668 267 TQsrIKENIQVFDFTLESEEMSQVTAL 293
Cdd:cd19091 294 EQ--LEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
37-289 |
3.94e-17 |
|
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: 80.34 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 37 ALESGYRHIDCAPIY---ANEPEIGEAFQEtmgpdkgiRREDVFVTSK---LWNTKHH-------PDDVEPSLLKTLKDL 103
Cdd:cd19076 41 ALELGVTFLDTADMYgpgTNEELLGKALKD--------RRDEVVIATKfgiVRDPGSGfrgvdgrPEYVRAACEASLKRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 104 KLEYLDLYLIHwpyafqRGDTPFPRKEdgtllyddidyklTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASIkpTV 183
Cdd:cd19076 113 GTDVIDLYYQH------RVDPNVPIEE-------------TVGAMAELVEEGKVRYIGLSEASADTIRRAHAVHPI--TA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 184 LQVESHPYLAQVE--LLSHCRDRGLVMTAYSPLG---------SPDRawKHPDE-----PVLLEE---------PAIAAL 238
Cdd:cd19076 172 VQSEYSLWTRDIEdeVLPTCRELGIGFVAYSPLGrgfltgaikSPED--LPEDDfrrnnPRFQGEnfdknlklvEKLEAI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528482668 239 AKKYNKTPAQIIIRWQTQRG--VVTIPKSITQSRIKENIQVFDFTLESEEMSQ 289
Cdd:cd19076 250 AAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAE 302
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-241 |
6.07e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 78.78 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTW---KSEPGLVKQAviwaLESGYRHIDCAPIYAN---EPEIGEAFqetmgpdKGIRREDVFVTSKLWN 84
Cdd:cd19105 9 TGLKVSRLGFGGGglpRESPELLRRA----LDLGINYFDTAEGYGNgnsEEIIGEAL-------KGLRRDKVFLATKASP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 85 TKHH--PDDVEPSLLKTLKDLKLEYLDLYLIHwpyafqRGDTPFPRKEDGTLLyddidykltwAAMEKLVGKGLVRAIGl 162
Cdd:cd19105 78 RLDKkdKAELLKSVEESLKRLQTDYIDIYQLH------GVDTPEERLLNEELL----------EALEKLKKEGKVRFIG- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 163 snfnsrqiddiLSVASIKPTVLQ--VESHPYlaqvellshcrDrgLVMTAYSPLGSPDRAwkhpdepvlleEPAIAALAK 240
Cdd:cd19105 141 -----------FSTHDNMAEVLQaaIESGWF-----------D--VIMVAYNFLNQPAEL-----------EEALAAAAE 185
|
.
gi 528482668 241 K 241
Cdd:cd19105 186 K 186
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
19-290 |
6.29e-17 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 79.59 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 19 GLG----TWKSEPGLVKQA--VI-WALESGYRHIDCA------PIYANEPEIGEAFQETmgPDKgirREDVFVTSKL-WN 84
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAfeTMkAALDAGSNLWNGGefygppDPHANLKLLARFFRKY--PEY---ADKVVLSVKGgLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 85 TKHH-----PDDVEPSLLKTLKD-LKLEYLDLYlihwpyAFQRGDTPFPRKEdgtllyddidyklTWAAMEKLVGKGLVR 158
Cdd:cd19077 84 PDTLrpdgsPEAVRKSIENILRAlGGTKKIDIF------EPARVDPNVPIEE-------------TIKALKELVKEGKIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 159 AIGLSNFNSRQIDDILSVASIkpTVLQVESHPYLAQVE---LLSHCRDRGLVMTAYSPLG-------------SPDRAW- 221
Cdd:cd19077 145 GIGLSEVSAETIRRAHAVHPI--AAVEVEYSLFSREIEengVLETCAELGIPIIAYSPLGrglltgriksladIPEGDFr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 222 KHPDEP---------VLLEepAIAALAKKYNKTPAQIIIRW---QTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQ 289
Cdd:cd19077 223 RHLDRFngenfeknlKLVD--ALQELAEKKGCTPAQLALAWilaQSGPKIIPIPGSTTLERVEENLKAANVELTDEELKE 300
|
.
gi 528482668 290 V 290
Cdd:cd19077 301 I 301
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
106-291 |
1.77e-16 |
|
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: 78.41 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 106 EYLDLYLIHWPyafqrgDTPFPRKEdgtllyddidyklTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVAS----IKP 181
Cdd:cd19081 114 DYIDLYQAHWD------DPATPLEE-------------TLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhglPRY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 182 TVLQ-----VESHPYlaQVELLSHCRDRGLVMTAYSPLGS-------------PDRAWKHPDEPVLLEEP------AIAA 237
Cdd:cd19081 175 VSLQpeynlVDRESF--EGELLPLCREEGIGVIPYSPLAGgfltgkyrseadlPGSTRRGEAAKRYLNERglrildALDE 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 238 LAKKYNKTPAQIIIRWQTQRGVVTIP----KSITQsrIKENIQVFDFTLESEEMSQVT 291
Cdd:cd19081 253 VAAEHGATPAQVALAWLLARPGVTAPiagaRTVEQ--LEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
10-286 |
4.59e-16 |
|
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: 76.83 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 10 STGRKMPLLGLGTW-----KSEPGLVKQAVIWALESGYRHIDCAPIYAN---EPEIGEAFQEtmgpdKGIRREDVFVTSK 81
Cdd:cd19092 1 PEGLEVSRLVLGCMrladwGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALAL-----NPGLREKIEIQTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 82 ----------LWNTKHH---PDDVEPSLLKTLKDLKLEYLDLYLIHwpyafqRGDTpfprkedgtLLyddiDYKLTWAAM 148
Cdd:cd19092 76 cgirlgddprPGRIKHYdtsKEHILASVEGSLKRLGTDYLDLLLLH------RPDP---------LM----DPEEVAEAF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 149 EKLVGKGLVRAIGLSNFNSRQIDDILSVASIKPTVLQVE---SHPYLAQVELLSHCRDRGLVMTAYSPLGSpDRAWKHPD 225
Cdd:cd19092 137 DELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLGG-GRLFGGFD 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528482668 226 EPVLLEEPAIAALAKKYNKTPAQIIIRWQTQR--GVVTIPKSITQSRIKENIQVFDFTLESEE 286
Cdd:cd19092 216 ERFQRLRAALEELAEEYGVTIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
3-286 |
1.05e-15 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 75.96 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 3 MNDFAVLSTGRKMPLLGLGTWK-SEPGLVKQAVI----WALESGYRHIDCAPIYAN---EPEIGEAFQETmgpdkGIRRE 74
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRlGEWDLSPAEAAalieAALELGITTFDHADIYGGytcEALFGEALKLS-----PSLRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 75 DVFVTSK---------LWNTKHHPD--------DVEPSLLKTLKdlklEYLDLYLIHwpyafqRGDTPFPRKEdgtllyd 137
Cdd:COG4989 76 KIELQTKcgirlpseaRDNRVKHYDtskehiiaSVEGSLRRLGT----DYLDLLLLH------RPDPLMDPEE------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 138 didyklTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASIKPTVLQVESHPYLAQV---ELLSHCRDRGLVMTAYSPL 214
Cdd:COG4989 139 ------VAEAFDELKASGKVRHFGVSNFTPSQFELLQSALDQPLVTNQIELSLLHTDAfddGTLDYCQLNGITPMAWSPL 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528482668 215 G-----SPDrawkHPDEPVLLEepAIAALAKKYNKTPAQIIIRWQTQR--GVVTIPKSITQSRIKENIQVFDFTLESEE 286
Cdd:COG4989 213 AggrlfGGF----DEQFPRLRA--ALDELAEKYGVSPEAIALAWLLRHpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
11-303 |
4.41e-15 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 74.86 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTW----KSEPGLVKQaVIWALESGYRHIDCAPIYAN-EPEIGEAFQEtmgpdkgiRREDVFVTSKLWNT 85
Cdd:COG1453 9 TGLEVSVLGFGGMrlprKDEEEAEAL-IRRAIDNGINYIDTARGYGDsEEFLGKALKG--------PRDKVILATKLPPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 86 KHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFprKEDGTLlyddidykltwAAMEKLVGKGLVRAIGLSNF 165
Cdd:COG1453 80 VRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVL--KPGGAL-----------EALEKAKAEGKIRHIGFSTH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 166 NSrqIDDILSVasikptvlqVESHP--------------YLAQVELLSHCRDRGL---VMtaySPL--GSpdrawkhpde 226
Cdd:COG1453 147 GS--LEVIKEA---------IDTGDfdfvqlqynyldqdNQAGEEALEAAAEKGIgviIM---KPLkgGR---------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 227 pvLLEEPAIAALAKKYNKTPAQIIIRW-QTQRGVVTI---PKSITQsrIKENIQVFD--FTLESEEMSQVTALH------ 294
Cdd:COG1453 203 --LANPPEKLVELLCPPLSPAEWALRFlLSHPEVTTVlsgMSTPEQ--LDENLKTADnlEPLTEEELAILERLAeelgel 278
|
330
....*....|....
gi 528482668 295 -----RGWRYIVPT 303
Cdd:COG1453 279 lkdfcTGCGYCMPC 292
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
19-290 |
4.41e-15 |
|
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: 74.27 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 19 GLGTWK--------SEPGLVKQAVIWALESGYRHIDCAPIY---ANEPEIGEAFQEtmgpdkGIRREDVFVTSKL---WN 84
Cdd:cd19148 8 ALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKE------YGKRDRVVIATKVgleWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 85 TKHHPD----------DVEPSLLKTLKdlklEYLDLYLIHWPyafqrgDTPFPRKEdgtllyddidyklTWAAMEKLVGK 154
Cdd:cd19148 82 EGGEVVrnssparirkEVEDSLRRLQT----DYIDLYQVHWP------DPLVPIEE-------------TAEALKELLDE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 155 GLVRAIGLSNFNSRQIDDILSVASikptvLQVESHPY-----LAQVELLSHCRDRGLVMTAYSPLG--------SPDRAW 221
Cdd:cd19148 139 GKIRAIGVSNFSPEQMETFRKVAP-----LHTVQPPYnlferEIEKDVLPYARKHNIVTLAYGALCrgllsgkmTKDTKF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 222 KHPD----EPVLLEE------PAIAAL----AKKYNKTPAQIIIRWQTQRGVVTIpkSITQSRIKENIQ----VFDFTLE 283
Cdd:cd19148 214 EGDDlrrtDPKFQEPrfsqylAAVEELdklaQERYGKSVIHLAVRWLLDQPGVSI--ALWGARKPEQLDavdeVFGWSLN 291
|
....*..
gi 528482668 284 SEEMSQV 290
Cdd:cd19148 292 DEDMKEI 298
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
18-293 |
1.35e-14 |
|
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: 73.22 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGT-----------WKSEPG--LVKQAviwaLESGYRHIDCAPIYA---NEPEIGEAFqetmgpdKGIRREDVFVTSK 81
Cdd:cd19083 14 IGLGTnavgghnlypnLDEEEGkdLVREA----LDNGVNLLDTAFIYGlgrSEELVGEVL-------KEYNRNEVVIATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 82 --LWNTKH------HPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqRGDTPfprKEDGTllyddidykltwAAMEKLVG 153
Cdd:cd19083 83 gaHKFGGDgsvlnnSPEFLRSAVEKSLKRLNTDYIDLYYIHFP----DGETP---KAEAV------------GALQELKD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 154 KGLVRAIGLSNFNSRQIDdilsvASIKPTVLQVESHPY-LAQVE----LLSHCRDRGLVMTAYSPL------GSPDRAWK 222
Cdd:cd19083 144 EGKIRAIGVSNFSLEQLK-----EANKDGYVDVLQGEYnLLQREaeedILPYCVENNISFIPYFPLasgllaGKYTKDTK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 223 HPDEPVLLEEP---------------AIAALAKKYNKTPAQIIIRWQ-TQRGV-VTIPKSITQSRIKENIQVFDFTLESE 285
Cdd:cd19083 219 FPDNDLRNDKPlfkgerfsenldkvdKLKSIADEKGVTVAHLALAWYlTRPAIdVVIPGAKRAEQVIDNLKALDVTLTEE 298
|
....*...
gi 528482668 286 EMSQVTAL 293
Cdd:cd19083 299 EIAFIDAL 306
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
37-290 |
1.76e-14 |
|
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: 72.85 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 37 ALESGYRHIDCAPIY---ANEPEIGEAFqetmgpdKGIRREDVFVTSKLWNT---------KHHPDDVEPSLLKTLKDLK 104
Cdd:cd19145 42 AFNSGVTFLDTSDIYgpnTNEVLLGKAL-------KDGPREKVQLATKFGIHeiggsgvevRGDPAYVRAACEASLKRLD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 105 LEYLDLYLIHwpyafqRGDTPFPrkedgtllyddidYKLTWAAMEKLVGKGLVRAIGLSNFNSrqiDDILSVASIKP-TV 183
Cdd:cd19145 115 VDYIDLYYQH------RIDTTVP-------------IEITMGELKKLVEEGKIKYIGLSEASA---DTIRRAHAVHPiTA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 184 LQVESHPYLAQVE--LLSHCRDRGLVMTAYSPLGSPDRAWKhpdePVLLEEPA-------------------------IA 236
Cdd:cd19145 173 VQLEWSLWTRDIEeeIIPTCRELGIGIVPYSPLGRGFFAGK----AKLEELLEnsdvrkshprfqgenleknkvlyerVE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 528482668 237 ALAKKYNKTPAQIIIRWQTQRG--VVTIPKSITQSRIKENIQVFDFTLESEEMSQV 290
Cdd:cd19145 249 ALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
18-285 |
5.11e-14 |
|
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: 71.08 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTWKSEPGLV-----KQAVIWALESGYRHIDCAPIYAN---EPEIGEAFqetmgpdKGIRREDVFVTSKL-WNTKHH 88
Cdd:cd19074 7 LSLGTWLTFGGQVddedaKACVRKAYDLGINFFDTADVYAAgqaEEVLGKAL-------KGWPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 89 PDD--------VEpSLLKTLKDLKLEYLDLYLIHWPYAfqrgDTPfprkedgtlLYDdidyklTWAAMEKLVGKGLVRAI 160
Cdd:cd19074 80 PNDrglsrkhiFE-SIHASLKRLQLDYVDIYYCHRYDP----ETP---------LEE------TVRAMDDLIRQGKILYW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 161 GLSNFNSRQIDDILSVAS----IKPTVLQVESHpYLAQV---ELLSHCRDRGLVMTAYSPL-----------GSP---DR 219
Cdd:cd19074 140 GTSEWSAEQIAEAHDLARqfglIPPVVEQPQYN-MLWREieeEVIPLCEKNGIGLVVWSPLaqglltgkyrdGIPppsRS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 220 AWKHPD----------EPVLLEEPAIAALAKKYNKTPAQIIIRWQTQRGVVT--IPKSITQSRIKENIQVFDFTLESE 285
Cdd:cd19074 219 RATDEDnrdkkrrlltDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-225 |
9.93e-14 |
|
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: 69.43 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 10 STGRKMPLLGLGTWKSEPGLVKQAVI---WALESGYRHIDCAPIYAN-EPEIGEAFQEtmgpdkgiRREDVFVTSKLWNT 85
Cdd:cd19100 6 RTGLKVSRLGFGGGPLGRLSQEEAAAiirRALDLGINYFDTAPSYGDsEEKIGKALKG--------RRDKVFLATKTGAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 86 KhhPDDVEPSLLKTLKDLKLEYLDLYLIHwpYAFQRGDTPFPRKEDGTLlyddidykltwAAMEKLVGKGLVRAIGLSNF 165
Cdd:cd19100 78 D--YEGAKRDLERSLKRLGTDYIDLYQLH--AVDTEEDLDQVFGPGGAL-----------EALLEAKEEGKIRFIGISGH 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528482668 166 NSRQIDDILSVASIKpTVL----QVESHPYLAQVELLSHCRDRGLVMTAYSPLGspDRAWKHPD 225
Cdd:cd19100 143 SPEVLLRALETGEFD-VVLfpinPAGDHIDSFREELLPLAREKGVGVIAMKVLA--GGRLLSGD 203
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
18-277 |
3.28e-13 |
|
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: 68.42 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTWK-------SEPGLVKQAVIWALESGYRHIDCAPIYAN-EPEIGEAFqetmgpdKGIRREDVFVTSKLW------ 83
Cdd:cd19095 3 LGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL-------AGLRRDDLFIATKVGthgegg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 84 -NTKHH-PDDVEPSLLKTLKDLKLEYLDLYLIHwpyafqrgdTPFPRKEDGTLLyddidykltwAAMEKLVGKGLVRAIG 161
Cdd:cd19095 76 rDRKDFsPAAIRASIERSLRRLGTDYIDLLQLH---------GPSDDELTGEVL----------ETLEDLKAAGKVRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 162 LSNFNSRqIDDILSVASIkpTVLQVESHPYL-AQVELLSHCRDRGLVMTAYSPLGSPDRAWKHPDEPVLLEEPAIAALAK 240
Cdd:cd19095 137 VSGDGEE-LEAAIASGVF--DVVQLPYNVLDrEEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAA 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 528482668 241 KYN-KTPAQIIIRWQTQRGVVT--IPKSITQSRIKENIQV 277
Cdd:cd19095 214 EIGgATWAQAALRFVLSHPGVSsaIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
37-263 |
4.62e-13 |
|
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: 68.75 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 37 ALESGYRHIDCAPIYAN---EPEIGEAFQEtmgpdkgiRREDVFVTSKLW------------NTKHHPDDVEPSLLKTLK 101
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAG--------RRDDIVLATKVFgpmgddpndrglSRRHIRRAVEASLRRLQT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 102 dlklEYLDLYLIHwpyAFQRgDTPFprkEDgtllyddidyklTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASIKP 181
Cdd:cd19087 111 ----DYIDLYQMH---HFDR-DTPL---EE------------TLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 182 TV-LQVESHPY-----LAQVELLSHCRDRGLVMTAYSPLG--------------SPDRAWKHPDEPVLLEEP-------A 234
Cdd:cd19087 168 LLrFVSEQPMYnllkrQAELEILPAARAYGLGVIPYSPLAgglltgkygkgkrpESGRLVERARYQARYGLEeyrdiaeR 247
|
250 260
....*....|....*....|....*....
gi 528482668 235 IAALAKKYNKTPAQIIIRWQTQRGVVTIP 263
Cdd:cd19087 248 FEALAAEAGLTPASLALAWVLSHPAVTSP 276
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
37-279 |
4.91e-13 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 67.97 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 37 ALESGYRHIDCAPIYAN---EPEIGEAFqetmgpdKGIRREDVFVTSKL-WNTKHHPDDVEPSLLKTLKDLKLEYLDLYL 112
Cdd:cd19096 30 AIDAGINYFDTAYGYGGgksEEILGEAL-------KEGPREKFYLATKLpPWSVKSAEDFRRILEESLKRLGVDYIDFYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 113 IHWpyaFQRGDTPFPRKEDGtllyddidyklTWAAMEKLVGKGLVRAIGLSnF--NSRQIDDILsvasikptvlqvESHP 190
Cdd:cd19096 103 LHG---LNSPEWLEKARKGG-----------LLEFLEKAKKEGLIRHIGFS-FhdSPELLKEIL------------DSYD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 191 --------------YLAQVELLSHCRDRGL---VMtaySPLGSPDRAWKhpdepvlleEPAIAALAKKYNKTPAQIIIRW 253
Cdd:cd19096 156 fdfvqlqynyldqeNQAGRPGIEYAAKKGMgviIM---EPLKGGGLANN---------PPEALAILCGAPLSPAEWALRF 223
|
250 260 270
....*....|....*....|....*....|
gi 528482668 254 -QTQRGVVTI---PKSITQsrIKENIQVFD 279
Cdd:cd19096 224 lLSHPEVTTVlsgMSTPEQ--LDENIAAAD 251
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
37-287 |
6.65e-12 |
|
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: 65.28 E-value: 6.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 37 ALESGYRHIDCAPIYA----------NEPEIGEAFQetmgpDKGiRREDVFVTSKL--------W----NTKHHPDDVEP 94
Cdd:cd19094 27 AFDEGVNFIDTAEMYPvppspetqgrTEEIIGSWLK-----KKG-NRDKVVLATKVagpgegitWprggGTRLDRENIRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 95 SLLKTLKDLKLEYLDLYLIHWP--YAFQRGDTPFPRKEDgtlLYDDIDYKLTWAAMEKLVGKGLVRAIGLSN-------- 164
Cdd:cd19094 101 AVEGSLKRLGTDYIDLYQLHWPdrYTPLFGGGYYTEPSE---EEDSVSFEEQLEALGELVKAGKIRHIGLSNetpwgvmk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 165 FNSRQIDDILS-VASIKptvlqvesHPY----------LAQVellshCRDRGLVMTAYSPLG----------SPDRA--W 221
Cdd:cd19094 178 FLELAEQLGLPrIVSIQ--------NPYsllnrnfeegLAEA-----CHRENVGLLAYSPLAggvltgkyldGAARPegG 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 222 KHPD----EPVLLEEPAIAA------LAKKYNKTPAQIIIRWQTQRGVV--TIPKSITQSRIKENIQVFDFTLeSEEM 287
Cdd:cd19094 245 RLNLfpgyMARYRSPQALEAvaeyvkLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPL-SDEL 321
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-276 |
1.02e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 64.28 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 38 LESGYRHIDCAPIYA----------NEPEIGEAFQetmgpDKGiRREDVFVTSKL---------WNTKHH---PDDVEPS 95
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGRWLK-----DRG-NRDDVVIATKVgagprdpdgGPESPEglsAETIEQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 96 LLKTLKDLKLEYLDLYLIHwpyafqrgdtpfprkedgtllYDDIDYKL--TWAAMEKLVGKGLVRAIGLSNFNSRQIDDI 173
Cdd:cd19752 101 IDKSLRRLGTDYIDLYYAH---------------------VDDRDTPLeeTLEAFNELVKAGKVRAIGASNFAAWRLERA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 174 LSVASIK----PTVLQvESHPYL-------------AQVELLSHCRDRG-LVMTAYSPL--GSPDRAWK-------HPDE 226
Cdd:cd19752 160 RQIARQQgwaeFSAIQ-QRHSYLrprpgadfgvqriVTDELLDYASSRPdLTLLAYSPLlsGAYTRPDRplpeqydGPDS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 528482668 227 PVLLEepAIAALAKKYNKTPAQIIIRWQTQRGVVTIP--KSITQSRIKENIQ 276
Cdd:cd19752 239 DARLA--VLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-293 |
1.31e-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: 64.21 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 33 AVIWALESGYRHIDCAPIYAN---EPEIGEAFQEtmgpdkgiRREDVFVTSKLWNTKHHPDD----VEPSLLKTLKDLKL 105
Cdd:cd19104 37 AVRRALDLGINFFDTAPSYGDgksEENLGRALKG--------LPAGPYITTKVRLDPDDLGDiggqIERSVEKSLKRLKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 106 EYLDLYLIHWPYAFQRGDTPFPrkedgTLLYDDIDYKL-TWAAMEKLVGKGLVRAIGLSNF-NSRQIDDILsvASIKPTV 183
Cdd:cd19104 109 DSVDLLQLHNRIGDERDKPVGG-----TLSTTDVLGLGgVADAFERLRSEGKIRFIGITGLgNPPAIRELL--DSGKFDA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 184 LQV----------ESHP--YLAQV--ELLSHCRDRGLVMTAYSPL------GSPDRAWKHPDEPVLLEEP------AIAA 237
Cdd:cd19104 182 VQVyynllnpsaaEARPrgWSAQDygGIIDAAAEHGVGVMGIRVLaagaltTSLDRGREAPPTSDSDVAIdfrraaAFRA 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 528482668 238 LAKKYNKTPAQIIIRWQ-TQRGVVTIPKSI-TQSRIKENIQVFDF-TLESEEMSQVTAL 293
Cdd:cd19104 262 LAREWGETLAQLAHRFAlSNPGVSTVLVGVkNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-216 |
1.82e-11 |
|
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: 62.88 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTW--------KSEPGLVKQAVIWALESGYRHIDCAPIYAN---EPEIGEAFQEtmgpdkgiRREDVFVTSK----L 82
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG--------RRDKVVIATKfgnrF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 83 WNTKHHPDDVEPSLLKTLKDL-----KLEYLDLYLIH-WPYAFQrgdtpfpRKEDgtllyddidyklTWAAMEKLVGKGL 156
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEAslkrlGTDYIDLYQLHnPPDEVL-------DNDE------------LFEALEKLKQEGK 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528482668 157 VRAIGLSnfnSRQIDDILS-VASIKPTVLQV-----ESHPYLaqvELLSHCRDRGLVMTAYSPLGS 216
Cdd:cd19086 139 IRAYGVS---VGDPEEALAaLRRGGIDVVQViynllDQRPEE---ELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-253 |
4.89e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 62.72 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTWKSEPGL-----VKQAVIWALESGYRHIDCAPIYAN---EPEIGEAFQETMGpDKGIRREDVFVTSK---LWNTK 86
Cdd:cd19099 6 LGLGTYRGDSDDetdeeYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIE-KGGIKRDEVVIVTKagyIPGDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 87 HHPDDVEPSLLKTLKDLKL------------------------------EYLDLYLIHWPYAFQrgdtpfpRKEDGTLLY 136
Cdd:cd19099 85 DEPLRPLKYLEEKLGRGLIdvadsaglrhcispayledqierslkrlglDTIDLYLLHNPEEQL-------LELGEEEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 137 DDIdyKLTWAAMEKLVGKGLVRAIGLSNFN-------SRQIDDILSVASIKPTVLQVESHPYLAQV-------------- 195
Cdd:cd19099 158 DRL--EEAFEALEEAVAEGKIRYYGISTWDgfrappaLPGHLSLEKLVAAAEEVGGDNHHFKVIQLplnllepealtekn 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528482668 196 -------ELLSHCRDRGLVMTAYSPLGSPDrawkhpdepVLLEEPAIAALAKKYNKTPAQIIIRW 253
Cdd:cd19099 236 tvkgealSLLEAAKELGLGVIASRPLNQGQ---------LLGELRLADLLALPGGATLAQRALQF 291
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
38-288 |
1.39e-10 |
|
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: 61.08 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 38 LESGYRHIDCAPIYAN---EPEIGEAFQEtmgpdkgiRREDVFVTSKL-WNTkhHPDD--------------VEPSLLKT 99
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAG--------NRDRIVLATKYtMNR--RPGDpnaggnhrknlrrsVEASLRRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 100 LKdlklEYLDLYLIHWPyafqrgdtpfprkeDGTLLYDDIdykltWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASI 179
Cdd:cd19080 111 QT----DYIDLLYVHAW--------------DFTTPVEEV-----MRALDDLVRAGKVLYVGISDTPAWVVARANTLAEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 180 K----PTVLQVESHpyLAQ----VELLSHCRDRGLVMTAYSPLGS--------------PDRAWKHPDEPVLLEEPAIA- 236
Cdd:cd19080 168 RgwspFVALQIEYS--LLErtpeRELLPMARALGLGVTPWSPLGGglltgkyqrgeegrAGEAKGVTVGFGKLTERNWAi 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 237 -----ALAKKYNKTPAQIIIRWQTQRGVVTIPkSI---TQSRIKENIQVFDFTLESEEMS 288
Cdd:cd19080 246 vdvvaAVAEELGRSAAQVALAWVRQKPGVVIP-IIgarTLEQLKDNLGALDLTLSPEQLA 304
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
37-290 |
2.80e-10 |
|
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: 60.32 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 37 ALESGYRHIDCAPIY---ANEPEIGEAFQEtmgpdkgiRREDVFVTSKLwntKHHPDDVEPSLLKTLKDLKL-------- 105
Cdd:cd19078 34 AVELGITFFDTAEVYgpyTNEELVGEALKP--------FRDQVVIATKF---GFKIDGGKPGPLGLDSRPEHirkavegs 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 106 ------EYLDLYLIHwpyafqRGDTPFPRKEdgtllyddidyklTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASI 179
Cdd:cd19078 103 lkrlqtDYIDLYYQH------RVDPNVPIEE-------------VAGTMKELIKEGKIRHWGLSEAGVETIRRAHAVCPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 180 kpTVLQVESH-----PylaQVELLSHCRDRGLVMTAYSPLG----------------SPDRAWKHPDEP-------VLLE 231
Cdd:cd19078 164 --TAVQSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGkgfltgkidentkfdeGDDRASLPRFTPealeanqALVD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528482668 232 epAIAALAKKYNKTPAQIIIRWQTQRG--VVTIPKSITQSRIKENIQVFDFTLESEEMSQV 290
Cdd:cd19078 239 --LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-293 |
1.16e-09 |
|
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: 58.50 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 14 KMPLLGLGTWK----------------SEPGLvKQAVIWALESGYRHIDCAPIY---ANEPEIGEAFqetmgpdKGIRRE 74
Cdd:cd19103 3 KLPKIALGTWSwgsggaggdqvfgnhlDEDTL-KAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFL-------KRYPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 75 DVFVTSKLWNTKHHP--DDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgdtpfprkedgtllyDDIDYKLTWAAmeKLV 152
Cdd:cd19103 75 DYIISTKFTPQIAGQsaDPVADMLEGSLARLGTDYIDIYWIHNP--------------------ADVERWTPELI--PLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 153 GKGLVRAIGLSNFNSRQI---DDILSVASIKptVLQVESHPYL-----AQVELLSHCRDRGLVMTAYSPL------GSPD 218
Cdd:cd19103 133 KSGKVKHVGVSNHNLAEIkraNEILAKAGVS--LSAVQNHYSLlyrssEEAGILDYCKENGITFFAYMVLeqgalsGKYD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 219 RAWKHPDE--------PVL--LEE--PAIAALAKKYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEE 286
Cdd:cd19103 211 TKHPLPEGsgraetynPLLpqLEEltAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDE 290
|
....*..
gi 528482668 287 MSQVTAL 293
Cdd:cd19103 291 IKELEQL 297
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
18-253 |
4.00e-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: 56.41 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGT--WKSEPGLV-----KQAVIWALESGYRHIDCAPIYAN-EPEIGEAFQEtmgpdkgIRREDVFVTSKL-----WN 84
Cdd:cd19090 3 LGLGTagLGGVFGGVdddeaVATIRAALDLGINYIDTAPAYGDsEERLGLALAE-------LPREPLVLSTKVgrlpeDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 85 TKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPrkeDGTLlyddidykltwAAMEKLVGKGLVRAIGLSN 164
Cdd:cd19090 76 ADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP---GGAL-----------EALLELKEEGLIKHIGLGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 165 ---------FNSRQIDDILSVASIkpTVLQVEshpylAQVELLSHCRDRGL-VMTAySPLG----------SPDRAWKHP 224
Cdd:cd19090 142 gppdllrraIETGDFDVVLTANRY--TLLDQS-----AADELLPAAARHGVgVINA-SPLGmgllagrppeRVRYTYRWL 213
|
250 260
....*....|....*....|....*....
gi 528482668 225 DEPVLLEEPAIAALAKKYNKTPAQIIIRW 253
Cdd:cd19090 214 SPELLDRAKRLYELCDEHGVPLPALALRF 242
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-253 |
4.69e-09 |
|
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: 56.41 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTWKSEPGL-----VKQAVIWALESGYRHIDCAPIYAN---EPEIGEAFQetmgPDKGIRredvfVTSK---LWNTK 86
Cdd:cd19075 5 LGTMTFGSQGRFttaeaAAELLDAFLERGHTEIDTARVYPDgtsEELLGELGL----GERGFK-----IDTKanpGVGGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 87 HHPDDVEPSLLKTLKDLKLEYLDLYLIHWPyafqrgD--TPFprkEDgtllyddidyklTWAAMEKLVGKGLVRAIGLSN 164
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAP------DrsTPL---EE------------TLAAIDELYKEGKFKEFGLSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 165 FNSRQIDDILSVAS----IKPTVLQ---------VEShpylaqvELLSHCRDRGLVMTAYSPLG---------------- 215
Cdd:cd19075 135 YSAWEVAEIVEICKengwVLPTVYQgmynaitrqVET-------ELFPCLRKLGIRFYAYSPLAggfltgkykysedkag 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 528482668 216 ----SP---------DRAWKhpdePVLLEepAIA---ALAKKYNKTPAQIIIRW 253
Cdd:cd19075 208 ggrfDPnnalgklyrDRYWK----PSYFE--ALEkveEAAEKEGISLAEAALRW 255
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
106-302 |
1.83e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 55.25 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 106 EYLDLYLIHWPyafQRGDTPFprkedGTLLYDDIDYKLTWAAMEKL------VGKGLVRAIGLSNFNSRQIDDILSVASI 179
Cdd:PRK10625 124 DYLDLYQVHWP---QRPTNCF-----GKLGYSWTDSAPAVSLLETLdalaeqQRAGKIRYIGVSNETAFGVMRYLHLAEK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 180 K--PTVLQVEsHPY----------LAQ------VELLSH-CRDRGLVMTAY----SPLGSPD----RAWKHPDEPVLLEE 232
Cdd:PRK10625 196 HdlPRIVTIQ-NPYsllnrsfevgLAEvsqyegVELLAYsCLAFGTLTGKYlngaKPAGARNtlfsRFTRYSGEQTQKAV 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528482668 233 PAIAALAKKYNKTPAQIIIRWQTQRGVV--TIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIVP 302
Cdd:PRK10625 275 AAYVDIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAVHQVYTYPAP 346
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-292 |
2.73e-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: 54.14 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 38 LESGYRHIDCAPIYAN-EPEIGEaFQETMGPDKGIRREDVFVT------SKLWNTKHHpddVEPSLLKTLKDLKLEYLDL 110
Cdd:cd19101 33 VDAGLTTFDCADIYGPaEELIGE-FRKRLRRERDAADDVQIHTkwvpdpGELTMTRAY---VEAAIDRSLKRLGVDRLDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 111 YLIHWpyafqrgdtpfprkEDgtllYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSvASIKPTVLQVeSHP 190
Cdd:cd19101 109 VQFHW--------------WD----YSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILD-AGVPIVSNQV-QYS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 191 YL---AQVELLSHCRDRGLVMTAYSPLG------------SPDRA-------------------WKHPDEpvLLEepAIA 236
Cdd:cd19101 169 LLdrrPENGMAALCEDHGIKLLAYGTLAggllsekylgvpEPTGPaletrslqkyklmidewggWDLFQE--LLR--TLK 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 237 ALAKKYNKTPAQIIIRW--QTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTA 292
Cdd:cd19101 245 AIADKHGVSIANVAVRWvlDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
11-286 |
2.57e-07 |
|
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: 51.49 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTWK-----SEPGLVKQAVIWALESGYRHIDCAPIYANEP-----EIGEAFQETMGPdkgiRREDVFVTS 80
Cdd:cd19089 7 SGLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYGPPPgsaeeNFGRILKRDLRP----YRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 81 KL-----------WNTKHHpddVEPSLLKTLKDLKLEYLDLYLIHwpyafqRGDTPFPRKEdgtllyddidyklTWAAME 149
Cdd:cd19089 83 KAgygmwpgpygdGGSRKY---LLASLDQSLKRMGLDYVDIFYHH------RYDPDTPLEE-------------TMTALA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 150 KLVGKGLVRAIGLSNFNS---RQIDDILSVASIKPTVLQVESHPYLAQVE--LLSHCRDRGLVMTAYSPL---------- 214
Cdd:cd19089 141 DAVRSGKALYVGISNYPGakaRRAIALLRELGVPLIIHQPRYSLLDRWAEdgLLEVLEEAGIGFIAFSPLaqglltdkyl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 215 -GSPDRAWKHPDEPVLLEEP----------AIAALAKKYNKTPAQIIIRWQTQRGVVTipkS--ITQSR---IKENIQVF 278
Cdd:cd19089 221 nGIPPDSRRAAESKFLTEEAltpekleqlrKLNKIAAKRGQSLAQLALSWVLRDPRVT---SvlIGASSpsqLEDNVAAL 297
|
....*...
gi 528482668 279 DFTLESEE 286
Cdd:cd19089 298 KNLDFSEE 305
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-252 |
4.98e-06 |
|
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: 47.14 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 18 LGLGTW--------KSEPGLVKQAVI-----WALESGYRHIDCAPIYAN-EPEIGEAFqetmgpdkgIRREDVFVTSKLW 83
Cdd:cd19097 3 LALGTAqfgldygiANKSGKPSEKEAkkileYALKAGINTLDTAPAYGDsEKVLGKFL---------KRLDKFKIITKLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 84 NTKHHPDDVEPSLLKTLKDLKL----EYLDLYLIHWPyafqrgdtpfprkedgtllyDDID--YKLTWAAMEKLVGKGLV 157
Cdd:cd19097 74 PLKEDKKEDEAAIEASVEASLKrlkvDSLDGLLLHNP--------------------DDLLkhGGKLVEALLELKKEGLI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 158 RAIGLSNFNSRQIDDILSvaSIKPTVLQV---------ESHPYLAQ-----VELlsHCRD---RGLVMTAYSPLGSPDRA 220
Cdd:cd19097 134 RKIGVSVYSPEELEKALE--SFKIDIIQLpfnildqrfLKSGLLAKlkkkgIEI--HARSvflQGLLLMEPDKLPAKFAP 209
|
250 260 270
....*....|....*....|....*....|..
gi 528482668 221 WKhpdepVLLEepAIAALAKKYNKTPAQIIIR 252
Cdd:cd19097 210 AK-----PLLK--KLHELAKKLGLSPLELALG 234
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
32-216 |
5.26e-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: 44.27 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 32 QAVIW-ALESGYRHIDCAPIYA---NEPEIGEAFQetmgpdkGIRREDVFVTSKL-----WNTKHHPDDVEP-------- 94
Cdd:cd19162 22 AATLDaAWDAGIRYFDTAPLYGlglSERRLGAALA-------RHPRAEYVVSTKVgrllePGAAGRPAGADRrfdfsadg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 95 ---SLLKTLKDLKLEYLDLYLIHWPyafqrgdtpfPRKEDGTLlyDDidyklTWAAMEKLVGKGLVRAIGLSNFNSRQID 171
Cdd:cd19162 95 irrSIEASLERLGLDRLDLVFLHDP----------DRHLLQAL--TD-----AFPALEELRAEGVVGAIGVGVTDWAALL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528482668 172 DILSVASIKpTVLQVESHPYL---AQVELLSHCRDRGLVMTAYSPLGS 216
Cdd:cd19162 158 RAARRADVD-VVMVAGRYTLLdrrAATELLPLCAAKGVAVVAAGVFNS 204
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
154-295 |
6.20e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 43.80 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 154 KGLVRAIGLSNFNSRQIDDILSVASIkptvLQVESHPYLAQV---ELLSHCRDRGLVMTAYSPLG--SPdrawkhpdepv 228
Cdd:PRK10376 156 QGLVRHIGLSNVTPTQVAEARKIAEI----VCVQNHYNLAHRaddALIDALARDGIAYVPFFPLGgfTP----------- 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528482668 229 lLEEPAIAALAKKYNKTPAQIIIRWQTQRG--VVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHR 295
Cdd:PRK10376 221 -LQSSTLSDVAASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIAR 288
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
11-253 |
1.15e-04 |
|
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: 43.35 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTW-----KSEPGLVKQAVIWALESGYRHIDCAPIYAN---EPEIGEAFQETmgpdkGIRREDVFVTSKL 82
Cdd:cd19143 9 SGLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKEL-----GWPRSDYVVSTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 83 -W------------NTKHHPDDVEPSLLKTLKdlklEYLDLYLIHwpyafqRGDTPFPRKEdgtllyddidyklTWAAME 149
Cdd:cd19143 84 fWggggpppndrglSRKHIVEGTKASLKRLQL----DYVDLVFCH------RPDPATPIEE-------------TVRAMN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 150 KLVGKGLVRAIGLSNFNSRQIDDILSVAS----IKPTVLQVES---HPYLAQVELLSHCRDRGLVMTAYSPLGS------ 216
Cdd:cd19143 141 DLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQYnlfHRERVEVEYAPLYEKYGLGTTTWSPLASglltgk 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 528482668 217 ------PDRAWKHPDEPVLLEEP------------AIAALAKKYNKTPAQIIIRW 253
Cdd:cd19143 221 ynngipEGSRLALPGYEWLKDRKeelgqekiekvrKLKPIAEELGCSLAQLAIAW 275
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
38-279 |
2.07e-04 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 42.54 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 38 LESGYRHIDCAPIYAN-------EPEIGEAFQETmgpdkgIRREDVFVTSK--------LWNTKHHPDDVEPSLLKTLKD 102
Cdd:cd19082 27 VELGGNFIDTARVYGDwvergasERVIGEWLKSR------GNRDKVVIATKgghpdledMSRSRLSPEDIRADLEESLER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 103 LKLEYLDLYLIHwpyafqRGDtpfPRKEDGTLLyddidykltwAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASIK-- 180
Cdd:cd19082 101 LGTDYIDLYFLH------RDD---PSVPVGEIV----------DTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHgl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 181 --PTVLQ-------VESHPYLAQV------ELLSHCRDRGLVMTAYSPLGS---PDRAwkHPDEPVLLEEPA-------- 234
Cdd:cd19082 162 pgFAASSpqwslarPNEPPWPGPTlvamdeEMRAWHEENQLPVFAYSSQARgffSKRA--AGGAEDDSELRRvyyseenf 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 528482668 235 -----IAALAKKYNKTPAQIIIRWQTQRGVVTIP----KSITQsrIKENIQVFD 279
Cdd:cd19082 240 erlerAKELAEEKGVSPTQIALAYVLNQPFPTVPiigpRTPEQ--LRDSLAAAD 291
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
11-215 |
6.24e-04 |
|
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: 41.18 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTWKSEPG-----LVKQAVIWALESGYRHIDCAPIYANEPeiGEAFQETMGPDKGIRREDVFVTSKLW-- 83
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGqisdeVAERLMTIAYESGVNLFDTAEVYAAGK--AEVILGSIIKKKGWRRSSLVITTKLYwg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 84 ---------NTKHHPDDVEPSllktLKDLKLEYLDLYLIHWPyafqrgDTPFPRKEdgtllyddidyklTWAAMEKLVGK 154
Cdd:cd19159 87 gkaeterglSRKHIIEGLKGS----LQRLQLEYVDVVFANRP------DSNTPMEE-------------IVRAMTHVINQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 155 GLVRAIGLSNFNSRQIDDILSVAS----IKPTVLQVESHPYL---AQVELLSHCRDRGLVMTAYSPLG 215
Cdd:cd19159 144 GMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQrekVEVQLPELYHKIGVGAMTWSPLA 211
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
37-279 |
1.19e-03 |
|
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: 40.21 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 37 ALESGYRHIDCAPIYANEPE---IGEAFQETMGPdkgirREDVFVTSKLWNTK-----HHPDDVEPSLLKTLKDLKLEYL 108
Cdd:cd19153 42 AFAAGINHFDTSPYYGAESSeavLGKALAALQVP-----RSSYTVATKVGRYRdsefdYSAERVRASVATSLERLHTTYL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 109 DLYLIHwpyafqrgDTPFprkedgtlLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASIKPT-VLQVE 187
Cdd:cd19153 117 DVVYLH--------DIEF--------VDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSLdAVLSY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 188 SHPYLAQVELLS----HCRDRGLVMTAYSPLG------SPDRAWkHPDEPVLLEEPAIA-ALAKKYNKTPAQIIIRWQ-- 254
Cdd:cd19153 181 CHLTLQDARLESdapgLVRGAGPHVINASPLSmglltsQGPPPW-HPASGELRHYAAAAdAVCASVEASLPDLALQYSla 259
|
250 260
....*....|....*....|....*...
gi 528482668 255 TQRGVVTI---PKSITQsrIKENIQVFD 279
Cdd:cd19153 260 AHAGVGTVllgPSSLAQ--LRSMLAAVD 285
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
11-214 |
1.57e-03 |
|
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: 39.75 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTWKS-EPGLVKQA----VIWALESGYRHIDCAPIYAN---EPEIGEAFQEtmgpdKGIRREDVFVTSKL 82
Cdd:cd19142 9 SGLRVSNVGLGTWSTfSTAISEEQaeeiVTLAYENGINYFDTSDAFTSgqaETELGRILKK-----KGWKRSSYIVSTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 83 -WNT---------KHHPDDVEPSLLKTLKdlklEYLDLYLIHwpyafqRGDTPFPRKEdgtllyddidyklTWAAMEKLV 152
Cdd:cd19142 84 yWSYgseerglsrKHIIESVRASLRRLQL----DYIDIVIIH------KADPMCPMEE-------------VVRAMSYLI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528482668 153 GKGLVRAIGLSNFNSRQIDDILSVAS----IKPTVLQVESHPYlaqvellshCRDR------------GLVMTAYSPL 214
Cdd:cd19142 141 DNGLIMYWGTSRWSPVEIMEAFSIARqfncPTPICEQSEYHMF---------CREKmelympelynkvGVGLITWSPL 209
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
11-215 |
3.30e-03 |
|
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: 38.91 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTWKSEPG-----LVKQAVIWALESGYRHIDCAPIYANEPeiGEAFQETMGPDKGIRREDVFVTSKL-WN 84
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGqitdeMAEHLMTLAYDNGINLFDTAEVYAAGK--AEVVLGNIIKKKGWRRSSLVITTKIfWG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 85 TKHHPD-DVEPSLLKTLKDLKLEYLDLYLIHWPYAfQRGDTPFPRKEdgtllyddidyklTWAAMEKLVGKGLVRAIGLS 163
Cdd:cd19158 87 GKAETErGLSRKHIIEGLKASLERLQLEYVDVVFA-NRPDPNTPMEE-------------TVRAMTHVINQGMAMYWGTS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528482668 164 NFNSRQIDDILSVAS----IKPTVLQVESHPYL---AQVELLSHCRDRGLVMTAYSPLG 215
Cdd:cd19158 153 RWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQrekVEVQLPELFHKIGVGAMTWSPLA 211
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
11-288 |
3.83e-03 |
|
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: 38.59 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGTWKS----EPGLVKQAVIW-ALESGYRHIDCAPIYANEPEIGE-AFQETMGPDKGIRREDVFVTSKL-- 82
Cdd:cd19150 8 SGLKLPALSLGLWHNfgddTPLETQRAILRtAFDLGITHFDLANNYGPPPGSAEeNFGRILREDFAGYRDELIISTKAgy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 83 ---------WNTKHHpddVEPSLLKTLKDLKLEYLDLYLIHwpyafqRGDTPFPRKEdgtllyddidyklTWAAMEKLVG 153
Cdd:cd19150 88 dmwpgpygeWGSRKY---LLASLDQSLKRMGLDYVDIFYSH------RFDPDTPLEE-------------TMGALDHAVR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 154 KGLVRAIGLSNFNS---RQIDDILSVASIkPTVLQVESHPYL----AQVELLSHCRDRGLVMTAYSPL-----------G 215
Cdd:cd19150 146 SGKALYVGISSYSPertREAAAILRELGT-PLLIHQPSYNMLnrwvEESGLLDTLQELGVGCIAFTPLaqglltdkylnG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 216 SPD--RAWK-HPDEPVLLEEPAIA------ALAKKYNKTPAQIIIRWQTQRGVVTiPKSITQSR---IKENIQVFD-FTL 282
Cdd:cd19150 225 IPEgsRASKeRSLSPKMLTEANLNsiralnEIAQKRGQSLAQMALAWVLRDGRVT-SALIGASRpeqLEENVGALDnLTF 303
|
....*.
gi 528482668 283 ESEEMS 288
Cdd:cd19150 304 SADELA 309
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
11-288 |
6.73e-03 |
|
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: 37.53 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 11 TGRKMPLLGLGT--WKSEPGLVK-----QAVIWALESGYRHIDCAPIYAN---EPEIGEAFqetmgpdKGIRREDVFVTS 80
Cdd:cd19163 9 TGLKVSKLGFGAspLGGVFGPVDeeeaiRTVHEALDSGINYIDTAPWYGQgrsETVLGKAL-------KGIPRDSYYLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 81 KLWNTKHHPDD--------VEPSLLKTLKDLKLEYLDLYLIHwpyafqrgDTPFPrkedgtllyDDIDYKL--TWAAMEK 150
Cdd:cd19163 82 KVGRYGLDPDKmfdfsaerITKSVEESLKRLGLDYIDIIQVH--------DIEFA---------PSLDQILneTLPALQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 151 LVGKGLVRAIGLSNFNsrqIDDILSVASIKPTVLQVeshpylaqveLLSHCR----------------DRGL-VMTAySP 213
Cdd:cd19163 145 LKEEGKVRFIGITGYP---LDVLKEVLERSPVKIDT----------VLSYCHytlndtsllellpffkEKGVgVINA-SP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528482668 214 L--------GSPDraWkHPDEPVLLEE-PAIAALAKKYNKTPAQIIIRW--QTQRGVVTIPKSITQSRIKENIQVFDFTL 282
Cdd:cd19163 211 LsmgllterGPPD--W-HPASPEIKEAcAKAAAYCKSRGVDISKLALQFalSNPDIATTLVGTASPENLRKNLEAAEEPL 287
|
....*.
gi 528482668 283 ESEEMS 288
Cdd:cd19163 288 DAHLLA 293
|
|
| |
