|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
7-301 |
2.26e-137 |
|
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: 390.98 E-value: 2.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 7 LNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGK-VKREELFITSKVWNTFHS 85
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 86 EAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFTHS 165
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 166 QIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAfFRKDGDPNVLTNEVVAGIAKAHGKTPA 245
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRP-WAKPDEPVLLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17537075 246 QIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVDPS 301
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVPM 295
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-289 |
3.20e-127 |
|
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: 363.34 E-value: 3.20e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 13 IPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILdegkVKREELFITSKVWNTFHSEAKAHEN 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 93 IDIILSDLQLSYVDLMLIHWPQGyaegaelfpagenGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWD 172
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVP-------------GKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 173 AAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAffrkdgdpnVLTNEVVAGIAKAHGKTPAQIILRWF 252
Cdd:cd19071 144 AARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP---------LLDDPVLKEIAKKYGKTPAQVLLRWA 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 17537075 253 VDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19071 215 LQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-300 |
7.44e-127 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 362.45 E-value: 7.44e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 9 SGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTFHSEAK 88
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA----SGVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 89 AHENIDIILSDLQLSYVDLMLIHWPqgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQ 168
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWP--------------------GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 169 RVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGsaffrkdgdpnVLTNEVVAGIAKAHGKTPAQII 248
Cdd:COG0656 137 ELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKTPAQVV 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17537075 249 LRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRL-VDP 300
Cdd:COG0656 206 LRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLgPDP 258
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
4-298 |
6.57e-125 |
|
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: 358.90 E-value: 6.57e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 4 SLKLNSGYSIPAIGLGTWQSKPGE-VAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNT 82
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDEgVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 83 FHSEAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAElfpAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNF 162
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENND---SESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 163 THSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFFrkDGDPNVLTNEVVAGIAKAHGK 242
Cdd:cd19116 159 NSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQ--TNPPPRLDDPTLVAIAKKYGK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17537075 243 TPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLV 298
Cdd:cd19116 237 TTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-297 |
1.14e-121 |
|
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: 351.33 E-value: 1.14e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 2 VQSLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWN 81
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 82 TFHSEAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSN 161
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 162 FTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFFRKDGD----PNVLTNEVVAGIA 237
Cdd:cd19154 161 FNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTGvspaPNLLQDPIVKAIA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 238 KAHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRL 297
Cdd:cd19154 241 EKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
10-316 |
2.23e-119 |
|
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: 345.56 E-value: 2.23e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 10 GYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTFHSEAKA 89
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 90 HENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQR 169
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 170 VWD--AAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAfFRKDGDPNVLTNEVVAGIAKAHGKTPAQI 247
Cdd:cd19107 161 ILNkpGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRP-WAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537075 248 ILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRlVDPSPRDGDHKYFGFNEEF 316
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR-ACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
3-291 |
8.48e-116 |
|
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: 335.85 E-value: 8.48e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 3 QSLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNT 82
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 83 FHSEAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGEngkmrYSDVDYLETWKAFEAAQKAGKCRSIGLSNF 162
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEE-----VLPPDIPSTWKAMEKLVDSGKVRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 163 THSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFFRkdgdPNVLTNEVVAGIAKAHGK 242
Cdd:cd19125 156 SVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVK----KNVLKDPIVTKVAEKLGK 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17537075 243 TPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGV 291
Cdd:cd19125 232 TPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
2-298 |
1.55e-114 |
|
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: 332.84 E-value: 1.55e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 2 VQSLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWN 81
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 82 TFHSEAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAeLFPAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSN 161
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGV-GFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 162 FTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPG-SAFFRKDGDPNVLTNEVVAGIAKAH 240
Cdd:cd19123 160 FSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrPAAMKAEGEPVLLEDPVINKIAEKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17537075 241 GKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLV 298
Cdd:cd19123 240 GASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-289 |
1.46e-106 |
|
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: 312.04 E-value: 1.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 7 LNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDE-GKVKREELFITSKVWNTFHS 85
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 86 EAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAE---LFPAGENGKMRYSD--VDYLETWKAFEAAQKAGKCRSIGLS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDlnpLTAVPTNGGEVDLDlsVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 161 NFTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSaffrkdGDPNVLTNEVVAGIAKAH 240
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLA------GLPLLVQHPEVKAIAAKL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17537075 241 GKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISviDFQLSAEEIQAID 289
Cdd:cd19118 235 GKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVT 281
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-299 |
1.07e-102 |
|
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: 302.49 E-value: 1.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 10 GYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTFHSEAKA 89
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 90 HENIDIILSDLQLSYVDLMLIHWPQGYAEgaelfpAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQR 169
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVN------KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 170 VWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFFRKDGD-PNVLTNEVVAGIAKAHGKTPAQII 248
Cdd:cd19111 155 ILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSLWPDqPDLLEDPTVLAIAKELDKTPAQVL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17537075 249 LRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVD 299
Cdd:cd19111 235 LRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFD 285
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
3-296 |
5.98e-102 |
|
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: 301.07 E-value: 5.98e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 3 QSLKLNSGYSIPAIGLGTWqsKPGEVAAAIKTAVA-----AGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITS 77
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTY--APEEVPKSKALEATklaidAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 78 KVWNTFHSEAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSI 157
Cdd:cd19108 79 KLWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 158 GLSNFTHSQIQRVWD--AAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLgnpGSAFFRKDGDPN--VLTNE-V 232
Cdd:cd19108 159 GVSNFNRRQLEMILNkpGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSAL---GSQRDKEWVDQNspVLLEDpV 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537075 233 VAGIAKAHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWR 296
Cdd:cd19108 236 LCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
10-299 |
3.17e-100 |
|
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: 297.10 E-value: 3.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 10 GYSIPAIGLGTWQSK----PGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTFHS 85
Cdd:cd19109 1 GNSIPIIGLGTYSEPkttpKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 86 EAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFTHS 165
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 166 QIQRVWD--AAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFFRKDGDPNVLTNEVVAGIAKAHGKT 243
Cdd:cd19109 161 QLELILNkpGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17537075 244 PAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVD 299
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVE 296
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-291 |
9.14e-100 |
|
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: 294.15 E-value: 9.14e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 13 IPAIGLGTWQSKPGE-VAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTFHSEAKAHE 91
Cdd:cd19136 1 MPILGLGTFRLRGEEeVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 92 NIDIILSDLQLSYVDLMLIHWPqgyaeGAELFPAG--ENGKMRysdvdyLETWKAFEAAQKAGKCRSIGLSNFTHSQIQR 169
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWP-----GVQGLKPSdpRNAELR------RESWRALEDLYKEGKLRAIGVSNYTVRHLEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 170 VWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNpgsaffrkdGDPNVLTNEVVAGIAKAHGKTPAQIIL 249
Cdd:cd19136 150 LLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS---------GDLRLLEDPTVLAIAKKYGRTPAQVLL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17537075 250 RWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGV 291
Cdd:cd19136 221 RWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
4-292 |
2.10e-97 |
|
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: 287.73 E-value: 2.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 4 SLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTF 83
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA----SGVPREELFITTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSEAKAHENIDIILSDLQLSYVDLMLIHWPQgyaegaelfPAgeNGKmrysdvdYLETWKAFEAAQKAGKCRSIGLSNFT 163
Cdd:cd19131 77 QGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---------PA--QDK-------YVETWKALIELKKEGRVKSIGVSNFT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 164 HSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGsaffrkdgdpnVLTNEVVAGIAKAHGKT 243
Cdd:cd19131 139 IEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEKHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17537075 244 PAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVN 292
Cdd:cd19131 208 PAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-299 |
7.76e-96 |
|
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: 285.57 E-value: 7.76e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 4 SLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTF 83
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSEAKAHENIDIILSDLQLSYVDLMLIHWPQGY-AEGAELFPAGENGKMRYS-DVDYLETWKAFEAAQKAGKCRSIGLSN 161
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSlSKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 162 FTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFFRKD-GDP-----NVLTNEVVAG 235
Cdd:cd19155 163 FNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPGtGSPsgsspDLLQDPVVKA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537075 236 IAKAHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVD 299
Cdd:cd19155 243 IAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGRT 306
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
13-316 |
4.60e-94 |
|
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: 281.08 E-value: 4.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 13 IPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTFHSEAKAHEN 92
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 93 IDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWD 172
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 173 AA--EVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFfrkdgdpNVLTNEVVAGIAKAHGKTPAQIILR 250
Cdd:cd19110 164 KPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGV-------DLIDDPVIQRIAKKHGKSPAQILIR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17537075 251 WFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVdPSPRDGDHKYFGFNEEF 316
Cdd:cd19110 237 FQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLA-TFPITENHKDYPFHIEY 301
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-292 |
1.78e-93 |
|
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: 277.92 E-value: 1.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 5 LKLNSGYSIPAIGLGTWQ-SKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTF 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK----SGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSEAKAHENIDIILSDLQLSYVDLMLIHWPQGyaegaelfpagengkmrysdvDYLETWKAFEAAQKAGKCRSIGLSNFT 163
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVSNFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 164 HSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGnpgsaffrkDGDPNVLTNEVVAGIAKAHGKT 243
Cdd:cd19133 136 PDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFA---------EGRNNLFENPVLTEIAEKYGKS 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17537075 244 PAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVN 292
Cdd:cd19133 207 VAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
3-300 |
2.89e-93 |
|
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: 279.33 E-value: 2.89e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 3 QSLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNT 82
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 83 FHSEAKAHENIDIILSDLQLSYVDLMLIHWP---------QGYAEGaelFPAGENGKMRYSDVDYLETWKAFEAAQKAGK 153
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieEKYPPG---FYCGDGDNFVYEDVPILDTWKALEKLVDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 154 CRSIGLSNFTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGnPGSaFFRKDGD-----PNVL 228
Cdd:cd19113 158 IKSIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFG-PQS-FVELNQGralntPTLF 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17537075 229 TNEVVAGIAKAHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVDP 300
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFNDP 307
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
4-289 |
4.50e-93 |
|
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: 277.88 E-value: 4.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 4 SLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGkVKREELFITSKVWNTF 83
Cdd:cd19121 3 SFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWSTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSeaKAHENIDIILSDLQLSYVDLMLIHWPQGY-AEGA-ELFPAGENGKMRYS-DVDYLETWKAFEAAQKAGKCRSIGLS 160
Cdd:cd19121 82 HR--RVELCLDRSLKSLGLDYVDLYLVHWPVLLnPNGNhDLFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 161 NFTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFFRKDGdpnvltnevVAGIAKAH 240
Cdd:cd19121 160 NYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEP---------VVEIAKKH 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17537075 241 GKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFqlSAEEIQAID 289
Cdd:cd19121 231 NVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLN 277
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
3-293 |
5.28e-90 |
|
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: 270.14 E-value: 5.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 3 QSLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKeilDEGkVKREELFITSKVWNT 82
Cdd:cd19117 4 KTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSG-VPREEIFITTKLWCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 83 FHSEAKahENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMR--YSDVDYLETWKAFEAAQKAGKCRSIGLS 160
Cdd:cd19117 80 WHRRVE--EALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKdhEPDWDFIKTWELMQKLPATGKVKAIGVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 161 NFTHSQIQRVWDA--AEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAffrkdgdpnVLTNEVVAGIAK 238
Cdd:cd19117 158 NFSIKNLEKLLASpsAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP---------LLKEPVIIKIAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17537075 239 AHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVidFQLSAEEIQAIDGVNR 293
Cdd:cd19117 229 KHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-309 |
1.77e-89 |
|
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: 269.74 E-value: 1.77e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 4 SLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTF 83
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HS---EAKAHEnidiiLSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYSDVD----YLETWKAFEAAQKAGKCRS 156
Cdd:cd19112 82 HGhviEACKDS-----LKKLQLDYLDLYLVHFPVATKHTGVGTTGSALGEDGVLDIDvtisLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 157 IGLSNFTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNpGSAFFRKDGDPNVLTNEVVAGI 236
Cdd:cd19112 157 IGISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGG-AAANAEWFGSVSPLDDPVLKDL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17537075 237 AKAHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVDPSPRDGDHKY 309
Cdd:cd19112 236 AKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPAKFWGIDLY 308
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
7-293 |
7.36e-89 |
|
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: 266.06 E-value: 7.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 7 LNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTFHSE 86
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 87 AKAHENIDIILSDLQLSYVDLMLIHWPQgyaegaelfPagENGKmrysdvdYLETWKAFEAAQKAGKCRSIGLSNFTHSQ 166
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWPN---------P--SRDL-------YVEAWQALIEAREEGLVRSIGVSNFLPEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 167 IQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGnpgsaffRKDGdpnVLTNEVVAGIAKAHGKTPAQ 246
Cdd:cd19132 139 LDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG-------RGSG---LLDEPVIKAIAEKHGKTPAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17537075 247 IILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNR 293
Cdd:cd19132 209 VVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-292 |
8.91e-89 |
|
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: 266.19 E-value: 8.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 5 LKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTFH 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRR----SGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 85 SEAKAHENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagengKMRYSDVdyLETWKAFEAAQKAGKCRSIGLSNFTH 164
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPV---------------PNDFDRT--IQAYKALEKLLAEGRVRAIGVSNFTP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 165 SQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGnpGSAFFRKDGDP---NVLTNEVVAGIAKAHG 241
Cdd:cd19127 140 EHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIG--GVMRYGASGPTgpgDVLQDPTITGLAEKYG 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17537075 242 KTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVN 292
Cdd:cd19127 218 KTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-302 |
2.39e-87 |
|
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: 262.71 E-value: 2.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 4 SLKLNSGYSIPAIGLGTWQSKPG-EVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNT 82
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGsEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 83 FHSEAKAHENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpageNGKmrysdvdYLETWKAFEAAQKAGKCRSIGLSNF 162
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWPV-------------KGK-------YKETWKALEKLYKDGRVRAIGVSNF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 163 THSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPgsaffrkdgdpNVLTNEVVAGIAKAHGK 242
Cdd:cd19157 137 QVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQG-----------QLLDNPVLKEIAEKYNK 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 243 TPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRlVDPSP 302
Cdd:cd19157 206 SVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLR-VGPDP 264
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-289 |
2.93e-86 |
|
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: 260.89 E-value: 2.93e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 4 SLKLNSGYSIPAIGLGTW--QSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWN 81
Cdd:cd19119 3 SFKLNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 82 TFHSEAKahENIDIILSDLQLSYVDLMLIHWPQGYA-----EGAELFPAGENGKMRYS-DVDYLETWKAFEAAQKAGKCR 155
Cdd:cd19119 83 TFYDEVE--RSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAaSGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 156 SIGLSNFTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAffrkdgdpnVLTNEVVAG 235
Cdd:cd19119 161 AIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPLVKK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17537075 236 IAKAHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIdfQLSAEEIQAID 289
Cdd:cd19119 232 IAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIV--SLTKEDLQKLD 283
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-291 |
8.80e-86 |
|
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: 259.12 E-value: 8.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 9 SGYSIPAIGLGT--WQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVK-REELFITSKVWNtfhS 85
Cdd:cd19124 1 SGQTMPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWC---S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 86 EAKAHeniDII------LSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYsdvDYLETWKAFEAAQKAGKCRSIGL 159
Cdd:cd19124 78 DAHPD---LVLpalkksLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPF---DIKGVWEAMEECQRLGLTKAIGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 160 SNFTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFfrkdGDPNVLTNEVVAGIAKA 239
Cdd:cd19124 152 SNFSCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKW----GSNAVMESDVLKEIAAA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17537075 240 HGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGV 291
Cdd:cd19124 228 KGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-290 |
3.54e-85 |
|
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: 256.42 E-value: 3.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 10 GYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEIldegKVKREELFITSKVWNTFHSEAKA 89
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAAS----GVPRDELFLTTKVWPDNYSPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 90 HENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQR 169
Cdd:cd19140 81 LASVEESLRKLRTDYVDLLLLHWPN-------------------KDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 170 VWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGnpgsaffrkDGDpnVLTNEVVAGIAKAHGKTPAQIIL 249
Cdd:cd19140 142 AVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA---------RGE--VLKDPVLQEIGRKHGKTPAQVAL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17537075 250 RWFVD-SGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDG 290
Cdd:cd19140 211 RWLLQqEGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-300 |
8.56e-85 |
|
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: 257.73 E-value: 8.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 1 MVQSLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVW 80
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 81 NTFHSEAKAHENIDIILSDLQLSYVDLMLIHWP--QGYAEGAELFPAG---ENGKMRYSDVDYLETWKAFEAAQKAGKCR 155
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPiaLKYVDPAVRYPPGwfyDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 156 SIGLSNFTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGnPGS----AFFRKDGDPNVLTNE 231
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PQSflelDLPGAKDTPPLFEHD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537075 232 VVAGIAKAHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVDP 300
Cdd:cd19115 240 VIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFNNP 308
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-292 |
1.21e-82 |
|
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: 250.05 E-value: 1.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 5 LKLNSGYSIPAIGLGTWQSKPG-EVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTF 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSEAKAHENIDIILSDLQLSYVDLMLIHWPqgyaegaelfpagenGKMRYSDvdyleTWKAFEAAQKAGKCRSIGLSNFT 163
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWP---------------GKDKFID-----TWKALEKLYASGKVKAIGVSNFQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 164 HSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGsaffrkdgdpnVLTNEVVAGIAKAHGKT 243
Cdd:cd19126 137 EHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGEKYGKS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17537075 244 PAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVN 292
Cdd:cd19126 206 AAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-294 |
4.46e-82 |
|
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: 250.07 E-value: 4.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTFHSEA 87
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 88 KAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYSD-VDYLETWKAFEAAQKAGKCRSIGLSNFTHSQ 166
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 167 IQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNpgsaffrkDGDPNVLTNEVVAGIAKAHGKTPAQ 246
Cdd:cd19129 161 LREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGH--------GMEPKLLEDPVITAIARRVNKTPAQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17537075 247 IILRWFVDSGLSAIPKSVTPQRIIENisvidFQLSAEEIQAIDGVNRG 294
Cdd:cd19129 233 VLLAWAIQRGTALLTTSKTPSRIREN-----FDISTLPEDAMREINEG 275
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-289 |
1.31e-81 |
|
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: 247.18 E-value: 1.31e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 13 IPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEIldegKVKREELFITSKVWNTFHSEAKAHEN 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 93 IDIILSDLQLSYVDLMLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWD 172
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN-------------------PTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 173 AAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNpgsaffrkdgdPNVLTNEVVAGIAKAHGKTPAQIILRWF 252
Cdd:cd19073 138 ISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLAR-----------GEVLRDPVIQEIAEKYDKTPAQVALRWL 206
|
250 260 270
....*....|....*....|....*....|....*..
gi 17537075 253 VDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19073 207 VQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
5-300 |
4.93e-80 |
|
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: 243.96 E-value: 4.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 5 LKLNSGYSIPAIGLGTWQSKPG-EVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTF 83
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGaEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE----SGVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSEAKAHENIDIILSDLQLSYVDLMLIHWPQGyaegaelfpagenGKmrysdvdYLETWKAFEAAQKAGKCRSIGLSNFT 163
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPVK-------------GK-------FKDTWKAFEKLYKEKKVRAIGVSNFH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 164 HSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNpgsaffrkdgdPNVLTNEVVAGIAKAHGKT 243
Cdd:cd19156 137 EHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQ-----------GKLLSNPVLKAIGKKYGKS 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17537075 244 PAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRL-VDP 300
Cdd:cd19156 206 AAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRYgPDP 263
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-288 |
2.48e-78 |
|
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: 240.12 E-value: 2.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 14 PAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTFHSEAKAHENI 93
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 94 DIILSDLQLSYVDLMLIHWPQGYAEGAELFPAGENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDA 173
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 174 AEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGnpGSaffRKDGDPNVLTNEVVAGIAKAHGKTPAQIILRWFV 253
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLG--GS---YGDGNLTFLNDSELKALATKYNTTPPQVIIAWHL 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 17537075 254 D---SGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAI 288
Cdd:cd19128 237 QkwpKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
5-302 |
6.37e-75 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 231.11 E-value: 6.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 5 LKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEIldegKVKREELFITSKVWNTFH 84
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA----SVAREELFITTKLWNDDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 85 SEAKA--HENidiiLSDLQLSYVDLMLIHWPqgyaegaelFPAGENgkmrysdvdYLETWKAFEAAQKAGKCRSIGLSNF 162
Cdd:PRK11565 83 KRPREalEES----LKKLQLDYVDLYLMHWP---------VPAIDH---------YVEAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 163 THSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSaffrkdgdpNVLTNEVVAGIAKAHGK 242
Cdd:PRK11565 141 QIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK---------GVFDQKVIRDLADKYGK 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 243 TPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLvDPSP 302
Cdd:PRK11565 212 TPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKRL-GPDP 270
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-289 |
1.80e-73 |
|
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: 227.12 E-value: 1.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 10 GYSIPAIGLGT----WQSKPGEVAAAIKTAVAA----GYRHIDCAHVYQNQKEVGEALKEILdegkVKREELFITSKVWN 81
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLVDSVKLalkaGFRHIDTAEMYGNEKEVGEALKESG----VPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 82 TFHSEAKAhenIDIILSDLQLSYVDLMLIHWPqgyaegaelFPAGENGKmrysdvDYLETWKAFEAAQKAGKCRSIGLSN 161
Cdd:cd19120 77 GIKDPREA---LRKSLAKLGVDYVDLYLIHSP---------FFAKEGGP------TLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 162 FTHSQIQRVWDAAEVKPACLQVELHPYFT--QVKLREFCKEKGIVVVGYSPLgnpgSAFFRKDGDPnvlTNEVVAGIAKA 239
Cdd:cd19120 139 FRIEDLEELLDTAKIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPL----SPLTRDAGGP---LDPVLEKIAEK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17537075 240 HGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19120 212 YGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-300 |
5.71e-72 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 224.74 E-value: 5.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 10 GYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEGKVKREELFITSKVWNTFHSEAKA 89
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 90 HENIDIILSDLQLSYVDLMLIHWP--QGYAEGAELFPAG----ENGKMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFT 163
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPipAAYVDPAENYPFLwkdkELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 164 HSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAFFRKDGD--PNVLTNEVVAGIAKAHG 241
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKhfTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 17537075 242 KTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVDP 300
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDP 299
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
5-290 |
2.92e-71 |
|
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: 221.43 E-value: 2.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 5 LKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTFH 84
Cdd:cd19135 5 VRLSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIKE----SGVPREDLFLTTKLWPSDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 85 SEAKAHENIDIILSDLQLSYVDLMLIHWPQGyaegaelfPAGENGKMRYSDvdylETWKAFEAAQKAGKCRSIGLSNFTH 164
Cdd:cd19135 81 GYESTKQAFEASLKRLGVDYLDLYLLHWPDC--------PSSGKNVKETRA----ETWRALEELYDEGLCRAIGVSNFLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 165 SQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLgNPGSAFfrkdGDPNVLTnevvagIAKAHGKTP 244
Cdd:cd19135 149 EHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-AKGKAL----EEPTVTE------LAKKYQKTP 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17537075 245 AQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDG 290
Cdd:cd19135 218 AQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDS 263
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
4-292 |
3.30e-71 |
|
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: 221.32 E-value: 3.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 4 SLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTF 83
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAA----SGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSEAKAHENIDIILSDLQLSYVDLMLIHWPqgyaegaelFPAGENgkmrysdvdYLETWKAFEAAQKAGKCRSIGLSNFT 163
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWP---------TPAAGN---------YVHTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 164 HSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNpGSAFfrkdGDPnvltneVVAGIAKAHGKT 243
Cdd:cd19130 139 PPHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQ-GKLL----GDP------PVGAIAAAHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17537075 244 PAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVN 292
Cdd:cd19130 208 PAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-297 |
1.54e-67 |
|
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: 212.02 E-value: 1.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 4 SLKLNSGYSIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTF 83
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAA----SGIPRGELFVTTKLATPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSEAKAHENIDIILSDLQLSYVDLMLIHWPqgyaegaelfpAGENGKmrysdvdYLETWKAFEAAQKAGKCRSIGLSNFT 163
Cdd:cd19134 78 QGFTASQAACRASLERLGLDYVDLYLIHWP-----------AGREGK-------YVDSWGGLMKLREEGLARSIGVSNFT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 164 HSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNpGSAffrkdgdpnvLTNEVVAGIAKAHGKT 243
Cdd:cd19134 140 AEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGV-GRL----------LDNPAVTAIAAAHGRT 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17537075 244 PAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRL 297
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-289 |
6.96e-63 |
|
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: 199.50 E-value: 6.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 13 IPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTFHSEAKAHEN 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 93 IDIILSDLQLSYVDLMLIHWPQGYAEgaelFPAGEngkmrysdvdYLEtwkAFEAAQKAGKCRSIGLSNFTHSQIQRVWD 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPSPNDE----VPVEE----------YIG---ALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 173 A-AEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPgsaffrkdgdpNVLTNEVVAGIAKAHGKTPAQIILRW 251
Cdd:cd19139 140 VvGAGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYG-----------KVLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270
....*....|....*....|....*....|....*...
gi 17537075 252 FVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIA 246
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
6-291 |
7.64e-62 |
|
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: 198.23 E-value: 7.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 6 KLNSGYSIPAIGLGTWQSK--PGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEILDEG-KVKREELFITSKVWNT 82
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 83 FHSEAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPA-GENGKmrYSDVDYLE-----TWKAFEAAQKAGKCRS 156
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGK--YVILKDLTenpepTWRAMEEIYESGKAKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 157 IGLSNFTHSQIQRVWDAAEVKPACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLGNPGSAffrKDGDPNVLTNEVVAGI 236
Cdd:cd19122 160 IGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQV---PSTGERVSENPTLNEV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17537075 237 AKAHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDfqLSAEEIQAIDGV 291
Cdd:cd19122 237 AEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQV 289
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-300 |
8.48e-61 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 194.86 E-value: 8.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 12 SIPAIGLGTWQSKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKEVGEALKEildeGKVKREELFITSKVWNTFHSEAKAHE 91
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 92 NIDIILSDLQLSYVDLMLIHWPqgyaegaelfpAGENGkmrysdVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVW 171
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWP-----------SPNDE------VSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 172 DAAEVKP-ACLQVELHPYFTQVKLREFCKEKGIVVVGYSPLgnpgsAFFRkdgdpnVLTNEVVAGIAKAHGKTPAQIILR 250
Cdd:PRK11172 141 AAVGAENiATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTL-----AYGK------VLKDPVIARIAAKHNATPAQVILA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17537075 251 WFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVNRGWRLVDP 300
Cdd:PRK11172 210 WAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSP 259
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-292 |
4.32e-60 |
|
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: 193.68 E-value: 4.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 16 IGLGTWQSKPG-------EVAAAIKTAVAAGYRHIDCAHVY---QNQKEVGEALKEIldegKVKREELFITSKV------ 79
Cdd:pfam00248 1 IGLGTWQLGGGwgpiskeEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 80 WNTFHSEAKAHENIDIILSDLQLSYVDLMLIHWPqgyaegaelFPagengkmrysDVDYLETWKAFEAAQKAGKCRSIGL 159
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP---------DP----------DTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 160 SNFTHSQIQRVWDAAEVKPACLQVELHPYFTQV--KLREFCKEKGIVVVGYSPLGNPG-SAFFRKDGDP----------- 225
Cdd:pfam00248 138 SNFDAEQIEKALTKGKIPIVAVQVEYNLLRRRQeeELLEYCKKNGIPLIAYSPLGGGLlTGKYTRDPDKgpgerrrllkk 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17537075 226 ----NVLTNEVVAGIAKAHGKTPAQIILRWFVDS--GLSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGVN 292
Cdd:pfam00248 218 gtplNLEALEALEEIAKEHGVSPAQVALRWALSKpgVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-289 |
1.79e-53 |
|
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: 175.88 E-value: 1.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 10 GYSIPAIGLGTW---------QSKPGEVAAAIKTAVAAGYRHIDCAHVYQN---QKEVGEALKeildegKVKREELFITS 77
Cdd:cd19072 1 GEEVPVLGLGTWgigggmskdYSDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 78 KVWNTFHSEAKAHENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSI 157
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPN-------------------PSIPIEETLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 158 GLSNFTHSQIQRVWDAAE-VKPACLQVELHPYFTQV--KLREFCKEKGIVVVGYSPLGNpGSAFFRKdgdpnvlTNEVVA 234
Cdd:cd19072 136 GVSNFSLEELEEAQSYLKkGPIVANQVEYNLFDREEesGLLPYCQKNGIAIIAYSPLEK-GKLSNAK-------GSPLLD 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17537075 235 GIAKAHGKTPAQIILRWFV-DSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19072 208 EIAKKYGKTPAQIALNWLIsKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-289 |
4.21e-47 |
|
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: 159.34 E-value: 4.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 5 LKLNSGYSIPAIGLGTWQ-----SKPGEVAAAIKTAVAAGYRHIDCAHVYQN---QKEVGEALKEIldegkvkREELFIT 76
Cdd:cd19138 3 VTLPDGTKVPALGQGTWYmgedpAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 77 SKVWNTFHSEAKAHENIDIILSDLQLSYVDLMLIHWPqgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRS 156
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR--------------------GGVPLAETVAAMEELKKEGKIRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 157 IGLSNFTHSQIQRVWDAAEVKP-ACLQVELHpyftqVKLR--EF-----CKEKGIVVVGYSPLGNPGSAffrkdgDPNVL 228
Cdd:cd19138 136 WGVSNFDTDDMEELWAVPGGGNcAANQVLYN-----LGSRgiEYdllpwCREHGVPVMAYSPLAQGGLL------RRGLL 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17537075 229 TNEVVAGIAKAHGKTPAQIILRWFV-DSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19138 205 ENPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-289 |
1.03e-41 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 145.41 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 10 GYSIPAIGLGTWQ---------SKPGEVAAAIKTAVAAGYRHIDCAHVY---QNQKEVGEALKEIldegkvKREELFITS 77
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKDF------PREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 78 KVWNTFHSEAKAHENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSI 157
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPN-------------------PNIPLEETLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 158 GLSNFTHSQIQRVWDAAEVKPACLQVELHPY---FTQVKLREFCKEKGIVVVGYSPLGNPGsaffrkdgdpnVLTNEVVA 234
Cdd:cd19137 136 GVSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRGL-----------EKTNRTLE 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17537075 235 GIAKAHGKTPAQIILRWFVDS-GLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19137 205 EIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
8-291 |
2.67e-40 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 143.01 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLGTWQ--SKPGEVAAAIKTA-----VAAGYRHIDCAHVY---QNQKEVGEALKEildegkVKREELFITS 77
Cdd:COG0667 8 RSGLKVSRLGLGTMTfgGPWGGVDEAEAIAildaaLDAGINFFDTADVYgpgRSEELLGEALKG------RPRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 78 KVWNTF--------HSEAKAHENIDIILSDLQLSYVDLMLIHWPQGyaegaelfpagengkmrysDVDYLETWKAFEAAQ 149
Cdd:COG0667 82 KVGRRMgpgpngrgLSREHIRRAVEASLRRLGTDYIDLYQLHRPDP-------------------DTPIEETLGALDELV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 150 KAGKCRSIGLSNFTHSQIQRVWDAAE--VKPACLQVELHPYFTQV--KLREFCKEKGIVVVGYSPLGN------------ 213
Cdd:COG0667 143 REGKIRYIGVSNYSAEQLRRALAIAEglPPIVAVQNEYSLLDRSAeeELLPAARELGVGVLAYSPLAGglltgkyrrgat 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 214 ------PGSAFFRKDGDPNVLTN-EVVAGIAKAHGKTPAQIILRW-----FVDsglSAIPKSVTPQRIIENISVIDFQLS 281
Cdd:COG0667 223 fpegdrAATNFVQGYLTERNLALvDALRAIAAEHGVTPAQLALAWllaqpGVT---SVIPGARSPEQLEENLAAADLELS 299
|
330
....*....|
gi 17537075 282 AEEIQAIDGV 291
Cdd:COG0667 300 AEDLAALDAA 309
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-289 |
9.59e-37 |
|
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: 133.12 E-value: 9.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 13 IPAIGLGTWQ-----------SKPGEVAAAIKTAVAAGYRHIDCAHVY---QNQKEVGEALKEILDegkvkREELFITSK 78
Cdd:cd19093 2 VSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGD-----RDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 79 VW-----NTFHSEAKAHENIdiiLSDLQLSYVDLMLIHWPQGYaegaelfpagengkmrYSDVDYLetWKAFEAAQKAGK 153
Cdd:cd19093 77 FAplpwrLTRRSVVKALKAS---LERLGLDSIDLYQLHWPGPW----------------YSQIEAL--MDGLADAVEEGL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 154 CRSIGLSNFTHSQIQRVWDAAE---VKPACLQVE---LHPYFTQVKLREFCKEKGIVVVGYSPL---------------- 211
Cdd:cd19093 136 VRAVGVSNYSADQLRRAHKALKergVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLaqglltgkyspenppp 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 212 GNPGSAFFRK--DGDPNVLtnEVVAGIAKAHGKTPAQIILRWFVDSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19093 216 GGRRRLFGRKnlEKVQPLL--DALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
43-289 |
2.42e-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: 126.87 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 43 IDCAHVYQN---QKEVGEALKEildegkvKREELFITSKV---WNTFHSEAK----AH--ENIDIILSDLQLSYVDLMLI 110
Cdd:cd19084 42 FDTAPVYGFghsEEILGKALKG-------RRDDVVIATKCglrWDGGKGVTKdlspESirKEVEQSLRRLQTDYIDLYQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 111 HWPQGyaegaelfpagengkmrysDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVwdAAEVKPACLQVELHPYFT 190
Cdd:cd19084 115 HWPDP-------------------NTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA--RKYGPIVSLQPPYSMLER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 191 QV--KLREFCKEKGIVVVGYSPLGN--------------PG-----SAFFRKDGDPNVLtnEVVAG---IAKAHGKTPAQ 246
Cdd:cd19084 174 EIeeELLPYCRENGIGVLPYGPLAQglltgkykkeptfpPDdrrsrFPFFRGENFEKNL--EIVDKlkeIAEKYGKSLAQ 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17537075 247 IILRW-----FVDsglSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19084 252 LAIAWtlaqpGVT---SAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-291 |
7.52e-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: 122.70 E-value: 7.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 13 IPAIGLGTWQSKPGEVAAAIKTAVA---------AGYRHIDCAHVYQN---QKEVGEALKEildegkvKREELFITSKVW 80
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWGDQDDEESiatihaaldAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 81 --NTFHSEAKAHenIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSIG 158
Cdd:cd19085 74 pdNLTPEDVRKS--CERSLKRLGTDYIDLYQIHWPS-------------------SDVPLEETMEALEKLKEEGKIRAIG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 159 LSNFTHSQIQRVWDAAEVkpACLQVELHPYFTQVK--LREFCKEKGIVVVGYSPLG--------NPGSAF--------FR 220
Cdd:cd19085 133 VSNFGPAQLEEALDAGRI--DSNQLPYNLLWRAIEyeILPFCREHGIGVLAYSPLAqglltgkfSSAEDFppgdartrLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 221 KDGDPNV--LTNEVVA---GIAKAHGKTPAQIILRW-----FVDsglSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDG 290
Cdd:cd19085 211 RHFEPGAeeETFEALEklkEIADELGVTMAQLALAWvlqqpGVT---SVIVGARNPEQLEENAAAVDLELSPSVLERLDE 287
|
.
gi 17537075 291 V 291
Cdd:cd19085 288 I 288
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
39-274 |
1.05e-28 |
|
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: 110.30 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVY---QNQKEVGEALKEildegKVKREELFITSKVWNTFH--------SEAKAHENIDIILSDLQLSYVDL 107
Cdd:cd06660 30 GGNFFDTADVYgdgRSERLLGRWLKG-----RGNRDDVVIATKGGHPPGgdpsrsrlSPEHIRRDLEESLRRLGTDYIDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 108 MLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAE----VKPACLQV 183
Cdd:cd06660 105 YYLHRDD-------------------PSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKahglPGFAAVQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 184 E---LHPYFTQVKLREFCKEKGIVVVGYSPLgnpgsaffrkdgdpnvltnevvagiakAHGktPAQIILRWFVDSGL--S 258
Cdd:cd06660 166 QyslLDRSPMEEELLDWAEENGLPLLAYSPL---------------------------ARG--PAQLALAWLLSQPFvtV 216
|
250
....*....|....*.
gi 17537075 259 AIPKSVTPQRIIENIS 274
Cdd:cd06660 217 PIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-289 |
1.25e-25 |
|
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: 103.52 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 13 IPAIGLGTWQSKPG------------EVAAAIKTAVAAGYRHIDCAHVY---QNQKEVGEALKEIldegkvkREELFITS 77
Cdd:cd19102 1 LTTIGLGTWAIGGGgwgggwgpqddrDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 78 K---VWN------TFHSEAKAHENIDIILSDLQLSYVDLMLIHWPQGyaegaelfpagengkmrysDVDYLETWKAFEAA 148
Cdd:cd19102 74 KcglLWDeegrirRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP-------------------DEPIEEAWGALAEL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 149 QKAGKCRSIGLSNFTHSQIQRVWDAAEVkpACLQVE---LHPYFTQVKLReFCKEKGIVVVGYSPLGN------------ 213
Cdd:cd19102 135 KEEGKVRAIGVSNFSVDQMKRCQAIHPI--ASLQPPyslLRRGIEAEILP-FCAEHGIGVIVYSPMQSglltgkmtperv 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 214 ---------PGSAFFRKDG-DPNVLTNEVVAGIAKAHGKTPAQIILRWFV--DSGLSAIPKSVTPQRIIENISVIDFQLS 281
Cdd:cd19102 212 aslpaddwrRRSPFFQEPNlARNLALVDALRPIAERHGRTVAQLAIAWVLrrPEVTSAIVGARRPDQIDETVGAADLRLT 291
|
....*...
gi 17537075 282 AEEIQAID 289
Cdd:cd19102 292 PEELAEIE 299
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
39-289 |
5.51e-22 |
|
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: 93.80 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVYQN---QKEVGEALKEILdegkvKREELFITSKVWNTFHSEAKA--------HENIDIILSDLQLSYVDL 107
Cdd:cd19079 48 GINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFPMGDGPNGrglsrkhiMAEVDASLKRLGTDYIDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 108 MLIHWpqgyaegaeLFPagengkmrysDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAE----VKPACLQv 183
Cdd:cd19079 123 YQIHR---------WDY----------ETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEkngwTKFVSMQ- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 184 elhPYFTQV---KLRE---FCKEKGIVVVGYSPLGN-------------------PGSAFFRKDGDPNVLTNEVVAGIAK 238
Cdd:cd19079 183 ---NHYNLLyreEEREmipLCEEEGIGVIPWSPLARgrlarpwgdtterrrsttdTAKLKYDYFTEADKEIVDRVEEVAK 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17537075 239 AHGKTPAQIILRWFVDSGLSAIP--KSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19079 260 ERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
42-284 |
4.31e-21 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 91.08 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 42 HIDCAHVYQNQKeVGEALKEILDEGKVKREELFITSK----VWNTFHSEAKAH-----ENI----DIILSDLQLSYVDLM 108
Cdd:cd19092 40 TFDHADIYGGGK-CEELFGEALALNPGLREKIEIQTKcgirLGDDPRPGRIKHydtskEHIlasvEGSLKRLGTDYLDLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 109 LIHWPqgyaegaelfpagengkmrysdvDYL----ETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAEVKPACLQVE 184
Cdd:cd19092 119 LLHRP-----------------------DPLmdpeEVAEAFDELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 185 LHPYFTQV---KLREFCKEKGIVVVGYSPLGnpGSAFFRKDGDPNVLTNEVVAGIAKAHGKTPAQIILRWFVD--SGLSA 259
Cdd:cd19092 176 LSLLHTEAiddGTLDYCQLLDITPMAWSPLG--GGRLFGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRhpARIQP 253
|
250 260
....*....|....*....|....*
gi 17537075 260 IPKSVTPQRIIENISVIDFQLSAEE 284
Cdd:cd19092 254 ILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
140-289 |
7.03e-21 |
|
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: 90.76 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 140 ETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVwdAAEVKPACLQVELHPYFTQVKLR---EFCKEKGIVVVGYSPLG---- 212
Cdd:cd19077 129 ETIKALKELVKEGKIRGIGLSEVSAETIRRA--HAVHPIAAVEVEYSLFSREIEENgvlETCAELGIPIIAYSPLGrgll 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 213 ------------NPGSAFFRKDGDPNVLTN----EVVAGIAKAHGKTPAQIILRWFVDSGLSAI---PKSVTPQRIIENI 273
Cdd:cd19077 207 tgriksladipeGDFRRHLDRFNGENFEKNlklvDALQELAEKKGCTPAQLALAWILAQSGPKIipiPGSTTLERVEENL 286
|
170
....*....|....*.
gi 17537075 274 SVIDFQLSAEEIQAID 289
Cdd:cd19077 287 KAANVELTDEELKEIN 302
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
8-288 |
1.68e-20 |
|
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: 89.58 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLG----TW---QSKPGEVAAAIKTAVAAGYRHIDCAHVYQ---NQKEVGEALKEildegkvKREELFITS 77
Cdd:cd19076 7 TQGLEVSALGLGcmgmSAfygPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD-------RRDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 78 K---VWNTFHSEAK-------AHENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEA 147
Cdd:cd19076 80 KfgiVRDPGSGFRGvdgrpeyVRAACEASLKRLGTDVIDLYYQHRVD-------------------PNVPIEETVGAMAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 148 AQKAGKCRSIGLSNFTHSQIQRvwdAAEVKP-ACLQVELHPYFTQVKLREF--CKEKGIVVVGYSPLGN----------- 213
Cdd:cd19076 141 LVEEGKVRYIGLSEASADTIRR---AHAVHPiTAVQSEYSLWTRDIEDEVLptCRELGIGFVAYSPLGRgfltgaikspe 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 214 --PGSAFFRKDG-------DPNVLTNEVVAGIAKAHGKTPAQIILRWFVDSG--LSAIPKSVTPQRIIENISVIDFQLSA 282
Cdd:cd19076 218 dlPEDDFRRNNPrfqgenfDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTP 297
|
....*.
gi 17537075 283 EEIQAI 288
Cdd:cd19076 298 EELAEI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
39-289 |
1.79e-20 |
|
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: 89.79 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVY---QNQKEVGEALKEildegkVKREELFITSKVWNTF--------HSEAKAHENIDIILSDLQLSYVDL 107
Cdd:cd19083 46 GVNLLDTAFIYglgRSEELVGEVLKE------YNRNEVVIATKGAHKFggdgsvlnNSPEFLRSAVEKSLKRLNTDYIDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 108 MLIHWPQGYAEGAELFPAgengkmrysdvdyLETWKafeaaqKAGKCRSIGLSNFTHSQIQrvwDAAevKPACLQVELHP 187
Cdd:cd19083 120 YYIHFPDGETPKAEAVGA-------------LQELK------DEGKIRAIGVSNFSLEQLK---EAN--KDGYVDVLQGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 188 YF-----TQVKLREFCKEKGIVVVGYSPL------GNPGSAFFRKDGD--------------PNVLTNEVVAGIAKAHGK 242
Cdd:cd19083 176 YNllqreAEEDILPYCVENNISFIPYFPLasgllaGKYTKDTKFPDNDlrndkplfkgerfsENLDKVDKLKSIADEKGV 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17537075 243 TPAQIILRWFV--DSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19083 256 TVAHLALAWYLtrPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFID 304
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
39-289 |
1.49e-19 |
|
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: 86.88 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVYQNQKE----------VGEALKEildegKVKREELFITSKV-WNTFH-----SEAKAHENIDIILSDLQL 102
Cdd:cd19081 39 GGNFIDTADVYSAWVPgnaggesetiIGRWLKS-----RGKRDRVVIATKVgFPMGPngpglSRKHIRRAVEASLRRLQT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 103 SYVDLMLIHWPQGyaegaelfpagengkmrysDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAE----VKP 178
Cdd:cd19081 114 DYIDLYQAHWDDP-------------------ATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhglPRY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 179 ACLQVE---LHPYFTQVKLREFCKEKGIVVVGYSPLGN-------------PGS-----AFFRKDGDPNVLTNEVVAGIA 237
Cdd:cd19081 175 VSLQPEynlVDRESFEGELLPLCREEGIGVIPYSPLAGgfltgkyrseadlPGStrrgeAAKRYLNERGLRILDALDEVA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17537075 238 KAHGKTPAQIILRWFV--DSGLSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19081 255 AEHGATPAQVALAWLLarPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
8-291 |
1.66e-19 |
|
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: 86.90 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLGT--------WQSKPGEVAAAIKTAVA-----AGYRHIDCAHVYQN-QKEV--GEALKEildegkvKRE 71
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggFFGAWGGVDQEEADRLVdialdAGINFFDTADVYSEgESEEilGKALKG-------RRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 72 ELFITSKVWNTF-----HSEAKAH---ENIDIILSDLQLSYVDLMLIHWPQGYAEgaelfpagengkmrysdvdYLETWK 143
Cdd:cd19091 81 DVLIATKVRGRMgegpnDVGLSRHhiiRAVEASLKRLGTDYIDLYQLHGFDALTP-------------------LEETLR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 144 AFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAE----VKPACLQVelhpYFTQV------KLREFCKEKGIVVVGYSPLGN 213
Cdd:cd19091 142 ALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQA----YYSLLgrdlehELMPLALDQGVGLLVWSPLAG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 214 --------------PGSAFFRKDGDPNVLTNE-------VVAGIAKAHGKTPAQIILRWFV--DSGLSAIPKSVTPQRII 270
Cdd:cd19091 218 gllsgkyrrgqpapEGSRLRRTGFDFPPVDRErgydvvdALREIAKETGATPAQVALAWLLsrPTVSSVIIGARNEEQLE 297
|
330 340
....*....|....*....|.
gi 17537075 271 ENISVIDFQLSAEEIQAIDGV 291
Cdd:cd19091 298 DNLGAAGLSLTPEEIARLDKV 318
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-283 |
2.56e-19 |
|
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: 86.11 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 10 GYSIPAIGLGTWQSKPGEVAAAIKTAVA-----AGYRHIDCAHVY---QNQKEVGEALKEIldegkvKREELFITSKV-W 80
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVrkaydLGINFFDTADVYaagQAEEVLGKALKGW------PRESYVISTKVfW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 81 NTFHSE-----AKAH--ENIDIILSDLQLSYVDLMLIHwpqgyaegaelfpagengkmRYS-DVDYLETWKAFEAAQKAG 152
Cdd:cd19074 75 PTGPGPndrglSRKHifESIHASLKRLQLDYVDIYYCH--------------------RYDpETPLEETVRAMDDLIRQG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 153 KCRSIGLSNFTHSQIQRVWDAAE----VKPACLQVELHPYFTQV--KLREFCKEKGIVVVGYSPL-----------GNP- 214
Cdd:cd19074 135 KILYWGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYNMLWREIeeEVIPLCEKNGIGLVVWSPLaqglltgkyrdGIPp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 215 --GSAFFRKDGDP---NVLTNEVVA------GIAKAHGKTPAQIILRWFV--DSGLSAIPKSVTPQRIIENISVIDFQLS 281
Cdd:cd19074 215 psRSRATDEDNRDkkrRLLTDENLEkvkklkPIADELGLTLAQLALAWCLrnPAVSSAIIGASRPEQLEENVKASGVKLS 294
|
..
gi 17537075 282 AE 283
Cdd:cd19074 295 PE 296
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
8-288 |
5.78e-19 |
|
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: 85.57 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLGTW-------QSKPGEVAAAI-KTAVAAGYRHIDCAHVYQ-NQKEVGEALKeiLDEGKvkREELFITSK 78
Cdd:cd19144 8 RNGPSVPALGFGAMglsafygPPKPDEERFAVlDAAFELGCTFWDTADIYGdSEELIGRWFK--QNPGK--REKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 79 VWNTFHSEAKA----------HENIDIILSDLQLSYVDLMLIHwpqgyaegaelfpagengkmRYSDVDYLE-TWKAFEA 147
Cdd:cd19144 84 FGIEKNVETGEysvdgspeyvKKACETSLKRLGVDYIDLYYQH--------------------RVDGKTPIEkTVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 148 AQKAGKCRSIGLSNFTHSQIQRvwdAAEVKP-ACLQVELHPYFT-----QVKLREFCKEKGIVVVGYSPLGN---PGSAF 218
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETLRR---AHAVHPiAAVQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGRgflTGAIR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 219 FRKDGDPN------------------VLTNEVVAgIAKAHGKTPAQIILRWFVDSGLSA--IPKSVTPQRIIENISVIDF 278
Cdd:cd19144 221 SPDDFEEGdfrrmaprfqaenfpknlELVDKIKA-IAKKKNVTAGQLTLAWLLAQGDDIipIPGTTKLKRLEENLGALKV 299
|
330
....*....|
gi 17537075 279 QLSAEEIQAI 288
Cdd:cd19144 300 KLTEEEEKEI 309
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-276 |
3.23e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 82.25 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVYQNQKE---VGEALKeildegKVKREELFITSKVWNTFHSEAKAH--ENIDIILSDLQLSYVDLMLIHwp 113
Cdd:cd19105 38 GINYFDTAEGYGNGNSeeiIGEALK------GLRRDKVFLATKASPRLDKKDKAEllKSVEESLKRLQTDYIDIYQLH-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 114 qgyaegaelfpAGENGKMRYSDVDYLEtwkAFEAAQKAGKCRSIGLSnfTHSQIQRVWDAAeVKPACLQVELHPY--FTQ 191
Cdd:cd19105 110 -----------GVDTPEERLLNEELLE---ALEKLKKEGKVRFIGFS--THDNMAEVLQAA-IESGWFDVIMVAYnfLNQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 192 VKLRE----FCKEKGIVVVGYSPLGnpGSAFFRKDGDPNVLTnevvagiakahGKTPAQIILRW-----FVDSGLSAIPk 262
Cdd:cd19105 173 PAELEealaAAAEKGIGVVAMKTLA--GGYLQPALLSVLKAK-----------GFSLPQAALKWvlsnpRVDTVVPGMR- 238
|
250
....*....|....
gi 17537075 263 svTPQRIIENISVI 276
Cdd:cd19105 239 --NFAELEENLAAA 250
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
39-281 |
4.26e-18 |
|
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: 81.88 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVY---QNQKEVGEALKEildegkvKREELFITSKV---------WNTFHSEAKAHENIDIILSDLQLSYVD 106
Cdd:cd19088 37 GVNFIDTADSYgpdVNERLIAEALHP-------YPDDVVIATKGglvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRID 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 107 LMLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAEVkpACLQVELH 186
Cdd:cd19088 110 LYQLHRID-------------------PKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI--VSVQNRYN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 187 PYFTQ-VKLREFCKEKGIVVVGYSPLgnpGSAFFRKDGDPnvltnevVAGIAKAHGKTPAQIILRWFVDSG--LSAIPKS 263
Cdd:cd19088 169 LANRDdEGVLDYCEAAGIAFIPWFPL---GGGDLAQPGGL-------LAEVAARLGATPAQVALAWLLARSpvMLPIPGT 238
|
250
....*....|....*...
gi 17537075 264 VTPQRIIENISVIDFQLS 281
Cdd:cd19088 239 SSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
39-289 |
6.11e-18 |
|
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: 82.28 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVY---QNQKEVGEALKEildegkvKREELFITSKVWNTFHSEAKAHENID----II-------LSDLQLSY 104
Cdd:cd19078 38 GITFFDTAEVYgpyTNEELVGEALKP-------FRDQVVIATKFGFKIDGGKPGPLGLDsrpeHIrkavegsLKRLQTDY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 105 VDLMLIHwpqgyaegaelfpagengkmRYS-DVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRvwdAAEVKP-ACLQ 182
Cdd:cd19078 111 IDLYYQH--------------------RVDpNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRR---AHAVCPvTAVQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 183 VELHPYFTQV--KLREFCKEKGIVVVGYSPLG--------NPGSAFFRKDgDPNVLTN-------------EVVAGIAKA 239
Cdd:cd19078 168 SEYSMMWREPekEVLPTLEELGIGFVPFSPLGkgfltgkiDENTKFDEGD-DRASLPRftpealeanqalvDLLKEFAEE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17537075 240 HGKTPAQIILRWFVDSG--LSAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19078 247 KGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
8-289 |
1.01e-17 |
|
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: 81.94 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLGTW---------QSKPGEVAAAIKTAVAAGYRHIDCAHVYQN---QKEVGEALKEildegkvKREELFI 75
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 76 TSK---VWNT----FHSEAKAH------------ENIDIILSDLQLSYVDLMLIHWPqgyaegAELFPAGEngkmrysdv 136
Cdd:cd19149 79 ATKcglRWDReggsFFFVRDGVtvyknlspesirEEVEQSLKRLGTDYIDLYQTHWQ------DVETPIEE--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 137 dyleTWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAEVkpACLQV-----------ELHPYftqvklrefCKEKGIVV 205
Cdd:cd19149 144 ----TMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQEkysmldrgiekELLPY---------CKKNNIAF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 206 VGYSPLG--------------NPGSA-----FFRKDGDPNVLT-NEVVAGIAKAHGKTPAQIILRWFVDSG--LSAIPKS 263
Cdd:cd19149 209 QAYSPLEqglltgkitpdrefDAGDArsgipWFSPENREKVLAlLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGA 288
|
330 340
....*....|....*....|....*.
gi 17537075 264 VTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19149 289 RKPEQAEENAKAGDIRLSAEDIATMR 314
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-273 |
4.02e-17 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 79.20 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 14 PAIGLGTWQskPGEVAAAIKTAVAA---------GYRHIDCAHVYQNQKEV-GEALKEILdegkvkREELFITSKVWNTF 83
Cdd:cd19095 1 SVLGLGTSG--IGRVWGVPSEAEAArllntaldlGINLIDTAPAYGRSEERlGRALAGLR------RDDLFIATKVGTHG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSEAKAH--------ENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFPAgengkmrysdvdyLETWKAfeaaqkAGKCR 155
Cdd:cd19095 73 EGGRDRKdfspaairASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLET-------------LEDLKA------AGKVR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 156 SIGLSNFThsqiQRVWDAAEVKP-ACLQVELHPY-FTQVKLREFCKEKGIVVVGYSPLGNpGSAFFRKDGDPNVLTNEVV 233
Cdd:cd19095 134 YIGVSGDG----EELEAAIASGVfDVVQLPYNVLdREEEELLPLAAEAGLGVIVNRPLAN-GRLRRRVRRRPLYADYARR 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17537075 234 AGIAKAHG-KTPAQIILRWFVDSGL--SAIPKSVTPQRIIENI 273
Cdd:cd19095 209 PEFAAEIGgATWAQAALRFVLSHPGvsSAIVGTTNPEHLEENL 251
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
42-291 |
5.93e-17 |
|
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: 79.92 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 42 HIDCAHVY--------QNQKE--VGEALKeildeGKVKREELFITSKV-----WNTFHSEAKA---HENI----DIILSD 99
Cdd:cd19094 34 FIDTAEMYpvppspetQGRTEeiIGSWLK-----KKGNRDKVVLATKVagpgeGITWPRGGGTrldRENIreavEGSLKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 100 LQLSYVDLMLIHWPQGYAEGAELFPAGENGKmRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAEV--- 176
Cdd:cd19094 109 LGTDYIDLYQLHWPDRYTPLFGGGYYTEPSE-EEDSVSFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQlgl 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 177 -KPACLQvelHPY--FTQ---VKLREFCKEKGIVVVGYSPLG--------------NPG---SAFF----RKDGDPNVLT 229
Cdd:cd19094 188 pRIVSIQ---NPYslLNRnfeEGLAEACHRENVGLLAYSPLAggvltgkyldgaarPEGgrlNLFPgymaRYRSPQALEA 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17537075 230 NEVVAGIAKAHGKTPAQIIL-----RWFVDsglSAIPKSVTPQRIIENISVIDFQLSAEEIQAIDGV 291
Cdd:cd19094 265 VAEYVKLARKHGLSPAQLALawvrsRPFVT---STIIGATTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
8-285 |
1.19e-15 |
|
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: 76.14 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLGTWQ-----SKPGEVAAAIKTAVAAGYRHIDCAHVY-----QNQKEVGEALKEILdegKVKREELFITS 77
Cdd:cd19089 6 RSGLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDL---RPYRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 78 KV----W----NTFHSEAKAHENIDIILSDLQLSYVDLMLIHwpqgyaegaelfpagengkmRY-SDVDYLETWKAFEAA 148
Cdd:cd19089 83 KAgygmWpgpyGDGGSRKYLLASLDQSLKRMGLDYVDIFYHH--------------------RYdPDTPLEETMTALADA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 149 QKAGKCRSIGLSNFTHSQIQR---VWDAAEVKPACLQVELHPYFTQVK--LREFCKEKGIVVVGYSPL-----------G 212
Cdd:cd19089 143 VRSGKALYVGISNYPGAKARRaiaLLRELGVPLIIHQPRYSLLDRWAEdgLLEVLEEAGIGFIAFSPLaqglltdkylnG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 213 NPGSAFFRKDG---------DPNVLTNEVVAGIAKAHGKTPAQIILRWFV-DSGLSAIPKSVT-PQRIIENISVID-FQL 280
Cdd:cd19089 223 IPPDSRRAAESkflteealtPEKLEQLRKLNKIAAKRGQSLAQLALSWVLrDPRVTSVLIGASsPSQLEDNVAALKnLDF 302
|
....*
gi 17537075 281 SAEEI 285
Cdd:cd19089 303 SEEEL 307
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
8-302 |
1.31e-15 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 76.43 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLGTW----QSKPGEVAAAIKTAVAAGYRHIDCAHVYQ----------NQKEVGEALKEildegKVKREEL 73
Cdd:PRK10625 8 HSSLEVSTLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAK-----RGSREKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 74 FITSKV----WNTFHS----EAKAHENIDIILSD----LQLSYVDLMLIHWPQGyaegaelfPAGENGKM--RYSD---- 135
Cdd:PRK10625 83 IIASKVsgpsRNNDKGirpnQALDRKNIREALHDslkrLQTDYLDLYQVHWPQR--------PTNCFGKLgySWTDsapa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 136 VDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAEVK--PACLQVElHPYFT-----QVKLREFCKEKGIVVVGY 208
Cdd:PRK10625 155 VSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHdlPRIVTIQ-NPYSLlnrsfEVGLAEVSQYEGVELLAY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 209 SPLG------------NPGSA-------FFRKDGDPNVLTNEVVAGIAKAHGKTPAQIILRW-----FVDSGLSAipkSV 264
Cdd:PRK10625 234 SCLAfgtltgkylngaKPAGArntlfsrFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFvrrqpFVASTLLG---AT 310
|
330 340 350
....*....|....*....|....*....|....*...
gi 17537075 265 TPQRIIENISVIDFQLSAEEIQAIDGVNRgwRLVDPSP 302
Cdd:PRK10625 311 TMEQLKTNIESLHLTLSEEVLAEIEAVHQ--VYTYPAP 346
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
39-291 |
1.84e-14 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 72.93 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVYQNQKE-VGEALKEIldegkvkREELFITSKVWNTFHSEAKAHENIDIILSDLQLSYVDLMLIH------ 111
Cdd:COG1453 42 GINYIDTARGYGDSEEfLGKALKGP-------RDKVILATKLPPWVRDPEDMRKDLEESLKRLQTDYIDLYLIHglntee 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 112 -WPQGYAEGaelfpagengkmrysdvdylETWKAFEAAQKAGKCRSIGLSnfTHSQ---IQRV-----WDaaevkpaCLQ 182
Cdd:COG1453 115 dLEKVLKPG--------------------GALEALEKAKAEGKIRHIGFS--THGSlevIKEAidtgdFD-------FVQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 183 VELHPYFTQVKLR----EFCKEKGIVVVGYSPLgnpgsaffrKDGDPNVLTNEVVAGIAKahGKTPAQIILRWF------ 252
Cdd:COG1453 166 LQYNYLDQDNQAGeealEAAAEKGIGVIIMKPL---------KGGRLANPPEKLVELLCP--PLSPAEWALRFLlshpev 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17537075 253 --VDSGLSaipksvTPQRIIENISVID--FQLSAEEIQAIDGV 291
Cdd:COG1453 235 ttVLSGMS------TPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
39-277 |
3.47e-14 |
|
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: 71.05 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVYQNQK-E--VGEALKEildegkVKREELFITSKV-WNTFHSEAKAHENIDIILSDLQLSYVDLMLIHWPQ 114
Cdd:cd19096 34 GINYFDTAYGYGGGKsEeiLGEALKE------GPREKFYLATKLpPWSVKSAEDFRRILEESLKRLGVDYIDFYLLHGLN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 115 GYaegaELFPAGENGKMrysdvdyletWKAFEAAQKAGKCRSIGLSnfTHSQ---IQRVWDAAEVkpACLQVELH----P 187
Cdd:cd19096 108 SP----EWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS--FHDSpelLKEILDSYDF--DFVQLQYNyldqE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 188 YFTQVKLREFCKEKGIVVVGYSPLgnpgsaffRKDGDPNvlTNEVVAGIAKAHGKTPAQIILRWFVD--------SGLSa 259
Cdd:cd19096 170 NQAGRPGIEYAAKKGMGVIIMEPL--------KGGGLAN--NPPEALAILCGAPLSPAEWALRFLLShpevttvlSGMS- 238
|
250
....*....|....*...
gi 17537075 260 ipksvTPQRIIENISVID 277
Cdd:cd19096 239 -----TPEQLDENIAAAD 251
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
16-289 |
5.22e-14 |
|
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: 71.18 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 16 IGLGTWQ--------SKPGEVAAAIKTAVAAGYRHIDCAHVY---QNQKEVGEALKEIldegkVKREELFITSKV---WN 81
Cdd:cd19148 7 IALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEY-----GKRDRVVIATKVgleWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 82 TFH------SEAKAHENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCR 155
Cdd:cd19148 82 EGGevvrnsSPARIRKEVEDSLRRLQTDYIDLYQVHWPD-------------------PLVPIEETAEALKELLDEGKIR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 156 SIGLSNFTHSQIQRVWDAAEvkpacLQVELHPY--FTQVKLRE---FCKEKGIVVVGYSPLG--------NPGSAF---- 218
Cdd:cd19148 143 AIGVSNFSPEQMETFRKVAP-----LHTVQPPYnlFEREIEKDvlpYARKHNIVTLAYGALCrgllsgkmTKDTKFegdd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 219 -------FRKDGDPNVLTN-EVVAGIAKAH-GKTPAQIILRWFVDSGLSAIP--KSVTPQRIIENISVIDFQLSAEEIQA 287
Cdd:cd19148 218 lrrtdpkFQEPRFSQYLAAvEELDKLAQERyGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKE 297
|
..
gi 17537075 288 ID 289
Cdd:cd19148 298 ID 299
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-212 |
8.57e-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: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLGT---WQSKPGEVAAAIKTAVAAGYRHIDCAHVYQN-QKEVGEALKEildegkvKREELFITSKVWNtf 83
Cdd:cd19100 6 RTGLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATKTGA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 84 HSEAKAHENIDIILSDLQLSYVDLMLIHWPQGYAEGAELFpaGENGkmrysdvdyleTWKAFEAAQKAGKCRSIGLSnfT 163
Cdd:cd19100 77 RDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVF--GPGG-----------ALEALLEAKEEGKIRFIGIS--G 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17537075 164 HSqIQRVWDAAEVKP-ACLQV-------ELHPYFTQVkLREfCKEKGIVVVGYSPLG 212
Cdd:cd19100 142 HS-PEVLLRALETGEfDVVLFpinpagdHIDSFREEL-LPL-AREKGVGVIAMKVLA 195
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-291 |
9.70e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 70.32 E-value: 9.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 12 SIPAIGLGTWQ--------SKPGEVAAAIKTAVAAGYRHIDCAHVYQNQKE-VGEALKEILDEGKVKREELFITSKVWNT 82
Cdd:cd19101 1 TISRVINGMWQlsgghggiRDEDAAVRAMAAYVDAGLTTFDCADIYGPAEElIGEFRKRLRRERDAADDVQIHTKWVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 83 FH---SEAKAHENIDIILSDLQLSYVDLMLIHWpqgyaegaelfpagengkMRYSDVDYLETWKAFEAAQKAGKCRSIGL 159
Cdd:cd19101 81 GEltmTRAYVEAAIDRSLKRLGVDRLDLVQFHW------------------WDYSDPGYLDAAKHLAELQEEGKIRHLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 160 SNFTHSQIQRVWDAAeVKPACLQVEL-----HPyftQVKLREFCKEKGIVVVGYSPLgnpGSAFF------RKDGDPNVL 228
Cdd:cd19101 143 TNFDTERLREILDAG-VPIVSNQVQYslldrRP---ENGMAALCEDHGIKLLAYGTL---AGGLLsekylgVPEPTGPAL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 229 TN-----------------------EVVAGIAKAHGKTPAQIILRWFVDS-GLSAIPKSVTPQR-IIENISVIDFQLSAE 283
Cdd:cd19101 216 ETrslqkyklmidewggwdlfqellRTLKAIADKHGVSIANVAVRWVLDQpGVAGVIVGARNSEhIDDNVRAFSFRLDDE 295
|
....*...
gi 17537075 284 EIQAIDGV 291
Cdd:cd19101 296 DRAAIDAV 303
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-251 |
1.41e-13 |
|
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: 70.04 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 43 IDCAHVYQNQ---KEVGEALKEILDEGKVKREELFITSKV-------------WNTFHSEAKAHEN-------------- 92
Cdd:cd19099 38 IDTAINYRGGrseRLIGKALRELIEKGGIKRDEVVIVTKAgyipgdgdeplrpLKYLEEKLGRGLIdvadsaglrhcisp 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 93 ------IDIILSDLQLSYVDLMLIHWPqgyaegaELFPAGENGKMRYSDVDylETWKAFEAAQKAGKCRSIGLS------ 160
Cdd:cd19099 118 ayledqIERSLKRLGLDTIDLYLLHNP-------EEQLLELGEEEFYDRLE--EAFEALEEAVAEGKIRYYGIStwdgfr 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 161 -----NFTHSQIQRVWDAAEV---KPAC--LQVELHPYFTQVKLR------------EFCKEKGIVVVGYSPLgNPGsaf 218
Cdd:cd19099 189 appalPGHLSLEKLVAAAEEVggdNHHFkvIQLPLNLLEPEALTEkntvkgealsllEAAKELGLGVIASRPL-NQG--- 264
|
250 260 270
....*....|....*....|....*....|...
gi 17537075 219 frKDGDPNVLTNEVvagiAKAHGKTPAQIILRW 251
Cdd:cd19099 265 --QLLGELRLADLL----ALPGGATLAQRALQF 291
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
39-253 |
2.07e-13 |
|
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: 69.51 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVYQNqkevGEAlKEILDEGKVKREELFITSKV---WNTFHSEAKAHENIDIILSDLQLSYVDLMLIHWPQg 115
Cdd:cd19075 33 GHTEIDTARVYPD----GTS-EELLGELGLGERGFKIDTKAnpgVGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 116 yaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAE----VKPACLQ--------- 182
Cdd:cd19075 107 ------------------RSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTVYQgmynaitrq 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 183 --VELHPYftqvkLREFckekGIVVVGYSPLG-----------------------NPGSAFFRK--DGDPNVLTNEVVAG 235
Cdd:cd19075 169 veTELFPC-----LRKL----GIRFYAYSPLAggfltgkykysedkagggrfdpnNALGKLYRDryWKPSYFEALEKVEE 239
|
250
....*....|....*...
gi 17537075 236 IAKAHGKTPAQIILRWFV 253
Cdd:cd19075 240 AAEKEGISLAEAALRWLY 257
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
12-211 |
3.71e-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: 62.11 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 12 SIPAIGLGTWQ--------SKPGEVAAAIKTAVAAGYRHIDCAHVYQN---QKEVGEALKEildegkvKREELFITSKVW 80
Cdd:cd19086 2 EVSEIGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVVIATKFG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 81 NTFHSEAKAHENID---II------LSDLQLSYVDLMLIHwpqgyaegaelfpageNGKMRYSDVDylETWKAFEAAQKA 151
Cdd:cd19086 75 NRFDGGPERPQDFSpeyIReaveasLKRLGTDYIDLYQLH----------------NPPDEVLDND--ELFEALEKLKQE 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17537075 152 GKCRSIGLSnfthsqIQRVWDAAEV----KPACLQVELHPyFTQVKLREF---CKEKGIVVVGYSPL 211
Cdd:cd19086 137 GKIRAYGVS------VGDPEEALAAlrrgGIDVVQVIYNL-LDQRPEEELfplAEEHGVGVIARVPL 196
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
43-289 |
4.15e-11 |
|
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: 62.59 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 43 IDCAHVYQNQKE---VGEALKEildegkvKREELFITSKVWNTFHSEAKAH--------ENIDIILSDLQLSYVDLMLIH 111
Cdd:cd19087 47 FDTADVYGGGRSeeiIGRWIAG-------RRDDIVLATKVFGPMGDDPNDRglsrrhirRAVEASLRRLQTDYIDLYQMH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 112 WPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQR-VWDAAEVKPACLQVELHPY-- 188
Cdd:cd19087 120 HFD-------------------RDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKaQGIAARRGLLRFVSEQPMYnl 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 189 -FTQ--VKLREFCKEKGIVVVGYSPLG------------NPGSAFFRKDGDPNVL--------TNEVVAGIAKAHGKTPA 245
Cdd:cd19087 181 lKRQaeLEILPAARAYGLGVIPYSPLAgglltgkygkgkRPESGRLVERARYQARygleeyrdIAERFEALAAEAGLTPA 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17537075 246 QIILRWfVDS--GL-SAIPKSVTPQRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19087 261 SLALAW-VLShpAVtSPIIGPRTLEQLEDSLAALEITLTPELLAEID 306
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
43-274 |
5.62e-11 |
|
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: 62.19 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 43 IDCAHVYQNQKEVGEALKEILD--EGKVKREELFITSK----VWNTFH----SEAKAHENIDIILSDLQLSYVDLMLIHW 112
Cdd:cd19082 34 IDTARVYGDWVERGASERVIGEwlKSRGNRDKVVIATKgghpDLEDMSrsrlSPEDIRADLEESLERLGTDYIDLYFLHR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 113 --PQgyaegaelFPAGENgkmrysdVDYLETWkafeaaQKAGKCRSIGLSNFTHSqiqRVWDAAE-------VKPACLQV 183
Cdd:cd19082 114 ddPS--------VPVGEI-------VDTLNEL------VRAGKIRAFGASNWSTE---RIAEANAyakahglPGFAASSP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 184 ---------ELHPYFTQV----KLREFCKEKGIVVVGYSPLGNpGsaFFRK----------------DGDPNVLTNEVVA 234
Cdd:cd19082 170 qwslarpnePPWPGPTLVamdeEMRAWHEENQLPVFAYSSQAR-G--FFSKraaggaeddselrrvyYSEENFERLERAK 246
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17537075 235 GIAKAHGKTPAQIILRWFVDSGLSAIP--KSVTPQRIIENIS 274
Cdd:cd19082 247 ELAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSLA 288
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
55-273 |
1.40e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 60.81 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 55 VGEALKEildegKVKREELFITSKV----------WNTFHSEAKA--HENIDIILSDLQLSYVDLMLIHwpqgyaegael 122
Cdd:cd19752 56 IGRWLKD-----RGNRDDVVIATKVgagprdpdggPESPEGLSAEtiEQEIDKSLRRLGTDYIDLYYAH----------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 123 fpagengkMRYSDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAEVK----PACLQvELHPYF--------- 189
Cdd:cd19752 120 --------VDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQgwaeFSAIQ-QRHSYLrprpgadfg 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 190 TQVKLR----EFCKEKG-IVVVGYSPL--------GNPGSAFFRKDGDPNVLTneVVAGIAKAHGKTPAQIILRWFVDSG 256
Cdd:cd19752 191 VQRIVTdellDYASSRPdLTLLAYSPLlsgaytrpDRPLPEQYDGPDSDARLA--VLEEVAGELGATPNQVVLAWLLHRT 268
|
250
....*....|....*....
gi 17537075 257 LSAIP--KSVTPQRIIENI 273
Cdd:cd19752 269 PAIIPllGASTVEQLEENL 287
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
43-289 |
1.96e-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: 60.70 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 43 IDCAHVYQN---QKEVGEALKEildegkvKREELFITSKVWNTFH--------SEAKA-HENIDIILSDLQLSYVDLMLI 110
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKYTMNRRpgdpnaggNHRKNlRRSVEASLRRLQTDYIDLLYV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 111 HWPQGYAEGAELfpagengkMRysdvdyletwkAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAEVK----PACLQVELH 186
Cdd:cd19080 121 HAWDFTTPVEEV--------MR-----------ALDDLVRAGKVLYVGISDTPAWVVARANTLAELRgwspFVALQIEYS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 187 PYFTQVKlREF---CKEKGIVVVGYSPLG--------NPGS-AFFRKDGDPNVLTN----------EVVAGIAKAHGKTP 244
Cdd:cd19080 182 LLERTPE-RELlpmARALGLGVTPWSPLGgglltgkyQRGEeGRAGEAKGVTVGFGklternwaivDVVAAVAEELGRSA 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17537075 245 AQIILRWfvdsgLSAIPKSVTPqrII---------ENISVIDFQLSAEEIQAID 289
Cdd:cd19080 261 AQVALAW-----VRQKPGVVIP--IIgartleqlkDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
152-288 |
1.69e-09 |
|
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: 57.83 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 152 GKCRSIGLSNFTHSQIQRvwdAAEVKP-ACLQVELHPYFTQVK--LREFCKEKGIVVVGYSPLG------------NPGS 216
Cdd:cd19145 146 GKIKYIGLSEASADTIRR---AHAVHPiTAVQLEWSLWTRDIEeeIIPTCRELGIGIVPYSPLGrgffagkakleeLLEN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 217 AFFRK--------DGDPNVLTNEVVAGIAKAHGKTPAQIILRWFVDSG--LSAIPKSVTPQRIIENISVIDFQLSAEEIQ 286
Cdd:cd19145 223 SDVRKshprfqgeNLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLK 302
|
..
gi 17537075 287 AI 288
Cdd:cd19145 303 EI 304
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
43-286 |
1.51e-08 |
|
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: 54.86 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 43 IDCAHVY-QNQKEV--GEALKEIldegkvKREELFITSKV-------WNTF-HSEAKAHENIDIILSDLQLSYVDLMLIH 111
Cdd:cd19163 50 IDTAPWYgQGRSETvlGKALKGI------PRDSYYLATKVgrygldpDKMFdFSAERITKSVEESLKRLGLDYIDIIQVH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 112 wpqgyaegaelfpagengkmrysDVDYL--------ETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAEVKPACLQV 183
Cdd:cd19163 124 -----------------------DIEFApsldqilnETLPALQKLKEEGKVRFIGITGYPLDVLKEVLERSPVKIDTVLS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 184 ELHpYFTQ----VKLREFCKEKGIVVVGYSPLgnpGSAFFRKDGDPN--VLTNEVVAGIAKA------HGKTPAQIILRW 251
Cdd:cd19163 181 YCH-YTLNdtslLELLPFFKEKGVGVINASPL---SMGLLTERGPPDwhPASPEIKEACAKAaaycksRGVDISKLALQF 256
|
250 260 270
....*....|....*....|....*....|....*....
gi 17537075 252 FVDSglSAIPKSV----TPQRIIENISVIDFQLSAEEIQ 286
Cdd:cd19163 257 ALSN--PDIATTLvgtaSPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-250 |
1.67e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 54.96 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVYQNQK-EV--GEALKEIldegkvkREELFITSKVW--NTFHSEAKAH--ENIDIILSDLQLSYVDLMLIH 111
Cdd:cd19104 45 GINFFDTAPSYGDGKsEEnlGRALKGL-------PAGPYITTKVRldPDDLGDIGGQieRSVEKSLKRLKRDSVDLLQLH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 112 WPQGYAEGAELFPAGEngkmrYSDVDYL-ETWKAFEAAQKAGKCRSIGLSNFTHSQ-IQRV-----WDAAEV-------K 177
Cdd:cd19104 118 NRIGDERDKPVGGTLS-----TTDVLGLgGVADAFERLRSEGKIRFIGITGLGNPPaIRELldsgkFDAVQVyynllnpS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 178 PACLQVELHPYFTQVKLREFCKEKGIVVVGYSPL--GNPGSAFFRKDGDPNVLTNEV---------VAGIAKAHGKTPAQ 246
Cdd:cd19104 193 AAEARPRGWSAQDYGGIIDAAAEHGVGVMGIRVLaaGALTTSLDRGREAPPTSDSDVaidfrraaaFRALAREWGETLAQ 272
|
....
gi 17537075 247 IILR 250
Cdd:cd19104 273 LAHR 276
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
39-160 |
2.72e-08 |
|
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: 54.10 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVYQN-QKEVGEALKEIldegkvKREELFITSKV-----WNTFHSEAKAHENIDIILSDLQLSYVDLMLIHW 112
Cdd:cd19090 33 GINYIDTAPAYGDsEERLGLALAEL------PREPLVLSTKVgrlpeDTADYSADRVRRSVEESLERLGRDRIDLLMIHD 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17537075 113 PQGYAEGAELFPAGengkmrysdvdyleTWKAFEAAQKAGKCRSIGLS 160
Cdd:cd19090 107 PERVPWVDILAPGG--------------ALEALLELKEEGLIKHIGLG 140
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
9-289 |
3.37e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 54.23 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 9 SGYSIPAIGLGTWQSKpGEVAAAIKTAV------AAGYRHIDCAHVY-----QNQKEVGEALKEildEGKVKREELFITS 77
Cdd:PRK09912 21 SGLRLPALSLGLWHNF-GHVNALESQRAilrkafDLGITHFDLANNYgpppgSAEENFGRLLRE---DFAAYRDELIIST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 78 K----VWNTFHSEAKAHE----NIDIILSDLQLSYVDLMLIHwpqgyaegaelfPAGENGKMRysdvdylETWKAFEAAQ 149
Cdd:PRK09912 97 KagydMWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSH------------RVDENTPME-------ETASALAHAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 150 KAGKCRSIGLSNFTHSQIQRVWDAAEVKPACLQVE------LHPYFTQVKLREFCKEKGIVVVGYSPL-----------G 212
Cdd:PRK09912 158 QSGKALYVGISSYSPERTQKMVELLREWKIPLLIHqpsynlLNRWVDKSGLLDTLQNNGVGCIAFTPLaqglltgkylnG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 213 NPGSAFFRKDGD------PNVLTN------EVVAGIAKAHGKTPAQIILRWFV-DSGLSAIPKSVT-PQRIIENISVI-D 277
Cdd:PRK09912 238 IPQDSRMHREGNkvrgltPKMLTEanlnslRLLNEMAQQRGQSMAQMALSWLLkDERVTSVLIGASrAEQLEENVQALnN 317
|
330
....*....|..
gi 17537075 278 FQLSAEEIQAID 289
Cdd:PRK09912 318 LTFSTEELAQID 329
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
8-285 |
6.33e-07 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 50.09 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 8 NSGYSIPAIGLGTWQSKPGEVAAAIKTAVAA-----GYRHIDCAHVY-----QNQKEVGEALKEILdegKVKREELFITS 77
Cdd:cd19151 7 RSGLKLPAISLGLWHNFGDVDRYENSRAMLRrafdlGITHFDLANNYgpppgSAEENFGRILKEDL---KPYRDELIIST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 78 K----VWN----TFHSEAKAHENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQ 149
Cdd:cd19151 84 KagytMWPgpygDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPD-------------------PETPLEETMGALDQIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 150 KAGKCRSIGLSNFTHSQIQRVWDA-AEVKPACLqveLH-PYFTQVK------LREFCKEKGIVVVGYSPL---------- 211
Cdd:cd19151 145 RQGKALYVGISNYPPEEAREAAAIlKDLGTPCL---IHqPKYSMFNrwveegLLDVLEEEGIGCIAFSPLaqglltdryl 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 212 -GNP-------GSAFFRKDGdpnvLTNEVVA------GIAKAHGKTPAQIILRWFVDSG--LSAIPKSVTPQRIIENISV 275
Cdd:cd19151 222 nGIPedsraakGSSFLKPEQ----ITEEKLAkvrrlnEIAQARGQKLAQMALAWVLRNKrvTSVLIGASKPSQIEDAVGA 297
|
330
....*....|.
gi 17537075 276 ID-FQLSAEEI 285
Cdd:cd19151 298 LDnREFSEEEL 308
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-289 |
9.02e-07 |
|
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: 49.64 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 44 DCAHVY---QNQKEVGEALKEIldegkvKREELFITSKvwntF------HSEAKAHENIDIILSDLQLSYVDLMLIHWPq 114
Cdd:cd19103 50 DTAAVYgmgASEKILGEFLKRY------PREDYIISTK----FtpqiagQSADPVADMLEGSLARLGTDYIDIYWIHNP- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 115 gyaegaelfpagengkmrySDVdylETWKAFEAA-QKAGKCRSIGLSNFTHSQIQRV---WDAAEVKPACLQVE---LHP 187
Cdd:cd19103 119 -------------------ADV---ERWTPELIPlLKSGKVKHVGVSNHNLAEIKRAneiLAKAGVSLSAVQNHyslLYR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 188 YFTQVKLREFCKEKGIVVVGYSPL------GNPGSAFFRKDGDPNVLT-----------NEVVAGIAKAHGKTPAQIILR 250
Cdd:cd19103 177 SSEEAGILDYCKENGITFFAYMVLeqgalsGKYDTKHPLPEGSGRAETynpllpqleelTAVMAEIGAKHGASIAQVAIA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17537075 251 WfvdsglsAIPKSVTP-------QRIIENISVIDFQLSAEEIQAID 289
Cdd:cd19103 257 W-------AIAKGTTPiigvtkpHHVEDAARAASITLTDDEIKELE 295
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
9-291 |
1.28e-06 |
|
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: 49.27 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 9 SGYSIPAIGLGTWQSKPGEVAAAIKT-----AVAAGYRHIDCAHVYQNQK-EVgeALKEILDEGKVKREELFITSKVW-- 80
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAAGKaEV--ILGSIIKKKGWRRSSLVITTKLYwg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 81 ---NTFHSEAKAH--ENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagENGKMRysdvdylETWKAFEAAQKAGKCR 155
Cdd:cd19159 87 gkaETERGLSRKHiiEGLKGSLQRLQLEYVDVVFANRPD------------SNTPME-------EIVRAMTHVINQGMAM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 156 SIGLSNFTHSQIQRVWDAAE----VKPACLQVELHPY---FTQVKLREFCKEKGIVVVGYSPL-----------GNPGSA 217
Cdd:cd19159 148 YWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFqreKVEVQLPELYHKIGVGAMTWSPLacgiisgkygnGVPESS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 218 -------------FFRKDGDPNVLTNEVVAGIAKAHGKTPAQIILRWFV-DSGLSAI-PKSVTPQRIIENISVIDF--QL 280
Cdd:cd19159 228 raslkcyqwlkerIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLrNEGVSSVlLGSSTPEQLIENLGAIQVlpKM 307
|
330
....*....|.
gi 17537075 281 SAEEIQAIDGV 291
Cdd:cd19159 308 TSHVVNEIDNI 318
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
44-291 |
3.91e-05 |
|
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: 44.51 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 44 DCAHVYQN-QKEV--GEALKEildeGKVKREELFITSKV-W------NTFHSEAKAH--ENIDIILSDLQLSYVDLMLIH 111
Cdd:cd19143 49 DNAEVYANgQSEEimGQAIKE----LGWPRSDYVVSTKIfWggggppPNDRGLSRKHivEGTKASLKRLQLDYVDLVFCH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 112 WPQgyaegaelfpagengkmrySDVDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAE----VKPACLQVE--- 184
Cdd:cd19143 125 RPD-------------------PATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQynl 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 185 LHPYFTQVKLREFCKEKGIVVVGYSPL-------------------GNPGSAFFRKDGDPNVLTN-EVV---AGIAKAHG 241
Cdd:cd19143 186 FHRERVEVEYAPLYEKYGLGTTTWSPLasglltgkynngipegsrlALPGYEWLKDRKEELGQEKiEKVrklKPIAEELG 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17537075 242 KTPAQIILRWFVD----SglSAIPKSVTPQRIIENISVIDF--QLSAEEIQAIDGV 291
Cdd:cd19143 266 CSLAQLAIAWCLKnpnvS--TVITGATKVEQLEENLKALEVlpKLTPEVMEKIEAI 319
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
9-291 |
7.32e-05 |
|
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: 43.92 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 9 SGYSIPAIGLGTWQSKPGEVAAAIKTAVAA-----GYRHIDCAHVYQNQK-EVgeALKEILDEGKVKREELFITSKVW-- 80
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGQITDEMAEHLMTlaydnGINLFDTAEVYAAGKaEV--VLGNIIKKKGWRRSSLVITTKIFwg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 81 ---NTFHSEAKAH--ENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagENGKMRysdvdylETWKAFEAAQKAGKCR 155
Cdd:cd19158 87 gkaETERGLSRKHiiEGLKASLERLQLEYVDVVFANRPD------------PNTPME-------ETVRAMTHVINQGMAM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 156 SIGLSNFTHSQIQRVWDAAE----VKPACLQVELHPY---FTQVKLREFCKEKGIVVVGYSPLG--------NPGSAFFR 220
Cdd:cd19158 148 YWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFqreKVEVQLPELFHKIGVGAMTWSPLAcgivsgkyDSGIPPYS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 221 KDG-------DPNVLTNE---------VVAGIAKAHGKTPAQIILRWFV-DSGLSAIPKSVT-PQRIIENISVIDF--QL 280
Cdd:cd19158 228 RASlkgyqwlKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLrNEGVSSVLLGASnAEQLMENIGAIQVlpKL 307
|
330
....*....|.
gi 17537075 281 SAEEIQAIDGV 291
Cdd:cd19158 308 SSSIVHEIDSI 318
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
9-285 |
1.22e-04 |
|
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: 43.21 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 9 SGYSIPAIGLGTWQS----KPGEVAAAIKTAV-AAGYRHIDCAHVY-----QNQKEVGEALKEILdegKVKREELFITSK 78
Cdd:cd19150 8 SGLKLPALSLGLWHNfgddTPLETQRAILRTAfDLGITHFDLANNYgpppgSAEENFGRILREDF---AGYRDELIISTK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 79 ----VWNTFHSEAKAHENI----DIILSDLQLSYVDLMLIHwpqgyaegaelfpagengkmRYS-DVDYLETWKAFEAAQ 149
Cdd:cd19150 85 agydMWPGPYGEWGSRKYLlaslDQSLKRMGLDYVDIFYSH--------------------RFDpDTPLEETMGALDHAV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 150 KAGKCRSIGLSNFTHSQIQRVWDA-AEVKPACLQVE-----LHPYFTQVKLREFCKEKGIVVVGYSPL-----------G 212
Cdd:cd19150 145 RSGKALYVGISSYSPERTREAAAIlRELGTPLLIHQpsynmLNRWVEESGLLDTLQELGVGCIAFTPLaqglltdkylnG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 213 NPGSAFFRKDGD--PNVLTNEVVA------GIAKAHGKTPAQIILRWFVDSG--LSAIPKSVTPQRIIENISVID-FQLS 281
Cdd:cd19150 225 IPEGSRASKERSlsPKMLTEANLNsiralnEIAQKRGQSLAQMALAWVLRDGrvTSALIGASRPEQLEENVGALDnLTFS 304
|
....
gi 17537075 282 AEEI 285
Cdd:cd19150 305 ADEL 308
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
9-111 |
2.40e-04 |
|
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: 42.07 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 9 SGYSIPAIGLGTWQSKPGEVAAAIKTAVAA-----GYRHIDCAHVYQNQK-EVgeALKEILDEGKVKREELFITSKV-WN 81
Cdd:cd19142 9 SGLRVSNVGLGTWSTFSTAISEEQAEEIVTlayenGINYFDTSDAFTSGQaET--ELGRILKKKGWKRSSYIVSTKIyWS 86
|
90 100 110
....*....|....*....|....*....|....*
gi 17537075 82 TFHSEA---KAH--ENIDIILSDLQLSYVDLMLIH 111
Cdd:cd19142 87 YGSEERglsRKHiiESVRASLRRLQLDYIDIVIIH 121
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
39-212 |
1.44e-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: 39.83 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVYQN---QKEVGEALKEIldegKVKREELFITSKVW----NTFHSEAKA-HENIDIILSDLQLSYVDLMLI 110
Cdd:cd19153 46 GINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVGryrdSEFDYSAERvRASVATSLERLHTTYLDVVYL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 111 HwpqgYAEGAELFPagengkmrysdvDYLETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDaaEVKPACLQVEL---HP 187
Cdd:cd19153 122 H----DIEFVDYDT------------LVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATR--RCSPGSLDAVLsycHL 183
|
170 180
....*....|....*....|....*....
gi 17537075 188 YFTQVKL----REFCKEKGIVVVGYSPLG 212
Cdd:cd19153 184 TLQDARLesdaPGLVRGAGPHVINASPLS 212
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
39-215 |
2.31e-03 |
|
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: 38.88 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 39 GYRHIDCAHVY---QNQKEVGEALKeildegKVKREELFITSKV------------------WNtfHSEAKAHENIDIIL 97
Cdd:cd19162 32 GIRYFDTAPLYglgLSERRLGAALA------RHPRAEYVVSTKVgrllepgaagrpagadrrFD--FSADGIRRSIEASL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 98 SDLQLSYVDLMLIHWPQGYAEGAelfpagengkmrysdVDylETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDAAEVK 177
Cdd:cd19162 104 ERLGLDRLDLVFLHDPDRHLLQA---------------LT--DAFPALEELRAEGVVGAIGVGVTDWAALLRAARRADVD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17537075 178 pACLQVELHPYFTQVKLREF---CKEKGIVVVGYSPLgNPG 215
Cdd:cd19162 167 -VVMVAGRYTLLDRRAATELlplCAAKGVAVVAAGVF-NSG 205
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
52-211 |
7.49e-03 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 37.45 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 52 QKEVGEALKEIldegKVKREELFITSKVW---NTFH-SEAKAHENIDIILSDLQLSYVDLMLIHwpqgyaegaelfpage 127
Cdd:PLN02587 60 EKVLGKALKAL----GIPREKYVVSTKCGrygEGFDfSAERVTKSVDESLARLQLDYVDILHCH---------------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 128 ngKMRYSDVDYL--ETWKAFEAAQKAGKCRSIGLSNFTHSQIQRVWDaaEVKPACLQVEL---HPYF---TQVKLREFCK 199
Cdd:PLN02587 120 --DIEFGSLDQIvnETIPALQKLKESGKVRFIGITGLPLAIFTYVLD--RVPPGTVDVILsycHYSLndsSLEDLLPYLK 195
|
170
....*....|..
gi 17537075 200 EKGIVVVGYSPL 211
Cdd:PLN02587 196 SKGVGVISASPL 207
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
9-211 |
8.41e-03 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 37.43 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 9 SGYSIPAIGLGTWQSKPGEVAAAIKTAV-----AAGYRHIDCAHVYQNQK-EVgeALKEILDEGKVKREELFITSKVWNT 82
Cdd:cd19141 8 SGLRVSCLGLGTWVTFGSQISDEVAEELvtlayENGINLFDTAEVYAAGKaEI--VLGKILKKKGWRRSSYVITTKIFWG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537075 83 FHSE-----AKAH--ENIDIILSDLQLSYVDLMLIHWPQgyaegaelfpagENGKMRysdvdylETWKAFEAAQKAGKCR 155
Cdd:cd19141 86 GKAEterglSRKHiiEGLKASLERLQLEYVDIVFANRPD------------PNTPME-------EIVRAFTHVINQGMAM 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537075 156 SIGLSNFTHSQIQRVWDAAE----VKPACLQVELHpYF----TQVKLREFCKEKGIVVVGYSPL 211
Cdd:cd19141 147 YWGTSRWSAMEIMEAYSVARqfnlIPPIVEQAEYH-LFqrekVEMQLPELFHKIGVGAMTWSPL 209
|
|
| |
