|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-312 |
0e+00 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 662.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 8 LHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKAVPREELFVTSKLWNTKHH 87
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 88 PEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVKALGLSNFNSR 167
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 168 QIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWRHPDEPVLLEEPVVLALAEKHGRSPAQ 247
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSPAQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10946870 248 ILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVPMITVDGKRVPR 312
Cdd:cd19106 241 ILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVPMITVDGKRVPR 305
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
4-299 |
2.56e-144 |
|
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: 408.72 E-value: 2.56e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 4 SSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKaVPREELFVTSKLWN 83
Cdd:cd19123 2 KTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGK-VKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGdNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVKALGLSN 163
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 164 FNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDR--AWRHPDEPVLLEEPVVLALAEKH 241
Cdd:cd19123 160 FSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRpaAMKAEGEPVLLEDPVINKIAEKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 10946870 242 GRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYI 299
Cdd:cd19123 240 GASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
14-290 |
4.64e-141 |
|
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: 398.78 E-value: 4.64e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 14 MPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVgsgkaVPREELFVTSKLWNTKHHPEDVEP 93
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG-----VPREELFITTKLWPTDHGYERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 94 ALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPknadgtvrydsthYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVL 173
Cdd:cd19071 76 ALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEA-------------RLETWRALEELVDEGLVRSIGVSNFNVEHLEELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 174 SVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRawrhpdepVLLEEPVVLALAEKHGRSPAQILLRWQ 253
Cdd:cd19071 143 AAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR--------PLLDDPVLKEIAKKYGKTPAQVLLRWA 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 10946870 254 VQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLD 290
Cdd:cd19071 215 LQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
11-325 |
5.89e-141 |
|
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: 400.64 E-value: 5.89e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 11 GQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVgSGKAVPREELFVTSKLWNTKHHPED 90
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKI-KEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 91 VEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVKALGLSNFNSRQID 170
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 171 DVLSVASVR--PAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWRHPDEPVLLEEPVVLALAEKHGRSPAQI 248
Cdd:cd19107 160 RILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10946870 249 LLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVpmitvdgkrVPRDAGHPLYPFNDPY 325
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACA---------LLSCSSHKDYPFHAEY 307
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-301 |
9.10e-134 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 380.55 E-value: 9.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 11 GQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNTKHHPED 90
Cdd:COG0656 2 GVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS-----GVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 91 VEPALRKTLADLQLEYLDLYLMHWPYafergdnpfpknadgtvrydSTHYKETWKALEVLVAKGLVKALGLSNFNSRQID 170
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPG--------------------PGPYVETWRALEELYEEGLIRAIGVSNFDPEHLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 171 DVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdepvLLEEPVVLALAEKHGRSPAQILL 250
Cdd:COG0656 137 ELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQVVL 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 10946870 251 RWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVP 301
Cdd:COG0656 207 RWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLGPD 257
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
5-299 |
1.30e-133 |
|
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: 381.24 E-value: 1.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 5 SVLLHTGQKMPLIGLGTWKS-EPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKaVPREELFVTSKLWN 83
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGV-VKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAF-ERGDNpfpkNADGTVRYDSTHYKETWKALEVLVAKGLVKALGLS 162
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFkENNDS----ESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 163 NFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAwRHPDEPVLLEEPVVLALAEKHG 242
Cdd:cd19116 157 NFNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPR-GQTNPPPRLDDPTLVAIAKKYG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 10946870 243 RSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYI 299
Cdd:cd19116 236 KTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-290 |
4.52e-131 |
|
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: 374.76 E-value: 4.52e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 8 LHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGkAVPREELFVTSKLWNTKHH 87
Cdd:cd19125 5 LNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDG-VVKREDLFITSKLWCTDHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 88 PEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDnPFPKNADgtvrYDSTHYKETWKALEVLVAKGLVKALGLSNFNSR 167
Cdd:cd19125 84 PEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA-HMPEPEE----VLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 168 QIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWRHPDepvLLEEPVVLALAEKHGRSPAQ 247
Cdd:cd19125 159 KLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKLGKTPAQ 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 10946870 248 ILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLD 290
Cdd:cd19125 236 VALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFS 278
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
3-297 |
1.42e-128 |
|
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: 369.05 E-value: 1.42e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 3 ASSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKaVPREELFVTSKLW 82
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGV-VKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 NTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVKALGLS 162
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 163 NFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWRHPD-----EPVLLEEPVVLAL 237
Cdd:cd19154 160 NFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKStgvspAPNLLQDPIVKAI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 238 AEKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWR 297
Cdd:cd19154 240 AEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-292 |
4.12e-120 |
|
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: 346.71 E-value: 4.12e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 8 LHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKAVPREELFVTSKLWNTKHH 87
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 88 PEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGT----VRYD-STHYKETWKALEVLVAKGLVKALGLS 162
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLTAVPTnggeVDLDlSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 163 NFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAwrhpdEPVLLEEPVVLALAEKHG 242
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLAG-----LPLLVQHPEVKAIAAKLG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 10946870 243 RSPAQILLRWQVQRKVICIPKSINPSRILQNIQvfDFTFSPEEMKQLDAL 292
Cdd:cd19118 236 KTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
5-299 |
2.13e-119 |
|
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: 345.75 E-value: 2.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 5 SVLLHTGQKMPLIGLGTWKSE---PGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGkAVPREELFVTSKL 81
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPEevpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADG-TVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVKALGL 161
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 162 SNFNSRQIDDVLSVASV--RPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSS-DRAWRHPDEPVLLEEPVVLALA 238
Cdd:cd19108 161 SNFNRRQLEMILNKPGLkyKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10946870 239 EKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYI 299
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-297 |
1.69e-117 |
|
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: 341.04 E-value: 1.69e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 4 SSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKaVPREELFVTSKLWN 83
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGK-VKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFE-RGDNPFPKNADGTVRYD-STHYKETWKALEVLVAKGLVKALGL 161
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 162 SNFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWRHP-------DEPVLLEEPVV 234
Cdd:cd19155 161 SNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10946870 235 LALAEKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWR 297
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-300 |
2.04e-115 |
|
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: 335.24 E-value: 2.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 11 GQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKaVPREELFVTSKLWNTKHHPED 90
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGK-LKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 91 VEPALRKTLADLQLEYLDLYLMHWPYAFE-RGDNPFPKNAdgtvrydSTHYKETWKALEVLVAKGLVKALGLSNFNSRQI 169
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVnKKDKGERELA-------SSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 170 DDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRA--WRHPDEPVLLEEPVVLALAEKHGRSPAQ 247
Cdd:cd19111 153 NKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPAQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 10946870 248 ILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIV 300
Cdd:cd19111 233 VLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFD 285
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
11-321 |
1.93e-114 |
|
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: 333.30 E-value: 1.93e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 11 GQKMPLIGLGTW----KSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKaVPREELFVTSKLWNTKH 86
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGK-VKREDIFYCGKLWNTCH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 87 HPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVKALGLSNFNS 166
Cdd:cd19109 80 PPELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 167 RQIDDVLSVASV--RPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSS-DRAWRHPDEPVLLEEPVVLALAEKHGR 243
Cdd:cd19109 160 RQLELILNKPGLkhKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10946870 244 SPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVPMITVDgkrvprdagHPLYPF 321
Cdd:cd19109 240 TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRD---------HPEYPF 308
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-325 |
1.47e-112 |
|
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: 328.46 E-value: 1.47e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 12 QKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGkAVPREELFVTSKLWNTKHHPEDV 91
Cdd:cd19110 2 EDIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEG-VVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 92 EPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVKALGLSNFNSRQIDD 171
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 172 VLSVAS--VRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWRhpdepvLLEEPVVLALAEKHGRSPAQIL 249
Cdd:cd19110 161 LLNKPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVD------LIDDPVIQRIAKKHGKSPAQIL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10946870 250 LRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVpmitvdgkrVPRDAGHPLYPFNDPY 325
Cdd:cd19110 235 IRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLAT---------FPITENHKDYPFHIEY 301
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
5-298 |
1.48e-106 |
|
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: 311.63 E-value: 1.48e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 5 SVLLHTGQKMPLIGLGTWKSEPGQ-VKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWN 83
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKES-----GIPREELFITSKVWN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknadgtvryDSTHYKETWKALEVLVAKGLVKALGLSN 163
Cdd:cd19157 76 ADQGYDSTLKAFEASLERLGLDYLDLYLIHWP--------------------VKGKYKETWKALEKLYKDGRVRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 164 FNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdepvLLEEPVVLALAEKHGR 243
Cdd:cd19157 136 FQVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEKYNK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 10946870 244 SPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRY 298
Cdd:cd19157 206 SVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
2-298 |
4.66e-106 |
|
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: 312.05 E-value: 4.66e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 2 TASSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGkAVPREELFVTSKL 81
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEG-IVKREDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDnP---FP---KNADGTVRYDSTHYKETWKALEVLVAKGL 155
Cdd:cd19115 80 WNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVD-PavrYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 156 VKALGLSNFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLG-SSDRAWRHP---DEPVLLEE 231
Cdd:cd19115 159 ARSIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpQSFLELDLPgakDTPPLFEH 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10946870 232 PVVLALAEKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRY 298
Cdd:cd19115 239 DVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
14-292 |
1.40e-103 |
|
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: 304.17 E-value: 1.40e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 14 MPLIGLGTWK---SEpgQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvGSGKAVPREELFVTSKLWNTKHHPED 90
Cdd:cd19136 1 MPILGLGTFRlrgEE--EVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDL-LPKYGLSREDIFITSKLAPKDQGYEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 91 VEPALRKTLADLQLEYLDLYLMHWP-YAFERGDNPfpKNADgtVRydsthyKETWKALEVLVAKGLVKALGLSNFNSRQI 169
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHWPgVQGLKPSDP--RNAE--LR------RESWRALEDLYKEGKLRAIGVSNYTVRHL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 170 DDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdePVLLEEPVVLALAEKHGRSPAQIL 249
Cdd:cd19136 148 EELLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD--------LRLLEDPTVLAIAKKYGRTPAQVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 10946870 250 LRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDAL 292
Cdd:cd19136 220 LRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
6-293 |
1.12e-101 |
|
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: 299.10 E-value: 1.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 6 VLLHTGQKMPLIGLGTWK-SEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNT 84
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKS-----GIPREELFITTKLWIQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYaferGDnpfpknadgtvrydsthYKETWKALEVLVAKGLVKALGLSNF 164
Cdd:cd19133 76 DAGYEKAKKAFERSLKRLGLDYLDLYLIHQPF----GD-----------------VYGAWRAMEELYKEGKIRAIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 165 NSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAwrhpdepvLLEEPVVLALAEKHGRS 244
Cdd:cd19133 135 YPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN--------LFENPVLTEIAEKYGKS 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 10946870 245 PAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALN 293
Cdd:cd19133 207 VAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-294 |
2.95e-101 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 299.03 E-value: 2.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 8 LHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNTKHH 87
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDS-----GVPREEIFITTKLWCTWHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 88 peDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDSTHYK--ETWKALEVLVAKGLVKALGLSNFN 165
Cdd:cd19117 83 --RVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKDHEPDWDfiKTWELMQKLPATGKVKAIGVSNFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 166 SRQIDDVLS--VASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAwrhpdepvLLEEPVVLALAEKHGR 243
Cdd:cd19117 161 IKNLEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 10946870 244 SPAQILLRWQVQRKVICIPKSINPSRILQNIQVfdFTFSPEEMKQLDALNK 294
Cdd:cd19117 233 TPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
10-292 |
5.01e-101 |
|
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: 298.41 E-value: 5.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLGTWKS--EPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKAVPREELFVTSKLWNTKHH 87
Cdd:cd19124 1 SGQTMPVIGMGTASDppSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 88 PEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDsthYKETWKALEVLVAKGLVKALGLSNFNSR 167
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPFD---IKGVWEAMEECQRLGLTKAIGVSNFSCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 168 QIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWrhpDEPVLLEEPVVLALAEKHGRSPAQ 247
Cdd:cd19124 158 KLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKW---GSNAVMESDVLKEIAAAKGKTVAQ 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 10946870 248 ILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDAL 292
Cdd:cd19124 235 VSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
4-298 |
1.17e-100 |
|
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: 298.59 E-value: 1.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 4 SSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGkAVPREELFVTSKLWN 83
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEG-LVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAF------ERGDNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVK 157
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFkfvpieEKYPPGFYCGDGDNFVYEDVPILDTWKALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 158 ALGLSNFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLG-SSDRAWRHP---DEPVLLEEPV 233
Cdd:cd19113 160 SIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpQSFVELNQGralNTPTLFEHDT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10946870 234 VLALAEKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRY 298
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
3-292 |
3.42e-100 |
|
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: 295.98 E-value: 3.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 3 ASSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGkaVPREELFVTSKLW 82
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG--VKREDLFVTTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 NTKHhpEDVEPALRKTLADLQLEYLDLYLMHWPYAF--ERGDNPFPKNADGTVRYDST-HYKETWKALEVLVAKGLVKAL 159
Cdd:cd19121 79 STYH--RRVELCLDRSLKSLGLDYVDLYLVHWPVLLnpNGNHDLFPTLPDGSRDLDWDwNHVDTWKQMEKVLKTGKTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 160 GLSNFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAwrhpdepvLLEEPVVLALAE 239
Cdd:cd19121 157 GVSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEIAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 10946870 240 KHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTfsPEEMKQLDAL 292
Cdd:cd19121 229 KHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
6-293 |
6.85e-100 |
|
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: 294.35 E-value: 6.85e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 6 VLLHTGQKMPLIGLGTWKSEPG-QVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNT 84
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRES-----GVPREELFVTTKLWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnpfpknadgtvrydsTHYKETWKALEVLVAKGLVKALGLSNF 164
Cdd:cd19126 76 DQRARRTEDAFQESLDRLGLDYVDLYLIHWPGK--------------------DKFIDTWKALEKLYASGKVKAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 165 NSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSdrawrhpdepVLLEEPVVLALAEKHGRS 244
Cdd:cd19126 136 QEHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----------GLLSNPVLAAIGEKYGKS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 10946870 245 PAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALN 293
Cdd:cd19126 206 AAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-301 |
1.79e-99 |
|
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: 295.55 E-value: 1.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 4 SSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGkAVPREELFVTSKLWN 83
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTG-LVKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 84 TKHhpEDVEPALRKTLADLQLEYLDLYLMHWPYAFER---GDNPFPKNADGTVRYDST-HYKETWKALEVLVAKGLVKAL 159
Cdd:cd19112 80 SDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLDIDVTiSLETTWHAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 160 GLSNFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLG--SSDRAWRHPDEPvlLEEPVVLAL 237
Cdd:cd19112 158 GISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWFGSVSP--LDDPVLKDL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10946870 238 AEKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVP 301
Cdd:cd19112 236 AKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQP 299
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
6-292 |
5.71e-96 |
|
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: 284.99 E-value: 5.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 6 VLLHTGQKMPLIGLGTWKSEpGQVKAAIKHALS-AGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNT 84
Cdd:cd19135 5 VRLSNGVEMPILGLGTSHSG-GYSHEAVVYALKeCGYRHIDTAKRYGCEELLGKAIKES-----GVPREDLFLTTKLWPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnPFPKNADGTVRydsthyKETWKALEVLVAKGLVKALGLSNF 164
Cdd:cd19135 79 DYGYESTKQAFEASLKRLGVDYLDLYLLHWPDC------PSSGKNVKETR------AETWRALEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 165 NSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSsdraWRhpdepvLLEEPVVLALAEKHGRS 244
Cdd:cd19135 147 LIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAK----GK------ALEEPTVTELAKKYQKT 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 10946870 245 PAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDAL 292
Cdd:cd19135 217 PAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-293 |
4.25e-95 |
|
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: 282.34 E-value: 4.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 5 SVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNT 84
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRAS-----GVPREELFITTKLWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknadgTVRYDstHYKETWKALEVLVAKGLVKALGLSNF 164
Cdd:cd19131 76 DQGYDSTLRAFDESLRKLGLDYVDLYLIHWP----------------VPAQD--KYVETWKALIELKKEGRVKSIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 165 NSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdepvLLEEPVVLALAEKHGRS 244
Cdd:cd19131 138 TIEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG----------LLSDPVIGEIAEKHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 10946870 245 PAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALN 293
Cdd:cd19131 208 PAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-293 |
5.38e-95 |
|
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: 282.37 E-value: 5.38e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 8 LHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNTKHH 87
Cdd:cd19127 3 LNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS-----GVDRSDIFVTTKLWISDYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 88 PEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpFPKNADGTVrydsthykETWKALEVLVAKGLVKALGLSNFNSR 167
Cdd:cd19127 78 YDKALRGFDASLRRLGLDYVDLYLLHWP---------VPNDFDRTI--------QAYKALEKLLAEGRVRAIGVSNFTPE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 168 QIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWR-HPDEPV-LLEEPVVLALAEKHGRSP 245
Cdd:cd19127 141 HLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGAsGPTGPGdVLQDPTITGLAEKYGKTP 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 10946870 246 AQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALN 293
Cdd:cd19127 221 AQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-285 |
1.98e-94 |
|
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: 282.04 E-value: 1.98e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKaVPREELFVTSKLWNTKHHP 88
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGK-IRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 89 EDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDS-THYKETWKALEVLVAKGLVKALGLSNFNSR 167
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 168 QIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGssdrawrHPDEPVLLEEPVVLALAEKHGRSPAQ 247
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG-------HGMEPKLLEDPVITAIARRVNKTPAQ 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 10946870 248 ILLRWQVQRKVICIPKSINPSRILQNiqvFDFTFSPEE 285
Cdd:cd19129 233 VLLAWAIQRGTALLTTSKTPSRIREN---FDISTLPED 267
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
9-292 |
1.06e-93 |
|
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: 278.76 E-value: 1.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNTKHHP 88
Cdd:cd19140 3 VNGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAAS-----GVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 89 EDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpkNADGTVRydsthykETWKALEVLVAKGLVKALGLSNFNSRQ 168
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWP------------NKDVPLA-------ETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 169 IDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdepvLLEEPVVLALAEKHGRSPAQI 248
Cdd:cd19140 139 LREAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE----------VLKDPVLQEIGRKHGKTPAQV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 10946870 249 LLRWQVQR-KVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDAL 292
Cdd:cd19140 209 ALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-294 |
1.27e-93 |
|
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: 279.41 E-value: 1.27e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 15 PLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGkAVPREELFVTSKLWNTKHHPEDVEPA 94
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDG-GVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 95 LRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVLS 174
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 175 VASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRawrhPDEPVLLEEPVVLALAEKHGRSPAQILLRWQV 254
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYG----DGNLTFLNDSELKALATKYNTTPPQVIIAWHL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 10946870 255 QR---KVICIPKSINPSRILQNIQVFDFTFSPEEMkqlDALNK 294
Cdd:cd19128 237 QKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDM---DAINT 276
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
6-298 |
3.28e-92 |
|
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: 275.55 E-value: 3.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 6 VLLHTGQKMPLIGLGTWKSEPGQVKA-AIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNT 84
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES-----GVPREEVFVTTKLWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnpfpknadgtvrydsTHYKETWKALEVLVAKGLVKALGLSNF 164
Cdd:cd19156 76 DQGYESTLAAFEESLEKLGLDYVDLYLIHWPVK--------------------GKFKDTWKAFEKLYKEKKVRAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 165 NSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdepvLLEEPVVLALAEKHGRS 244
Cdd:cd19156 136 HEHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKYGKS 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 10946870 245 PAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRY 298
Cdd:cd19156 206 AAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
14-290 |
1.45e-91 |
|
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: 272.99 E-value: 1.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 14 MPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNTKHHPEDVEP 93
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES-----GVPREDLFITTKVWRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 94 ALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgtvrydSTHYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVL 173
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLIHWP-------NP------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 174 SVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdepvLLEEPVVLALAEKHGRSPAQILLRWQ 253
Cdd:cd19073 137 DISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE----------VLRDPVIQEIAEKYDKTPAQVALRWL 206
|
250 260 270
....*....|....*....|....*....|....*..
gi 10946870 254 VQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLD 290
Cdd:cd19073 207 VQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-303 |
4.33e-89 |
|
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: 268.66 E-value: 4.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 11 GQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGkAVPREELFVTSKLWNTKHHPED 90
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEG-LVKREDLFIVTKLWNNFHGKDH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 91 VEPALRKTLADLQLEYLDLYLMHWPYAFERGD---NPFPKNADGTVR---YDSTHYKETWKALEVLVAKGLVKALGLSNF 164
Cdd:cd19114 80 VREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaeNYPFLWKDKELKkfpLEQSPMQECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 165 NSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSS--DRAWRHPDE-PVLLEEPVVLALAEKH 241
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvyTKVTKHLKHfTNLLEHPVVKKLADKH 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10946870 242 GRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVPMI 303
Cdd:cd19114 240 KRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPVV 301
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
11-298 |
1.23e-88 |
|
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: 266.41 E-value: 1.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 11 GQKMPLIGLGT----WKSEPG--QVKA--AIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLW 82
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDdiQRDLvdSVKLALKAGFRHIDTAEMYGNEKEVGEALKES-----GVPREDLFITTKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 ntkHHPEDVEPALRKTLADLQLEYLDLYLMHWPYafergdnpFPKNADGTVRydsthykETWKALEVLVAKGLVKALGLS 162
Cdd:cd19120 76 ---PGIKDPREALRKSLAKLGVDYVDLYLIHSPF--------FAKEGGPTLA-------EAWAELEALKDAGLVRSIGVS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 163 NFNSRQIDDVLSVASVRPAVLQVECHPYLA--QNELIAHCHARGLEVTAYSPLGSsdrAWRHPDEPVlleEPVVLALAEK 240
Cdd:cd19120 138 NFRIEDLEELLDTAKIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSP---LTRDAGGPL---DPVLEKIAEK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 10946870 241 HGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRY 298
Cdd:cd19120 212 YGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-293 |
1.83e-85 |
|
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: 257.58 E-value: 1.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 8 LHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNTKHH 87
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRS-----GVPREELFVTTKLPGRHHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 88 PEDVEPALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgtvRYDSthYKETWKALEVLVAKGLVKALGLSNFNSR 167
Cdd:cd19132 76 YEEALRTIEESLYRLGLDYVDLYLIHWP-------NP---------SRDL--YVEAWQALIEAREEGLVRSIGVSNFLPE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 168 QIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRawrhpdepvLLEEPVVLALAEKHGRSPAQ 247
Cdd:cd19132 138 HLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 10946870 248 ILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALN 293
Cdd:cd19132 209 VVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-292 |
7.84e-84 |
|
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: 255.11 E-value: 7.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 5 SVLLHTGQKMPLIGLGTW--KSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKaVPREELFVTSKLW 82
Cdd:cd19119 3 SFKLNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGS-IKREELFITTKVW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 NTKHhpEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNP-----FPKNADGTVRY-DSTHYKETWKALEVLVAKGLV 156
Cdd:cd19119 82 PTFY--DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDsgkpfTPVNDDGKTRYaASGDHITTYKQLEKIYLDGRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 157 KALGLSNFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSdrawRHPdepvLLEEPVVLA 236
Cdd:cd19119 160 KAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSH----GAP----NLKNPLVKK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 10946870 237 LAEKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTfsPEEMKQLDAL 292
Cdd:cd19119 232 IAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLT--KEDLQKLDDI 285
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-297 |
8.59e-79 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 241.52 E-value: 8.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 8 LHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNTKHH 87
Cdd:PRK11565 9 LQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA-----SVAREELFITTKLWNDDHK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 88 peDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnpfPKNadgtvrydstHYKETWKALEVLVAKGLVKALGLSNFNSR 167
Cdd:PRK11565 84 --RPREALEESLKKLQLDYVDLYLMHWPVP--------AID----------HYVEAWKGMIELQKEGLIKSIGVCNFQIH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 168 QIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAwrhpdepvLLEEPVVLALAEKHGRSPAQ 247
Cdd:PRK11565 144 HLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG--------VFDQKVIRDLADKYGKTPAQ 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 10946870 248 ILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWR 297
Cdd:PRK11565 216 IVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-298 |
4.24e-78 |
|
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: 239.37 E-value: 4.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 5 SVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNT 84
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS-----GIPRGELFVTTKLATP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnpfpknadgtvryDSTHYKETWKALEVLVAKGLVKALGLSNF 164
Cdd:cd19134 77 DQGFTASQAACRASLERLGLDYVDLYLIHWPAG------------------REGKYVDSWGGLMKLREEGLARSIGVSNF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 165 NSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdepvLLEEPVVLALAEKHGRS 244
Cdd:cd19134 139 TAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR----------LLDNPAVTAIAAAHGRT 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 10946870 245 PAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRY 298
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
5-293 |
2.86e-76 |
|
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: 234.42 E-value: 2.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 5 SVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALkesvgSGKAVPREELFVTSKLWNT 84
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI-----AASGIPRDELFVTTKLWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPyAFERGDnpfpknadgtvrydsthYKETWKALEVLVAKGLVKALGLSNF 164
Cdd:cd19130 76 RHDGDEPAAAFAESLAKLGLDQVDLYLVHWP-TPAAGN-----------------YVHTWEAMIELRAAGRTRSIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 165 NSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdepvLLEEPVVLALAEKHGRS 244
Cdd:cd19130 138 LPPHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK----------LLGDPPVGAIAAAHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 10946870 245 PAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALN 293
Cdd:cd19130 208 PAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-280 |
4.20e-74 |
|
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: 230.20 E-value: 4.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 8 LHTGQKMPLIGLGTWKSE--PGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKAVPREELFVTSKLWNTK 85
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENPSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 86 HHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPK-NADG--TVRYDSTHYKE-TWKALEVLVAKGLVKALGL 161
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGkyVILKDLTENPEpTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 162 SNFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWRHPDEpvLLEEPVVLALAEKH 241
Cdd:cd19122 163 SNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGER--VSENPTLNEVAEKG 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 10946870 242 GRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFT 280
Cdd:cd19122 241 GYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELS 279
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
14-292 |
1.73e-70 |
|
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: 219.15 E-value: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 14 MPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNTKHHPEDVEP 93
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAES-----GVPRDELFITTKIWIDNLSKDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 94 ALRKTLADLQLEYLDLYLMHWPyafergdnpfpknadgtVRYDSTHYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVL 173
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHWP-----------------SPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 174 SVASVRP-AVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGssdrawrhpdEPVLLEEPVVLALAEKHGRSPAQILLRW 252
Cdd:cd19139 139 AVVGAGAiATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA----------YGKVLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 10946870 253 QVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDAL 292
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
17-293 |
7.06e-68 |
|
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: 214.10 E-value: 7.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTW-------KSEPGQVKAAIKHALSAGYRHIDCASVYG---NETEIGEALKEsvgsgKAVPREELFVTSKL----- 81
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKD-----YPVKRDKVVIATKVpdgdg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 -WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnpfpknadgtvrydSTHYKETWKALEVLVAKGLVKALG 160
Cdd:pfam00248 76 pWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-------------------DTPIEETWDALEELKKEGKIRAIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 161 LSNFNSRQIDDVLSVASVRPAVLQVECHPY--LAQNELIAHCHARGLEVTAYSPLGSS------------DRAWRHPDEP 226
Cdd:pfam00248 137 VSNFDAEQIEKALTKGKIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkGPGERRRLLK 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10946870 227 VLLEE-----PVVLALAEKHGRSPAQILLRW--QVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALN 293
Cdd:pfam00248 217 KGTPLnlealEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-290 |
1.81e-64 |
|
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: 204.39 E-value: 1.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 11 GQKMPLIGLGTWK---------SEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKEsvgsgkaVPREELFVT 78
Cdd:cd19072 1 GEEVPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG-------FDREDLFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 79 SKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgtvrydSTHYKETWKALEVLVAKGLVKA 158
Cdd:cd19072 74 TKVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP-------NP------------SIPIEETLRAMEELVEEGKIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 159 LGLSNFNSRQIDDVLSVASVRP-AVLQVECHPYL--AQNELIAHCHARGLEVTAYSPLGSSDRAWRHPDEpvLLEEpvvl 235
Cdd:cd19072 135 IGVSNFSLEELEEAQSYLKKGPiVANQVEYNLFDreEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSP--LLDE---- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 10946870 236 aLAEKHGRSPAQILLRWQVQRK-VICIPKSINPSRILQNIQVFDFTFSPEEMKQLD 290
Cdd:cd19072 209 -IAKKYGKTPAQIALNWLISKPnVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-290 |
5.64e-59 |
|
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: 190.54 E-value: 5.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 6 VLLHTGQKMPLIGLGTW-----KSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESvgsgkavpREELFV 77
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR--------RDKVFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 78 TSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWpyafeRGDNPFpknadgtvrydsthyKETWKALEVLVAKGLVK 157
Cdd:cd19138 75 VSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHW-----RGGVPL---------------AETVAAMEELKKEGKIR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 158 ALGLSNFNSRQIDDVLSVASVRP-AVLQVECHpyLAQ----NELIAHCHARGLEVTAYSPLGSSDRAWRHpdepvLLEEP 232
Cdd:cd19138 135 AWGVSNFDTDDMEELWAVPGGGNcAANQVLYN--LGSrgieYDLLPWCREHGVPVMAYSPLAQGGLLRRG-----LLENP 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 10946870 233 VVLALAEKHGRSPAQILLRWQV-QRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLD 290
Cdd:cd19138 208 TLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
13-301 |
2.62e-58 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 188.69 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 13 KMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESvgsgkAVPREELFVTSKLWNTKHHPEDVE 92
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAES-----GVPRDELFITTKIWIDNLAKDKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 93 PALRKTLADLQLEYLDLYLMHWPYafergdnpfPKNAdgtvrydsTHYKETWKALEVLVAKGLVKALGLSNFN---SRQI 169
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHWPS---------PNDE--------VSVEEFMQALLEAKKQGLTREIGISNFTialMKQA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 170 DDVLSVASVrpAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDrawrhpdepvLLEEPVVLALAEKHGRSPAQIL 249
Cdd:PRK11172 140 IAAVGAENI--ATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK----------VLKDPVIARIAAKHNATPAQVI 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 10946870 250 LRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVP 301
Cdd:PRK11172 208 LAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSP 259
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-290 |
9.71e-53 |
|
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: 174.30 E-value: 9.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 11 GQKMPLIGLGTWK---------SEPGQVKAAIKHALSAGYRHIDCASVYG---NETEIGEALKEsvgsgkaVPREELFVT 78
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD-------FPREDLFIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 79 SKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgtvrydSTHYKETWKALEVLVAKGLVKA 158
Cdd:cd19137 74 TKVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP-------NP------------NIPLEETLSAMAEGVRQGLIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 159 LGLSNFNSRQIDDVLSVASVRPAVLQVECHPY---LAQNELIAHCHARGLEVTAYSPLgssdrawrhpDEPVLLEEPVVL 235
Cdd:cd19137 135 IGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL----------RRGLEKTNRTLE 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 10946870 236 ALAEKHGRSPAQILLRWQVQR-KVICIPKSINPSRILQNIQVFDFTFSPEEMKQLD 290
Cdd:cd19137 205 EIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
9-292 |
2.81e-51 |
|
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: 171.90 E-value: 2.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGTW-------KSEPGQVKAAIKHALSAGYRHIDCASVYG---NETEIGEALKEsvgsgkaVPREELFVT 78
Cdd:COG0667 8 RSGLKVSRLGLGTMtfggpwgGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKG-------RPRDDVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 79 SKL--------WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknaDGTVRYDsthykETWKALEVL 150
Cdd:COG0667 81 TKVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP--------------DPDTPIE-----ETLGALDEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 151 VAKGLVKALGLSNFNSRQIDDVLSVAS--VRPAVLQVEchpY-----LAQNELIAHCHARGLEVTAYSPLGS-------- 215
Cdd:COG0667 142 VREGKIRYIGVSNYSAEQLRRALAIAEglPPIVAVQNE---YslldrSAEEELLPAARELGVGVLAYSPLAGglltgkyr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 216 -------SDRAWRHPDEPVLLEE-----PVVLALAEKHGRSPAQILLRWQVQRKVICIPksI----NPSRILQNIQVFDF 279
Cdd:COG0667 219 rgatfpeGDRAATNFVQGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSV--IpgarSPEQLEENLAAADL 296
|
330
....*....|...
gi 10946870 280 TFSPEEMKQLDAL 292
Cdd:COG0667 297 ELSAEDLAALDAA 309
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-290 |
1.51e-47 |
|
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: 161.63 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTWK-----------SEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESVgsgkavPREELFVTSKLW 82
Cdd:cd19093 5 LGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG------DRDEVVIATKFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 NT--KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFpknadgtvrydsthyketWKALEVLVAKGLVKALG 160
Cdd:cd19093 79 PLpwRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLVRAVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 161 LSNFNSRQI---DDVLSVASVRPAVLQVE---CHPYLAQNELIAHCHARGLEVTAYSPLG--------SSDRAWRHPDEP 226
Cdd:cd19093 141 VSNYSADQLrraHKALKERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPPPGGRRR 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10946870 227 VLLEE------PVVLAL---AEKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLD 290
Cdd:cd19093 221 LFGRKnlekvqPLLDALeeiAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-295 |
7.62e-44 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 151.97 E-value: 7.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTW---------KSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKEsvgsgkavPREELFVTSKLWNT 84
Cdd:cd19085 4 LGLGCWqfgggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG--------RRDDVVIATKVSPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafeRGDNPFpknadgtvrydsthyKETWKALEVLVAKGLVKALGLSNF 164
Cdd:cd19085 76 NLTPEDVRKSCERSLKRLGTDYIDLYQIHWP----SSDVPL---------------EETMEALEKLKEEGKIRAIGVSNF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 165 NSRQIDDVLSVAsvRPAVLQVechPY-L----AQNELIAHCHARGLEVTAYSPLG--------SSD----------RAWR 221
Cdd:cd19085 137 GPAQLEEALDAG--RIDSNQL---PYnLlwraIEYEILPFCREHGIGVLAYSPLAqglltgkfSSAedfppgdartRLFR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 222 HPDEPVlleEPVVL-------ALAEKHGRSPAQILLRWQVQRKVI--CIPKSINPSRILQNIQVFDFTFSPEEMKQLDAL 292
Cdd:cd19085 212 HFEPGA---EEETFealeklkEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
...
gi 10946870 293 NKN 295
Cdd:cd19085 289 SDP 291
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
17-290 |
9.35e-40 |
|
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: 141.51 E-value: 9.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTW--------KSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKesvgsGKavpREELFVTSK---LW 82
Cdd:cd19084 7 IGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALK-----GR---RDDVVIATKcglRW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 NTKHH------PEDVEPALRKTLADLQLEYLDLYLMHWPyafergDNPFPKNadgtvrydsthykETWKALEVLVAKGLV 156
Cdd:cd19084 79 DGGKGvtkdlsPESIRKEVEQSLRRLQTDYIDLYQIHWP------DPNTPIE-------------ETAEALEKLKKEGKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 157 KALGLSNFNSRQIDDVLSVASVrpAVLQVechPY--LAQN---ELIAHCHARGLEVTAYSPLG---------------SS 216
Cdd:cd19084 140 RYIGVSNFSVEQLEEARKYGPI--VSLQP---PYsmLEREieeELLPYCRENGIGVLPYGPLAqglltgkykkeptfpPD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 217 DRAWRHPD--EPVLLEEPVVLA----LAEKHGRSPAQILLRWQVQRK----VICIPKsiNPSRILQNIQVFDFTFSPEEM 286
Cdd:cd19084 215 DRRSRFPFfrGENFEKNLEIVDklkeIAEKYGKSLAQLAIAWTLAQPgvtsAIVGAK--NPEQLEENAGALDWELTEEEL 292
|
....
gi 10946870 287 KQLD 290
Cdd:cd19084 293 KEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-275 |
2.03e-36 |
|
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: 130.72 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTW----KSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESVgsgkavPREELFVTSKLWNTKH--- 86
Cdd:cd06660 3 LGLGTMtfggDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRG------NRDDVVIATKGGHPPGgdp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 87 -----HPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknaDGTVRYDsthykETWKALEVLVAKGLVKALGL 161
Cdd:cd06660 77 srsrlSPEHIRRDLEESLRRLGTDYIDLYYLHRD--------------DPSTPVE-----ETLEALNELVREGKIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 162 SNFNSRQIDDVLSVAS----VRPAVLQVE---CHPYLAQNELIAHCHARGLEVTAYSPLgssdrawrhpdepvlleepvv 234
Cdd:cd06660 138 SNWSAERLAEALAYAKahglPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPL--------------------- 196
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 10946870 235 lalaekhGRSPAQILLRWQVQRK--VICIPKSINPSRILQNIQ 275
Cdd:cd06660 197 -------ARGPAQLALAWLLSQPfvTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-292 |
1.62e-34 |
|
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: 127.79 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTWKSEPGQ------------VKAAIKHALSAGYRHIDCASVYG---NETEIGEALKESvgsgkavpREELFVTSK- 80
Cdd:cd19102 4 IGLGTWAIGGGGwgggwgpqddrdSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKGL--------RDRPIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 81 --LWNTKHH------PEDVEPALRKTLADLQLEYLDLYLMHWPYaferGDNPFpknadgtvrydsthyKETWKALEVLVA 152
Cdd:cd19102 76 glLWDEEGRirrslkPASIRAECEASLRRLGVDVIDLYQIHWPD----PDEPI---------------EEAWGALAELKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 153 KGLVKALGLSNFNSRQIDDVLSVASVrpAVLQVechPYLA-----QNELIAHCHARGLEVTAYSPLGS------------ 215
Cdd:cd19102 137 EGKVRAIGVSNFSVDQMKRCQAIHPI--ASLQP---PYSLlrrgiEAEILPFCAEHGIGVIVYSPMQSglltgkmtperv 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 216 -----SDRAWRHPD--EPVL---LEEPVVL-ALAEKHGRSPAQILLRWQVQRKVI--CIPKSINPSRILQNIQVFDFTFS 282
Cdd:cd19102 212 aslpaDDWRRRSPFfqEPNLarnLALVDALrPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLT 291
|
330
....*....|
gi 10946870 283 PEEMKQLDAL 292
Cdd:cd19102 292 PEELAEIEAL 301
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
9-290 |
4.57e-29 |
|
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: 113.45 E-value: 4.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGT----------WKSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESVgsgkavPREEL 75
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA------PRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 76 FVTSKLwntkHHPEDVEP------------ALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgtvRYD-STHYKE 142
Cdd:cd19079 81 VIATKV----YFPMGDGPngrglsrkhimaEVDASLKRLGTDYIDLYQIH--------------------RWDyETPIEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 143 TWKALEVLVAKGLVKALGLSNFNSRQIDDVLSVASV----RPAVLQvechPYL------AQNELIAHCHARGLEVTAYSP 212
Cdd:cd19079 137 TLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKngwtKFVSMQ----NHYnllyreEEREMIPLCEEEGIGVIPWSP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 213 L----------GSSDRAWRHPDEPVLLE-------EPV---VLALAEKHGRSPAQILLRWQVQRKVICIPksI----NPS 268
Cdd:cd19079 213 LargrlarpwgDTTERRRSTTDTAKLKYdyfteadKEIvdrVEEVAKERGVSMAQVALAWLLSKPGVTAP--IvgatKLE 290
|
330 340
....*....|....*....|..
gi 10946870 269 RILQNIQVFDFTFSPEEMKQLD 290
Cdd:cd19079 291 HLEDAVAALDIKLSEEEIKYLE 312
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
17-284 |
8.06e-27 |
|
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: 106.91 E-value: 8.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTWKSEPGQV-----KAAIKHALSAGYRHIDCASVYGN---ETEIGEALKEsvgsgkaVPREELFVTSKL-WNTKHH 87
Cdd:cd19074 7 LSLGTWLTFGGQVddedaKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG-------WPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 88 PED--------VEpALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgtvRYD-STHYKETWKALEVLVAKGLVKA 158
Cdd:cd19074 80 PNDrglsrkhiFE-SIHASLKRLQLDYVDIYYCH--------------------RYDpETPLEETVRAMDDLIRQGKILY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 159 LGLSNFNSRQIDDVLSVAS----VRPAVLQVECHpYLAQ---NELIAHCHARGLEVTAYSPL---------------GSS 216
Cdd:cd19074 139 WGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYN-MLWReieEEVIPLCEKNGIGLVVWSPLaqglltgkyrdgippPSR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 217 DRA-----WRHPDEpvLLEEPVV------LALAEKHGRSPAQILLRWQVQRKVIC--IPKSINPSRILQNIQVFDFTFSP 283
Cdd:cd19074 218 SRAtdednRDKKRR--LLTDENLekvkklKPIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSP 295
|
.
gi 10946870 284 E 284
Cdd:cd19074 296 E 296
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
14-282 |
1.36e-26 |
|
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: 105.38 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 14 MPLIGLGTWK--SEPGQVKAAIKHALSAGYRHIDCASVYG---NETEIGEALKesvgsgkavPR-EELFVTSKL------ 81
Cdd:cd19088 9 MRLTGPGIWGppADREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALH---------PYpDDVVIATKGglvrtg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 ---WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknaDGTVRYDsthykETWKALEVLVAKGLVKA 158
Cdd:cd19088 80 pgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI--------------DPKVPFE-----EQLGALAELQDEGLIRH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 159 LGLSNFNSRQIDDVLSVASVrpAVLQVECHPYLAQNE-LIAHCHARGLEVTAYSPLGSsdrawrhpdEPVLLEEPVVLAL 237
Cdd:cd19088 141 IGLSNVTVAQIEEARAIVRI--VSVQNRYNLANRDDEgVLDYCEAAGIAFIPWFPLGG---------GDLAQPGGLLAEV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 10946870 238 AEKHGRSPAQILLRWQVQRK--VICIPKSINPSRILQNIQVFDFTFS 282
Cdd:cd19088 210 AARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
9-292 |
4.74e-26 |
|
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: 105.39 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGT--------WKSEPGQVKAA-----IKHALSAGYRHIDCASVYGN-ETEI--GEALKESvgsgkavpR 72
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggFFGAWGGVDQEeadrlVDIALDAGINFFDTADVYSEgESEEilGKALKGR--------R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 73 EELFVTSKLWN-----------TKHHpedVEPALRKTLADLQLEYLDLYLMHWpyafergdnpfpknadgtvrYDS-THY 140
Cdd:cd19091 80 DDVLIATKVRGrmgegpndvglSRHH---IIRAVEASLKRLGTDYIDLYQLHG--------------------FDAlTPL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 141 KETWKALEVLVAKGLVKALGLSNFNSRQIDDVLSVAS----VRPAVLQVecHPYLA----QNELIAHCHARGLEVTAYSP 212
Cdd:cd19091 137 EETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQA--YYSLLgrdlEHELMPLALDQGVGLLVWSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 213 LGSS------DRAWRHP----------DEPVLLEE---PVVLAL---AEKHGRSPAQILLRWQVQRKVIcipKSI----- 265
Cdd:cd19091 215 LAGGllsgkyRRGQPAPegsrlrrtgfDFPPVDRErgyDVVDALreiAKETGATPAQVALAWLLSRPTV---SSViigar 291
|
330 340
....*....|....*....|....*..
gi 10946870 266 NPSRILQNIQVFDFTFSPEEMKQLDAL 292
Cdd:cd19091 292 NEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-297 |
6.96e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 105.67 E-value: 6.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGTW----KSEPgQVKAAIKHALSAGYRHIDCASVYGN-ETEIGEALKEsvgsgkavPREELFVTSKLWN 83
Cdd:COG1453 8 KTGLEVSVLGFGGMrlprKDEE-EAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG--------PRDKVILATKLPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNadgtvrydsthykETWKALEVLVAKGLVKALGLSN 163
Cdd:COG1453 79 WVRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKPG-------------GALEALEKAKAEGKIRHIGFST 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 164 FNSrqiddvlsvasvrPAVLQ--VECHP---------YLAQN-----ELIAHCHARGLEVTAYSPLGSSDrawrhpdepv 227
Cdd:COG1453 146 HGS-------------LEVIKeaIDTGDfdfvqlqynYLDQDnqageEALEAAAEKGIGVIIMKPLKGGR---------- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10946870 228 LLEEPVVLALAEKHGRSPAQILLRWQVQRKVICIPKS--INPSRILQNIQVFD--FTFSPEEMKQLDALNKNWR 297
Cdd:COG1453 203 LANPPEKLVELLCPPLSPAEWALRFLLSHPEVTTVLSgmSTPEQLDENLKTADnlEPLTEEELAILERLAEELG 276
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-290 |
1.63e-24 |
|
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: 100.75 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 6 VLLHTGQKMPLIGLGT----WKSEPGQVKAAIKHALSAGYRHIDCASVYGN----------ETEIGEALKESVGsgkavp 71
Cdd:cd19081 1 PLGRTGLSVSPLCLGTmvfgWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKSRGK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 72 REELFVTSKL-WNTKH-----HPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknaDgtvryDSTHYKETWK 145
Cdd:cd19081 75 RDRVVIATKVgFPMGPngpglSRKHIRRAVEASLRRLQTDYIDLYQAHWD--------------D-----PATPLEETLG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 146 ALEVLVAKGLVKALGLSNFNSRQIDDVLSVAS----VRPAVLQVECHPY---LAQNELIAHCHARGLEVTAYSPLGS--- 215
Cdd:cd19081 136 ALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhglPRYVSLQPEYNLVdreSFEGELLPLCREEGIGVIPYSPLAGgfl 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 216 ----------SDRAWRHPDEPVLLEEP------VVLALAEKHGRSPAQILLRWQVQRKVICIPksI----NPSRILQNIQ 275
Cdd:cd19081 216 tgkyrseadlPGSTRRGEAAKRYLNERglrildALDEVAAEHGATPAQVALAWLLARPGVTAP--IagarTVEQLEDLLA 293
|
330
....*....|....*
gi 10946870 276 VFDFTFSPEEMKQLD 290
Cdd:cd19081 294 AAGLRLTDEEVARLD 308
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
15-290 |
3.44e-24 |
|
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: 99.99 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 15 PLIgLGT--------WKSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESvgsgkavpREELFVTSKL-W 82
Cdd:cd19080 12 PLA-LGTmtfgtewgWGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAGN--------RDRIVLATKYtM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 NTkhHPEDVEP----------ALRKTLADLQLEYLDLYLMHWPyafergdnpfpknaDGTvrydsTHYKETWKALEVLVA 152
Cdd:cd19080 83 NR--RPGDPNAggnhrknlrrSVEASLRRLQTDYIDLLYVHAW--------------DFT-----TPVEEVMRALDDLVR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 153 KGLVKALGLSNFNSRQIDDVLSVASVR----PAVLQVECHpyLAQ----NELIAHCHARGLEVTAYSPLGS--------- 215
Cdd:cd19080 142 AGKVLYVGISDTPAWVVARANTLAELRgwspFVALQIEYS--LLErtpeRELLPMARALGLGVTPWSPLGGglltgkyqr 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 216 -----SDRAWRHPDEPVLLEE------PVVLALAEKHGRSPAQILLRWQVQRKVICIPkSINPSRILQ---NIQVFDFTF 281
Cdd:cd19080 220 geegrAGEAKGVTVGFGKLTErnwaivDVVAAVAEELGRSAAQVALAWVRQKPGVVIP-IIGARTLEQlkdNLGALDLTL 298
|
....*....
gi 10946870 282 SPEEMKQLD 290
Cdd:cd19080 299 SPEQLARLD 307
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
31-289 |
4.65e-24 |
|
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: 99.60 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 31 AAIKHALSAGYRHIDCASVYG---NETEIGEALKEsvgsgkavPREELFVTSK---LWNTKHH-------PEDVEPALRK 97
Cdd:cd19076 36 ATLHRALELGVTFLDTADMYGpgtNEELLGKALKD--------RRDEVVIATKfgiVRDPGSGfrgvdgrPEYVRAACEA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 98 TLADLQLEYLDLYLMHwpyafergdnpfpknadgtvRYDS-THYKETWKALEVLVAKGLVKALGLSNFNSRQIDdvlSVA 176
Cdd:cd19076 108 SLKRLGTDVIDLYYQH--------------------RVDPnVPIEETVGAMAELVEEGKVRYIGLSEASADTIR---RAH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 177 SVRP-AVLQVECHPYL--AQNELIAHCHARGLEVTAYSPLGssdR-----AWRHPDEP---------------------V 227
Cdd:cd19076 165 AVHPiTAVQSEYSLWTrdIEDEVLPTCRELGIGFVAYSPLG---RgfltgAIKSPEDLpeddfrrnnprfqgenfdknlK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10946870 228 LLEEpvVLALAEKHGRSPAQILLRWQVQRK--VICIPKSINPSRILQNIQVFDFTFSPEEMKQL 289
Cdd:cd19076 242 LVEK--LEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
30-292 |
1.27e-23 |
|
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: 98.41 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 30 KAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESvgsgkavpREELFVTSKLwntkHHPEDVEP------------A 94
Cdd:cd19087 33 FAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR--------RDDIVLATKV----FGPMGDDPndrglsrrhirrA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 95 LRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgtvRYDS-THYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVL 173
Cdd:cd19087 101 VEASLRRLQTDYIDLYQMH--------------------HFDRdTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 174 SVASVRP-AVLQVECHPY-----LAQNELIAHCHARGLEVTAYSPLG--------------SSDRAWRHPDEPVLLEEPV 233
Cdd:cd19087 161 GIAARRGlLRFVSEQPMYnllkrQAELEILPAARAYGLGVIPYSPLAgglltgkygkgkrpESGRLVERARYQARYGLEE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10946870 234 VL-------ALAEKHGRSPAQILLRWQVQRKVICIPkSINPSRILQ---NIQVFDFTFSPEEMKQLDAL 292
Cdd:cd19087 241 YRdiaerfeALAAEAGLTPASLALAWVLSHPAVTSP-IIGPRTLEQledSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
10-290 |
1.99e-23 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 97.69 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLG----TWKSEP---GQVKAAIKHALSAGYRHIDCASVYG------NETEIGEALKesvgsgkAVP--REE 74
Cdd:cd19077 1 NGKLVGPIGLGlmglTWRPNPtpdEEAFETMKAALDAGSNLWNGGEFYGppdphaNLKLLARFFR-------KYPeyADK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 75 LFVTSKL-WNTKHH-----PEDVEPALRKTLADL-QLEYLDLYlmhwpyafergdnpfpknadGTVRYDSTHY-KETWKA 146
Cdd:cd19077 74 VVLSVKGgLDPDTLrpdgsPEAVRKSIENILRALgGTKKIDIF--------------------EPARVDPNVPiEETIKA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 147 LEVLVAKGLVKALGLSNFNSRQIDDVLSVASVrpAVLQVECHPY---LAQNELIAHCHARGLEVTAYSPLG--------- 214
Cdd:cd19077 134 LKELVKEGKIRGIGLSEVSAETIRRAHAVHPI--AAVEVEYSLFsreIEENGVLETCAELGIPIIAYSPLGrglltgrik 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 215 ----SSDRAWR-HPDEP---------VLLEEpvVLALAEKHGRSPAQILLRW---QVQRKVICIPKSINPSRILQNIQVF 277
Cdd:cd19077 212 sladIPEGDFRrHLDRFngenfeknlKLVDA--LQELAEKKGCTPAQLALAWilaQSGPKIIPIPGSTTLERVEENLKAA 289
|
330
....*....|...
gi 10946870 278 DFTFSPEEMKQLD 290
Cdd:cd19077 290 NVELTDEELKEIN 302
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
15-278 |
2.27e-23 |
|
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: 96.86 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 15 PLIGLGT------WKSE--PGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKEsvgsgkaVPREELFVTSKL-W 82
Cdd:cd19096 1 SVLGFGTmrlpesDDDSidEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE-------GPREKFYLATKLpP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 NTKHHPEDVEPALRKTLADLQLEYLDLYLMH------WPYAFERGDnpfpknadgtvrydsthykeTWKALEVLVAKGLV 156
Cdd:cd19096 74 WSVKSAEDFRRILEESLKRLGVDYIDFYLLHglnspeWLEKARKGG--------------------LLEFLEKAKKEGLI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 157 KALGLSnF--NSRQIDDVLSVASVRPAVLQvecHPYLAQN-----ELIAHCHARGLEVTAYSPLGSSDRAWRhpdepvll 229
Cdd:cd19096 134 RHIGFS-FhdSPELLKEILDSYDFDFVQLQ---YNYLDQEnqagrPGIEYAAKKGMGVIIMEPLKGGGLANN-------- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 10946870 230 eEPVVLALAEKHGRSPAQILLRWQV-QRKVICIpkSI---NPSRILQNIQVFD 278
Cdd:cd19096 202 -PPEALAILCGAPLSPAEWALRFLLsHPEVTTV--LSgmsTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-252 |
2.73e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 96.50 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLGTwKSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKEsvgsgkaVPREELFVTSKLWNTKH 86
Cdd:cd19105 9 TGLKVSRLGFGG-GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG-------LRRDKVFLATKASPRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 87 H--PEDVEPALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgTVRYDSTHYK--ETWKALEVLVAKGLVKALGLS 162
Cdd:cd19105 81 KkdKAELLKSVEESLKRLQTDYIDIYQLH------------------GVDTPEERLLneELLEALEKLKKEGKVRFIGFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 163 ------NFNSRQID----DVLSVA-SVRpavlqvecHPYLAQNELIAHCHARGLEVTAYSPLGSsdrAWRHPDEPVLLEE 231
Cdd:cd19105 143 thdnmaEVLQAAIEsgwfDVIMVAyNFL--------NQPAELEEALAAAAEKGIGVVAMKTLAG---GYLQPALLSVLKA 211
|
250 260
....*....|....*....|.
gi 10946870 232 PvvlalaekhGRSPAQILLRW 252
Cdd:cd19105 212 K---------GFSLPQAALKW 223
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-276 |
4.74e-23 |
|
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: 95.76 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTWK-------SEPGQVKAAIKHALSAGYRHIDCASVYGN-ETEIGEALKEsvgsgkaVPREELFVTSKLW------ 82
Cdd:cd19095 3 LGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG-------LRRDDLFIATKVGthgegg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 -NTKHH-PEDVEPALRKTLADLQLEYLDLYLMHwpyaferGDNPfPKNADGTVRydsthyketwkALEVLVAKGLVKALG 160
Cdd:cd19095 76 rDRKDFsPAAIRASIERSLRRLGTDYIDLLQLH-------GPSD-DELTGEVLE-----------TLEDLKAAGKVRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 161 LSNFNSRqIDDVLsvASVRPAVLQVECHPYLAQNE-LIAHCHARGLEVTAYSPLGSSDRAWRHPDEPVLLEEPVVLALAE 239
Cdd:cd19095 137 VSGDGEE-LEAAI--ASGVFDVVQLPYNVLDREEEeLLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAA 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 10946870 240 KHG-RSPAQILLRWQVQRKVI--CIPKSINPSRILQNIQV 276
Cdd:cd19095 214 EIGgATWAQAALRFVLSHPGVssAIVGTTNPEHLEENLAA 253
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-285 |
3.15e-22 |
|
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: 94.16 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 18 GLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESVGSgkavpREELFVTSK----------LWNT 84
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGL-----REKIEIQTKcgirlgddprPGRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 85 KHH---PEDVEPALRKTLADLQLEYLDLYLMHWPYAFergdnpfpknadgtvrydsTHYKETWKALEVLVAKGLVKALGL 161
Cdd:cd19092 90 KHYdtsKEHILASVEGSLKRLGTDYLDLLLLHRPDPL-------------------MDPEEVAEAFDELVKSGKVRYFGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 162 SNFNSRQIDDVLSVASVRPAVLQVEC---HPYLAQNELIAHCHARGLEVTAYSPLG----SSDRAWRHPDEPVLLEEpvv 234
Cdd:cd19092 151 SNFTPSQIELLQSYLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGggrlFGGFDERFQRLRAALEE--- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 10946870 235 laLAEKHGRSPAQILLRWqVQR---KVICIPKSINPSRILQNIQVFDFTFSPEE 285
Cdd:cd19092 228 --LAEEYGVTIEAIALAW-LLRhpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
17-215 |
3.09e-21 |
|
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: 90.61 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTW--------KSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKEsvgsgkavPREELFVTSKLWNTK 85
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG--------RRDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 86 HH---------PEDVEPALRKTLADLQLEYLDLYLMH-WPYAFERGDnpfpknadgtvrydsthykETWKALEVLVAKGL 155
Cdd:cd19086 78 DGgperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDND-------------------ELFEALEKLKQEGK 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10946870 156 VKALGLSnfnSRQIDDVLSVASVRPA-VLQV-----ECHPYlaqNELIAHCHARGLEVTAYSPLGS 215
Cdd:cd19086 139 IRAYGVS---VGDPEEALAALRRGGIdVVQViynllDQRPE---EELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
28-290 |
4.61e-21 |
|
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: 91.14 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 28 QVKAAIKHALSAGYRHIDCASVYG---NETEIGEALKEsvgsgkavPREELFVTSK----LWNTKHH-------PEDVEP 93
Cdd:cd19078 26 EMIELIRKAVELGITFFDTAEVYGpytNEELVGEALKP--------FRDQVVIATKfgfkIDGGKPGplgldsrPEHIRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 94 ALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgtvRYD-STHYKETWKALEVLVAKGLVKALGLSNFNSRQIDDV 172
Cdd:cd19078 98 AVEGSLKRLQTDYIDLYYQH--------------------RVDpNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 173 LSVASVrpAVLQVECH-----PylaQNELIAHCHARGLEVTAYSPLG----------------SSDRAW--RHPDEPV-- 227
Cdd:cd19078 158 HAVCPV--TAVQSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGkgfltgkidentkfdeGDDRASlpRFTPEALea 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10946870 228 ---LLEepVVLALAEKHGRSPAQILLRWQVQRK--VICIPKSINPSRILQNIQVFDFTFSPEEMKQLD 290
Cdd:cd19078 233 nqaLVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
31-289 |
4.85e-21 |
|
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: 91.74 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 31 AAIKHALSAGYRHIDCASVYG-NETEIGEALKESVGSgkavpREELFVTSKLWNTKH----------HPEDVEPALRKTL 99
Cdd:cd19144 38 AVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGK-----REKIFLATKFGIEKNvetgeysvdgSPEYVKKACETSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 100 ADLQLEYLDLYLMHwpyafergdnpfpknadgtvRYD-STHYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVLSVASV 178
Cdd:cd19144 113 KRLGVDYIDLYYQH--------------------RVDgKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHAVHPI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 179 rpAVLQVECHPYL-----AQNELIAHCHARGLEVTAYSPLGSS--DRAWRHPDE----------PVLLEE--PVVL---- 235
Cdd:cd19144 173 --AAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRGflTGAIRSPDDfeegdfrrmaPRFQAEnfPKNLelvd 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 10946870 236 ---ALAEKHGRSPAQILLRWQVQRK--VICIPKSINPSRILQNIQVFDFTFSPEEMKQL 289
Cdd:cd19144 251 kikAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
10-287 |
5.27e-21 |
|
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: 91.16 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLGTWK-----SEPGQVKAAIKHALSAGYRHIDCASVYGN-----ETEIGEALKESvgsgKAVPREELFVTS 79
Cdd:cd19089 7 SGLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRD----LRPYRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 80 KL-----------WNTKHHpedVEPALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgtvRYD-STHYKETWKAL 147
Cdd:cd19089 83 KAgygmwpgpygdGGSRKY---LLASLDQSLKRMGLDYVDIFYHH--------------------RYDpDTPLEETMTAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 148 EVLVAKGlvKAL--GLSNFNS---RQIDDVLSVASVRPAVLQVechPY-----LAQNELIAHCHARGLEVTAYSPLGS-- 215
Cdd:cd19089 140 ADAVRSG--KALyvGISNYPGakaRRAIALLRELGVPLIIHQP---RYslldrWAEDGLLEVLEEAGIGFIAFSPLAQgl 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 216 -SDRAWRHPDE------------PVLLEEPVVLAL------AEKHGRSPAQILLRWQVQRKVIC---IPKSiNPSRILQN 273
Cdd:cd19089 215 lTDKYLNGIPPdsrraaeskfltEEALTPEKLEQLrklnkiAAKRGQSLAQLALSWVLRDPRVTsvlIGAS-SPSQLEDN 293
|
330
....*....|....*
gi 10946870 274 IQVFDFT-FSPEEMK 287
Cdd:cd19089 294 VAALKNLdFSEEELA 308
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
17-292 |
5.45e-21 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 91.33 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGT-----------WKSEPGqvKAAIKHALSAGYRHIDCASVYG---NETEIGEALKESVgsgkavpREELFVTSK-- 80
Cdd:cd19083 14 IGLGTnavgghnlypnLDEEEG--KDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYN-------RNEVVIATKga 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 81 LWNTKH------HPEDVEPALRKTLADLQLEYLDLYLMHWPyafergDNPFPKNadgtvrydsthykETWKALEVLVAKG 154
Cdd:cd19083 85 HKFGGDgsvlnnSPEFLRSAVEKSLKRLNTDYIDLYYIHFP------DGETPKA-------------EAVGALQELKDEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 155 LVKALGLSNFNSRQIDDVLSVASVRpaVLQvecHPYL-----AQNELIAHCHARGLEVTAYSPLGS-------------S 216
Cdd:cd19083 146 KIRAIGVSNFSLEQLKEANKDGYVD--VLQ---GEYNllqreAEEDILPYCVENNISFIPYFPLASgllagkytkdtkfP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 217 DRAWRHpDEPVLLEEPV---------VLALAEKHGRSPAQILLRWQVQRKVI--CIPKSINPSRILQNIQVFDFTFSPEE 285
Cdd:cd19083 221 DNDLRN-DKPLFKGERFsenldkvdkLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEE 299
|
....*..
gi 10946870 286 MKQLDAL 292
Cdd:cd19083 300 IAFIDAL 306
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
9-291 |
6.74e-21 |
|
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: 91.18 E-value: 6.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGTW---------KSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESvgsgkavpREELF 76
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR--------RDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 77 VTSK---LWNTK---HHPEDVEPALRK-------------TLADLQLEYLDLYLMHWPyafergDNPFPknadgtvryds 137
Cdd:cd19149 78 LATKcglRWDREggsFFFVRDGVTVYKnlspesireeveqSLKRLGTDYIDLYQTHWQ------DVETP----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 138 thYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVLSVASVrpAVLQVechPY-----LAQNELIAHCHARGLEVTAYSP 212
Cdd:cd19149 141 --IEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQE---KYsmldrGIEKELLPYCKKNNIAFQAYSP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 213 LGS-------------------SDRAWRHPD--EPV--LLEEpvVLALAEKHGRSPAQILLRWQVQR----KVICipKSI 265
Cdd:cd19149 214 LEQglltgkitpdrefdagdarSGIPWFSPEnrEKVlaLLEK--WKPLCEKYGCTLAQLVIAWTLAQpgitSALC--GAR 289
|
330 340
....*....|....*....|....*.
gi 10946870 266 NPSRILQNIQVFDFTFSPEEMKQLDA 291
Cdd:cd19149 290 KPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-226 |
1.70e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 88.31 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 6 VLLHTGQKMPLIGLGT---WKSEPGQVKAAIKHALSAGYRHIDCASVYGN-ETEIGEALKEsvgsgkavPREELFVTSKL 81
Cdd:cd19100 3 RLGRTGLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG--------RRDKVFLATKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 WNTKhhPEDVEPALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgTVRYDSTHYKETWK--ALEVLV---AKGLV 156
Cdd:cd19100 75 GARD--YEGAKRDLERSLKRLGTDYIDLYQLH------------------AVDTEEDLDQVFGPggALEALLeakEEGKI 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10946870 157 KALGLSNFNsrqiDDVLSVASVRPA--VLQVECHPYLAQN-----ELIAHCHARGLEVTAYSPLGSSDRAWRHPDEP 226
Cdd:cd19100 135 RFIGISGHS----PEVLLRALETGEfdVVLFPINPAGDHIdsfreELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP 207
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
17-292 |
2.05e-20 |
|
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: 89.93 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGT--WKSE--PGQVKAAIKHALSAGYRHIDCASVY--------GNETE--IGEALKES------VGSGKAVPREELF 76
Cdd:cd19094 4 ICLGTmtWGEQntEAEAHEQLDYAFDEGVNFIDTAEMYpvppspetQGRTEeiIGSWLKKKgnrdkvVLATKVAGPGEGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 77 VTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafERGDNPFPKNADGTV--RYDSTHYKETWKALEVLVAKG 154
Cdd:cd19094 84 TWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWP---DRYTPLFGGGYYTEPseEEDSVSFEEQLEALGELVKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 155 LVKALGLSN--------FNSRQIDDVLSvasvRPAVLQvecHPY--LAQNELIAH---CHARGLEVTAYSPLG------- 214
Cdd:cd19094 161 KIRHIGLSNetpwgvmkFLELAEQLGLP----RIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLAggvltgk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 215 ---SSDRA--WRHPDEP--------VLLEEPV--VLALAEKHGRSPAQILLRWQVQRKVIC--IpksINPSRILQ---NI 274
Cdd:cd19094 234 yldGAARPegGRLNLFPgymaryrsPQALEAVaeYVKLARKHGLSPAQLALAWVRSRPFVTstI---IGATTLEQlkeNI 310
|
330
....*....|....*...
gi 10946870 275 QVFDFTFSPEEMKQLDAL 292
Cdd:cd19094 311 DAFDVPLSDELLAEIDAV 328
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-291 |
2.72e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 86.49 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 32 AIKHALSAGYRHIDCASVYGN-ETEIGEALKESVGSG----------KAVPR-EELFVTsklwntkhhPEDVEPALRKTL 99
Cdd:cd19101 28 AMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERdaaddvqihtKWVPDpGELTMT---------RAYVEAAIDRSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 100 ADLQLEYLDLYLMHWpyafergdnpfpknADgtvrYDSTHYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVLSvASVR 179
Cdd:cd19101 99 KRLGVDRLDLVQFHW--------------WD----YSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILD-AGVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 180 PAVLQVEcHPYL---AQNELIAHCHARGLEVTAYSPLGS---SDRaWRHPDEPV-------------------------- 227
Cdd:cd19101 160 IVSNQVQ-YSLLdrrPENGMAALCEDHGIKLLAYGTLAGgllSEK-YLGVPEPTgpaletrslqkyklmidewggwdlfq 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10946870 228 -LLEepVVLALAEKHGRSPAQILLRWQVQRKviCIPKSI----NPSRILQNIQVFDFTFSPEEMKQLDA 291
Cdd:cd19101 238 eLLR--TLKAIADKHGVSIANVAVRWVLDQP--GVAGVIvgarNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-292 |
3.47e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 86.55 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLG------TW-KSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESvgsgkavpREELFVTS 79
Cdd:cd19104 8 TGLKVSELTFGgggiggLMgRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL--------PAGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 80 KLWNTKHHPED----VEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKnadGTVRyDSTHYKETWKALEVLVAKGL 155
Cdd:cd19104 80 KVRLDPDDLGDiggqIERSVEKSLKRLKRDSVDLLQLHNRIGDERDKPVGGT---LSTT-DVLGLGGVADAFERLRSEGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 156 VKALGLSNF-NSRQIDDVLsvASVRPAVLQV----------ECHP--YLAQN--ELIAHCHARGLEVTAYSPLGS---SD 217
Cdd:cd19104 156 IRFIGITGLgNPPAIRELL--DSGKFDAVQVyynllnpsaaEARPrgWSAQDygGIIDAAAEHGVGVMGIRVLAAgalTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 218 RAWRHPDEPVLLEEPV---------VLALAEKHGRSPAQILLRWQV-QRKVICIPKSI-NPSRILQNIQVFDF-TFSPEE 285
Cdd:cd19104 234 SLDRGREAPPTSDSDVaidfrraaaFRALAREWGETLAQLAHRFALsNPGVSTVLVGVkNREELEEAVAAEAAgPLPAEN 313
|
....*..
gi 10946870 286 MKQLDAL 292
Cdd:cd19104 314 LARLEAL 320
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-252 |
5.73e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 85.83 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTWKSEPG-----QVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESVGSGKaVPREELFVTSK-------- 80
Cdd:cd19099 6 LGLGTYRGDSDdetdeEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGG-IKRDEVVIVTKagyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 81 -----------------LWNTK------H--HPEDVEPALRKTLADLQLEYLDLYLMHWPYAF--ERGDNPFpknadgtv 133
Cdd:cd19099 85 deplrplkyleeklgrgLIDVAdsaglrHciSPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQllELGEEEF-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 134 rYDstHYKETWKALEVLVAKGLVKALGLSNFNSRQID--------------DVLSVASVRP--AVLQVECHPYLAQ---- 193
Cdd:cd19099 157 -YD--RLEEAFEALEEAVAEGKIRYYGISTWDGFRAPpalpghlsleklvaAAEEVGGDNHhfKVIQLPLNLLEPEalte 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10946870 194 --------NELIAHCHARGLEVTAYSPLGSSDrawrhpdepVLLEEPVVLALAEKHGRSPAQILLRW 252
Cdd:cd19099 234 kntvkgeaLSLLEAAKELGLGVIASRPLNQGQ---------LLGELRLADLLALPGGATLAQRALQF 291
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
11-213 |
8.56e-19 |
|
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: 85.05 E-value: 8.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 11 GQKMPLIGLGTWK--------SEPGQVKAAIKHALSAGYRHIDCASVYG---NETEIGEALKEsvgsgkAVPREELFVTS 79
Cdd:cd19148 1 DLPVSRIALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKE------YGKRDRVVIAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 80 KL---WNTKHHP----------EDVEPALRKtladLQLEYLDLYLMHWPyafergdnpfpknaDGTVRYDsthykETWKA 146
Cdd:cd19148 75 KVgleWDEGGEVvrnssparirKEVEDSLRR----LQTDYIDLYQVHWP--------------DPLVPIE-----ETAEA 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10946870 147 LEVLVAKGLVKALGLSNFNSRQIDDVLSVASVrpAVLQVechPY-----LAQNELIAHCHARGLEVTAYSPL 213
Cdd:cd19148 132 LKELLDEGKIRAIGVSNFSPEQMETFRKVAPL--HTVQP---PYnlferEIEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
18-289 |
1.28e-18 |
|
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: 84.41 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 18 GLGTWKSEPGQVkAAIKHALSAGYRHIDCASVYG---NETEIGEALKESvgsgkavPREELFVTSKLWNT---------K 85
Cdd:cd19145 25 DYGAPKPEEEGI-ALIHHAFNSGVTFLDTSDIYGpntNEVLLGKALKDG-------PREKVQLATKFGIHeiggsgvevR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 86 HHPEDVEPALRKTLADLQLEYLDLYLMHwpyafeRGDNPFPknadgtvrydsthYKETWKALEVLVAKGLVKALGLSNFN 165
Cdd:cd19145 97 GDPAYVRAACEASLKRLDVDYIDLYYQH------RIDTTVP-------------IEITMGELKKLVEEGKIKYIGLSEAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 166 SrqiDDVLSVASVRP-AVLQVECHPYL--AQNELIAHCHARGLEVTAYSPLG---------------SSDRAWRHP---- 223
Cdd:cd19145 158 A---DTIRRAHAVHPiTAVQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLGrgffagkakleelleNSDVRKSHPrfqg 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10946870 224 ----DEPVLLEEpvVLALAEKHGRSPAQILLRWQVQR--KVICIPKSINPSRILQNIQVFDFTFSPEEMKQL 289
Cdd:cd19145 235 enleKNKVLYER--VEALAKKKGCTPAQLALAWVLHQgeDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
17-252 |
3.85e-16 |
|
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: 77.60 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESVG---SGKAVPReelfvtsklWNTKHHPED 90
Cdd:cd19075 10 FGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELGLGERGfkiDTKANPG---------VGGGLSPEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 91 VEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknaDgtvryDSTHYKETWKALEVLVAKGLVKALGLSNFNSRQID 170
Cdd:cd19075 81 VRKQLETSLKRLKVDKVDVFYLHAP--------------D-----RSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 171 DVLSVAS----VRPAVLQ---------VEchpylaqNELIAHCHARGLEVTAYSPLG--------------------SSD 217
Cdd:cd19075 142 EIVEICKengwVLPTVYQgmynaitrqVE-------TELFPCLRKLGIRFYAYSPLAggfltgkykysedkagggrfDPN 214
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 10946870 218 RAW------RHPDEPVL--LEEpvVLALAEKHGRSPAQILLRW 252
Cdd:cd19075 215 NALgklyrdRYWKPSYFeaLEK--VEEAAEKEGISLAEAALRW 255
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-292 |
7.33e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 76.60 E-value: 7.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 13 KMPLIGLGTWK----SEPGQV-----------KAAIKHALSAGYRHIDCASVYG---NETEIGEALKEsvgsgkaVPREE 74
Cdd:cd19103 3 KLPKIALGTWSwgsgGAGGDQvfgnhldedtlKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR-------YPRED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 75 LFVTSKLWNTKHHPED--VEPALRKTLADLQLEYLDLYLMHWPYAFERgdnpfpknadgtvrydsthyketW-KALEVLV 151
Cdd:cd19103 76 YIISTKFTPQIAGQSAdpVADMLEGSLARLGTDYIDIYWIHNPADVER-----------------------WtPELIPLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 152 AKGLVKALGLSNFNSRQI---DDVLSVASVRpaVLQVECHPYL-----AQNELIAHCHARGLEVTAYSPL------GSSD 217
Cdd:cd19103 133 KSGKVKHVGVSNHNLAEIkraNEILAKAGVS--LSAVQNHYSLlyrssEEAGILDYCKENGITFFAYMVLeqgalsGKYD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 218 RAWRHPDE--------PVL--LEE--PVVLALAEKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEE 285
Cdd:cd19103 211 TKHPLPEGsgraetynPLLpqLEEltAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDE 290
|
....*..
gi 10946870 286 MKQLDAL 292
Cdd:cd19103 291 IKELEQL 297
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-251 |
6.38e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 73.33 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGTW--------KSEPGQVKAA-----IKHALSAGYRHIDCASVYGN-ETEIGEALKESvgsgkavprEELFVTSKLW 82
Cdd:cd19097 3 LALGTAqfgldygiANKSGKPSEKeakkiLEYALKAGINTLDTAPAYGDsEKVLGKFLKRL---------DKFKIITKLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 83 NTKHHPEDVEPA----LRKTLADLQLEYLDLYLMHWPYAFERgdnpfpknadgtvrydstHYKETWKALEVLVAKGLVKA 158
Cdd:cd19097 74 PLKEDKKEDEAAieasVEASLKRLKVDSLDGLLLHNPDDLLK------------------HGGKLVEALLELKKEGLIRK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 159 LGLSNFNSRQIDDVLSvaSVRPAVLQVechPY------LAQNELIAHCHARGLEVTAYSPL--G-----SSDRAWRHPDE 225
Cdd:cd19097 136 IGVSVYSPEELEKALE--SFKIDIIQL---PFnildqrFLKSGLLAKLKKKGIEIHARSVFlqGlllmePDKLPAKFAPA 210
|
250 260
....*....|....*....|....*.
gi 10946870 226 PVLLEEpvVLALAEKHGRSPAQILLR 251
Cdd:cd19097 211 KPLLKK--LHELAKKLGLSPLELALG 234
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-274 |
7.97e-15 |
|
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: 73.36 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 17 IGLGT--WKSEPGQV-----KAAIKHALSAGYRHIDCASVYGN-ETEIGEALKEsvgsgkaVPREELFVTSKLWNtkhHP 88
Cdd:cd19090 3 LGLGTagLGGVFGGVdddeaVATIRAALDLGINYIDTAPAYGDsEERLGLALAE-------LPREPLVLSTKVGR---LP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 89 EDVEP----ALRKTLAD----LQLEYLDLYLMHWPYAFERGDNPFPknaDGTVRydsthyketwkALEVLVAKGLVKALG 160
Cdd:cd19090 73 EDTADysadRVRRSVEEslerLGRDRIDLLMIHDPERVPWVDILAP---GGALE-----------ALLELKEEGLIKHIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 161 LS----NFNSRQID----DVLSVASvRPAVLQVEchpylAQNELIAHCHARGLEVTAYSPLG----------SSDRAWRH 222
Cdd:cd19090 139 LGggppDLLRRAIEtgdfDVVLTAN-RYTLLDQS-----AADELLPAAARHGVGVINASPLGmgllagrppeRVRYTYRW 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 10946870 223 PDEPVLLEEPVVLALAEKHGRSPAQILLRWQVQ----RKVICIPKsiNPSRILQNI 274
Cdd:cd19090 213 LSPELLDRAKRLYELCDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNV 266
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
9-301 |
3.40e-14 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 72.19 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGTW----KSEPGQVKAAIKHALSAGYRHIDCASVYG----------NETEIGEALKESVGsgkavpREE 74
Cdd:PRK10625 8 HSSLEVSTLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRGS------REK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 75 LFVTSKLWN-TKHHPEDVEP-----------ALRKTLADLQLEYLDLYLMHWPyafERGDNPFpknadGTVRYDSTHYK- 141
Cdd:PRK10625 82 LIIASKVSGpSRNNDKGIRPnqaldrknireALHDSLKRLQTDYLDLYQVHWP---QRPTNCF-----GKLGYSWTDSAp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 142 -----ETWKALEVLVAKGLVKALGLSNFNSRQIDDVLSVASVR--PAVLQVEcHPYLAQNE-----LIAHCHARGLEVTA 209
Cdd:PRK10625 154 avsllETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHdlPRIVTIQ-NPYSLLNRsfevgLAEVSQYEGVELLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 210 YSPLGSS--------------------DRAWRHPDEPVLLEEPVVLALAEKHGRSPAQILLRWqVQRKVICIPKSINPSR 269
Cdd:PRK10625 233 YSCLAFGtltgkylngakpagarntlfSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAF-VRRQPFVASTLLGATT 311
|
330 340 350
....*....|....*....|....*....|....*
gi 10946870 270 ILQ---NIQVFDFTFSPEEMKQLDALNKNWRYIVP 301
Cdd:PRK10625 312 MEQlktNIESLHLTLSEEVLAEIEAVHQVYTYPAP 346
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
37-272 |
3.55e-13 |
|
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: 68.73 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 37 LSAGYRHIDCASVYGN-------ETEIGEALKESvgsGKavpREELFVTSK--------LWNTKHHPEDVEPALRKTLAD 101
Cdd:cd19082 27 VELGGNFIDTARVYGDwvergasERVIGEWLKSR---GN---RDKVVIATKgghpdledMSRSRLSPEDIRADLEESLER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 102 LQLEYLDLYLMHwpyafeRgDNP-FPknADGTVrydsthyketwKALEVLVAKGLVKALGLSN----------------- 163
Cdd:cd19082 101 LGTDYIDLYFLH------R-DDPsVP--VGEIV-----------DTLNELVRAGKIRAFGASNwsteriaeanayakahg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 164 -----FNSRQiddvLSVASVRPAVLQVECHPYLAQNELIAHcHARGLEVTAYSPLGS---SDRAWRHPDEPVLLEEP--- 232
Cdd:cd19082 161 lpgfaASSPQ----WSLARPNEPPWPGPTLVAMDEEMRAWH-EENQLPVFAYSSQARgffSKRAAGGAEDDSELRRVyys 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 10946870 233 --------VVLALAEKHGRSPAQILLRWQVQRKVICIPkSINPSRILQ 272
Cdd:cd19082 236 eenferleRAKELAEEKGVSPTQIALAYVLNQPFPTVP-IIGPRTPEQ 282
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
14-293 |
1.53e-12 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 66.92 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 14 MPLIGLGTW--KSEPGQVKAAIKHALSAGYRHIDCASVYG----NETeIGEALKesvgsgkavP-REELFVTSKL----- 81
Cdd:PRK10376 25 MQLAGPGVFgpPKDRDAAIAVLREAVALGVNHIDTSDFYGphvtNQL-IREALH---------PyPDDLTIVTKVgarrg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 ----WNTKHHPEDVEPALRKTLADLQLEYLD---LYLMhwpyaferGDNPFPknADGTVrydsthyKETWKALEVLVAKG 154
Cdd:PRK10376 95 edgsWLPAFSPAELRRAVHDNLRNLGLDVLDvvnLRLM--------GDGHGP--AEGSI-------EEPLTVLAELQRQG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 155 LVKALGLSNFNSRQIDDVLSVASvrpaVLQVECHPYLAQ---NELIAHCHARGLEVTAYSPLGSSDrawrhPdepvlLEE 231
Cdd:PRK10376 158 LVRHIGLSNVTPTQVAEARKIAE----IVCVQNHYNLAHradDALIDALARDGIAYVPFFPLGGFT-----P-----LQS 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10946870 232 PVVLALAEKHGRSPAQILLRWQVQR--KVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALN 293
Cdd:PRK10376 224 STLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIA 287
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
9-252 |
1.97e-12 |
|
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: 66.85 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGTWKSEPGQV-----KAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESVgsgkaVPREELFVTSK 80
Cdd:cd19143 8 RSGLKVSALSFGSWVTFGNQVdvdeaKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELG-----WPRSDYVVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 81 L-W------------NTKHHPEdvepALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgtvRYD-STHYKETWKA 146
Cdd:cd19143 83 IfWggggpppndrglSRKHIVE----GTKASLKRLQLDYVDLVFCH--------------------RPDpATPIEETVRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 147 LEVLVAKGLVKALGLSNFNSRQIDDVLSVAS----VRPAVLQVE---CHPYLAQNELIAHCHARGLEVTAYSPLGS---- 215
Cdd:cd19143 139 MNDLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQynlFHRERVEVEYAPLYEKYGLGTTTWSPLASgllt 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 10946870 216 --------SDRAWRHPDEPVLLEEPVVL------------ALAEKHGRSPAQILLRW 252
Cdd:cd19143 219 gkynngipEGSRLALPGYEWLKDRKEELgqekiekvrklkPIAEELGCSLAQLAIAW 275
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-287 |
7.71e-12 |
|
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: 64.88 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGT--WKSEPGQVK-----AAIKHALSAGYRHIDCASVYGN---ETEIGEALkesvgsgKAVPREELFVT 78
Cdd:cd19163 8 KTGLKVSKLGFGAspLGGVFGPVDeeeaiRTVHEALDSGINYIDTAPWYGQgrsETVLGKAL-------KGIPRDSYYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 79 SKLWNTKHHPED--------VEPALRKTLADLQLEYLDLYLMHwpyafergDNPFPKNADGTVRydsthykETWKALEVL 150
Cdd:cd19163 81 TKVGRYGLDPDKmfdfsaerITKSVEESLKRLGLDYIDIIQVH--------DIEFAPSLDQILN-------ETLPALQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 151 VAKGLVKALGLSNFNSRQIDDVLSVASVRPAVLQVECHPYLAQN---ELIAHCHARGLEVTAYSPLGS---SDR---AWr 221
Cdd:cd19163 146 KEEGKVRFIGITGYPLDVLKEVLERSPVKIDTVLSYCHYTLNDTsllELLPFFKEKGVGVINASPLSMgllTERgppDW- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10946870 222 HPDEPVLLEE-PVVLALAEKHGRSPAQILLRWQVQRKVI--CIPKSINPSRILQNIQVFDFTFSPEEMK 287
Cdd:cd19163 225 HPASPEIKEAcAKAAAYCKSRGVDISKLALQFALSNPDIatTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
31-278 |
7.90e-12 |
|
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: 64.86 E-value: 7.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 31 AAIKHALSAGYRHIDCASVYGNETE---IGEALKESvgsgkAVPREELFVTSKLWNTK-----HHPEDVEPALRKTLADL 102
Cdd:cd19153 37 AIVAEAFAAGINHFDTSPYYGAESSeavLGKALAAL-----QVPRSSYTVATKVGRYRdsefdYSAERVRASVATSLERL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 103 QLEYLDLYLMHwpyafergDNPFpknadgtVRYDsTHYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVLSVASVRPA- 181
Cdd:cd19153 112 HTTYLDVVYLH--------DIEF-------VDYD-TLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSLd 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 182 VLQVECH------------PYLAQNELIAHCHARGLEVTAYSPLGSsdRAWrHPDEPVLLE-EPVVLALAEKHGRSPAQI 248
Cdd:cd19153 176 AVLSYCHltlqdarlesdaPGLVRGAGPHVINASPLSMGLLTSQGP--PPW-HPASGELRHyAAAADAVCASVEASLPDL 252
|
250 260 270
....*....|....*....|....*....|...
gi 10946870 249 LLRWQVQRKVICIPKSINPS---RILQNIQVFD 278
Cdd:cd19153 253 ALQYSLAAHAGVGTVLLGPSslaQLRSMLAAVD 285
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
31-224 |
1.32e-10 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 61.22 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 31 AAIKHALSAGYRHIDCASVYG---NETEIGEALKesvgsgkAVPREELFVTSKLWNTKHHPEDVEPA------------- 94
Cdd:cd19162 23 ATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA-------RHPRAEYVVSTKVGRLLEPGAAGRPAgadrrfdfsadgi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 95 ---LRKTLADLQLEYLDLYLMHWPYafergdnpfpknadgtvRYDSTHYKETWKALEVLVAKGLVKALGLSNFNSRQIDD 171
Cdd:cd19162 96 rrsIEASLERLGLDRLDLVFLHDPD-----------------RHLLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 10946870 172 VLSVASVRpAVLQVECHPYL---AQNELIAHCHARGLEVTAYSPLGSSDRAWRHPD 224
Cdd:cd19162 159 AARRADVD-VVMVAGRYTLLdrrAATELLPLCAAKGVAVVAAGVFNSGILATDDPA 213
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
9-287 |
6.86e-09 |
|
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: 56.26 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGTWKSEPG-----QVKAAIKHALSAGYRHIDCASVYG-----NETEIGEALKESVgsgkAVPREELFVT 78
Cdd:cd19151 7 RSGLKLPAISLGLWHNFGDvdryeNSRAMLRRAFDLGITHFDLANNYGpppgsAEENFGRILKEDL----KPYRDELIIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 79 SKL-----------WNTKHHpedVEPALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgtvrydSTHYKETWKAL 147
Cdd:cd19151 83 TKAgytmwpgpygdWGSKKY---LIASLDQSLKRMGLDYVDIFYHHRP-------DP------------ETPLEETMGAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 148 EVLVAKGlvKAL--GLSNFNSRQIDDVLsvasvrpAVLQVECHPYL------------AQNELIAHCHARGLEVTAYSPL 213
Cdd:cd19151 141 DQIVRQG--KALyvGISNYPPEEAREAA-------AILKDLGTPCLihqpkysmfnrwVEEGLLDVLEEEGIGCIAFSPL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 214 GS---SDR-------------AWRHPDEPVLLEEPV-----VLALAEKHGRSPAQILLRWQVQRKVIC---IPKSiNPSR 269
Cdd:cd19151 212 AQgllTDRylngipedsraakGSSFLKPEQITEEKLakvrrLNEIAQARGQKLAQMALAWVLRNKRVTsvlIGAS-KPSQ 290
|
330
....*....|....*....
gi 10946870 270 ILQNIQVFDFT-FSPEEMK 287
Cdd:cd19151 291 IEDAVGALDNReFSEEELA 309
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
10-213 |
2.61e-08 |
|
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: 54.39 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLGTWKS-----EPGQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKEsvgsgKAVPREELFVTSKL 81
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaiSEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKK-----KGWKRSSYIVSTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 -WNT---------KHHPEDVEPALRKtladLQLEYLDLYLMHwpyafeRGDNPFPknadgtvrydsthYKETWKALEVLV 151
Cdd:cd19142 84 yWSYgseerglsrKHIIESVRASLRR----LQLDYIDIVIIH------KADPMCP-------------MEEVVRAMSYLI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10946870 152 AKGLVKALGLSNFNSRQIDDVLSVAS----VRPAVLQVECHPY------LAQNELIahcHARGLEVTAYSPL 213
Cdd:cd19142 141 DNGLIMYWGTSRWSPVEIMEAFSIARqfncPTPICEQSEYHMFcrekmeLYMPELY---NKVGVGLITWSPL 209
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
9-287 |
9.44e-08 |
|
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: 52.84 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 9 HTGQKMPLIGLGTWKS----EPGQVKAAIKH-ALSAGYRHIDCASVYG-----NETEIGEALKESVgsgkAVPREELFVT 78
Cdd:cd19150 7 KSGLKLPALSLGLWHNfgddTPLETQRAILRtAFDLGITHFDLANNYGpppgsAEENFGRILREDF----AGYRDELIIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 79 SKL-----------WNTKHHpedVEPALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgtvRYD-STHYKETWKA 146
Cdd:cd19150 83 TKAgydmwpgpygeWGSRKY---LLASLDQSLKRMGLDYVDIFYSH--------------------RFDpDTPLEETMGA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 147 LEVLVAKGlvKAL--GLSNFNS---RQIDDVLSVASVrPAVLQVECHPYL----AQNELIAHCHARGLEVTAYSPLG--- 214
Cdd:cd19150 140 LDHAVRSG--KALyvGISSYSPertREAAAILRELGT-PLLIHQPSYNMLnrwvEESGLLDTLQELGVGCIAFTPLAqgl 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 215 ----------SSDRAWR-HPDEPVLLEEPVVL------ALAEKHGRSPAQILLRWQVQRKVIC---IPKSiNPSRILQNI 274
Cdd:cd19150 217 ltdkylngipEGSRASKeRSLSPKMLTEANLNsiralnEIAQKRGQSLAQMALAWVLRDGRVTsalIGAS-RPEQLEENV 295
|
330
....*....|....
gi 10946870 275 QVFD-FTFSPEEMK 287
Cdd:cd19150 296 GALDnLTFSADELA 309
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
10-214 |
1.57e-07 |
|
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: 51.97 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLGTWKSEPGQVKAAIKH-----ALSAGYRHIDCASVYG---NETEIGEALKEsvgsgKAVPREELFVTSKL 81
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAagkAEVILGSIIKK-----KGWRRSSLVITTKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 -WNTKHHPE------DVEPALRKTLADLQLEYLDLYLMHWPyafergDNPFPknadgtvrydsthYKETWKALEVLVAKG 154
Cdd:cd19159 84 yWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDVVFANRP------DSNTP-------------MEEIVRAMTHVINQG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10946870 155 LVKALGLSNFNSRQIDDVLSVAS----VRPAVLQVECHPYLAQN---ELIAHCHARGLEVTAYSPLG 214
Cdd:cd19159 145 MAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLA 211
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
10-214 |
2.10e-06 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 48.54 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLGTWKSEPGQVKAAIKHALSA-----GYRHIDCASVYGN---ETEIGEALKEsvgsgKAVPREELFVTSKL 81
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGQITDEMAEHLMTlaydnGINLFDTAEVYAAgkaEVVLGNIIKK-----KGWRRSSLVITTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 -WNTKHHPE------DVEPALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgtvrydSTHYKETWKALEVLVAKG 154
Cdd:cd19158 84 fWGGKAETErglsrkHIIEGLKASLERLQLEYVDVVFANRP-------DP------------NTPMEETVRAMTHVINQG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10946870 155 LVKALGLSNFNSRQIDDVLSVAS----VRPAVLQVECHPYLAQN---ELIAHCHARGLEVTAYSPLG 214
Cdd:cd19158 145 MAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLA 211
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
10-213 |
8.68e-06 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 46.67 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLGTWKSEPGQVKAAI-KHALSAGYRH----IDCASVY-GNETEI--GEALKEsvgsgKAVPREELFVTSKL 81
Cdd:cd19141 8 SGLRVSCLGLGTWVTFGSQISDEVaEELVTLAYENginlFDTAEVYaAGKAEIvlGKILKK-----KGWRRSSYVITTKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 -WNTKHHPE------DVEPALRKTLADLQLEYLDLYlmhwpyafergdnpFPKNADGTvrydsTHYKETWKALEVLVAKG 154
Cdd:cd19141 83 fWGGKAETErglsrkHIIEGLKASLERLQLEYVDIV--------------FANRPDPN-----TPMEEIVRAFTHVINQG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10946870 155 LVKALGLSNFNSRQIDDVLSVAS----VRPAVLQVECHpyLAQNELI-AHC----HARGLEVTAYSPL 213
Cdd:cd19141 144 MAMYWGTSRWSAMEIMEAYSVARqfnlIPPIVEQAEYH--LFQREKVeMQLpelfHKIGVGAMTWSPL 209
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
32-113 |
2.09e-05 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 45.35 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 32 AIKHALSAGYRHIDCASVYGN-ETEIGEALKESVgsgKAVPREELFVTSK-----LWNTKHHPEDVEPALRKTLADLQLE 105
Cdd:cd19164 39 IVRRALELGIRAFDTSPYYGPsEIILGRALKALR---DEFPRDTYFIITKvgrygPDDFDYSPEWIRASVERSLRRLHTD 115
|
....*...
gi 10946870 106 YLDLYLMH 113
Cdd:cd19164 116 YLDLVYLH 123
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
10-216 |
2.93e-05 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 44.98 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLGTWKSEPGQVKAAI-KHALSAGYRH----IDCASVYGN---ETEIGEALKEsvgsgKAVPREELFVTSKL 81
Cdd:cd19160 11 SGLRVSCLGLGTWVTFGSQISDETaEDLLTVAYEHgvnlFDTAEVYAAgkaERTLGNILKS-----KGWRRSSYVVTTKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 82 -WNTKHHPE------DVEPALRKTLADLQLEYLDLYLMHwpyafeRGDNPFPknadgtvrydsthYKETWKALEVLVAKG 154
Cdd:cd19160 86 yWGGQAETErglsrkHIIEGLRGSLDRLQLEYVDIVFAN------RSDPNSP-------------MEEIVRAMTYVINQG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10946870 155 LVKALGLSNFNSRQIDDVLSVAS----VRPAVLQVECHPYL---AQNELIAHCHARGLEVTAYSPLGSS 216
Cdd:cd19160 147 MAMYWGTSRWSAMEIMEAYSVARqfnlIPPVCEQAEYHLFQrekVEMQLPELYHKIGVGSVTWSPLACG 215
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
15-284 |
5.47e-05 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 44.14 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 15 PLIGLGT------WKSEP-GQVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALKEsvgsgkaVPREELFVTSKL-Wn 83
Cdd:cd19152 1 PKLGFGTaplgnlYEAVSdEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE-------LGREDYVISTKVgR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 84 tKHHPEDVEPALRKTLAD--------------------------LQLEYLDLYLMHWPyafergDNPFPKNADGTVRYDS 137
Cdd:cd19152 73 -LLVPLQEVEPTFEPGFWnplpfdavfdysydgilrsiedslqrLGLSRIDLLSIHDP------DEDLAGAESDEHFAQA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 138 ThyKETWKALEVLVAKGLVKALGL-SNFnSRQIDDVLSVAsvRPAVLQVEC------HPylAQNELIAHCHARGLEVTAY 210
Cdd:cd19152 146 I--KGAFRALEELREEGVIKAIGLgVND-WEVILRILEEA--DLDWVMLAGrytlldHS--AARELLPECEKRGVKVVNA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 211 SPL-------GSSDRAWRHPDEPVLLEEPV--VLALAEKHGRSPA----QILLRWQVQRKVicIPKSINPSRILQNIQVF 277
Cdd:cd19152 219 GPFnsgflagGDNFDYYEYGPAPPELIARRdrIEALCEQHGVSLAaaalQFALAPPAVASV--APGASSPERVEENVALL 296
|
....*..
gi 10946870 278 DFTFSPE 284
Cdd:cd19152 297 ATEIPAA 303
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
28-285 |
8.26e-05 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 43.85 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 28 QVKAAIKHALSAGYRHIDCASVYGN---ETEIGEALK-----ESVGSGKA----VPREELFVTSKLWNTKHHPEDVE--- 92
Cdd:cd19161 21 DADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRekprdEFVLSTKVgrllKPAREGSVPDPNGFVDPLPFEIVydy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 93 ------PALRKTLADLQLEYLDLYLMHWPYAFERGDNPfpknadgTVRYDSTHYKETWKALEVLVAKGLVKALGLSNFNS 166
Cdd:cd19161 101 sydgimRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRK-------ERHHFAQLMSGGFKALEELKKAGVIKAFGLGVNEV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 167 RQIDDVLSVASVRPAVLQVEcHPYLAQN---ELIAHCHARGLEVTAYSPLGSSDRA----------WRHPDEPVLLEEPV 233
Cdd:cd19161 174 QICLEALDEADLDCFLLAGR-YSLLDQSaeeEFLPRCEQRGTSLVIGGVFNSGILAtgtksgakfnYGDAPAEIISRVME 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 10946870 234 VLALAEKHGRSPAQILLRWQVQRKVIcipKSI-----NPSRILQNIQVFDfTFSPEE 285
Cdd:cd19161 253 IEKICDAYNVPLAAAALQFPLRHPAV---ASVltgarNPAQLRQNVEAFQ-TDIPEE 305
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
10-113 |
1.07e-03 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 40.15 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946870 10 TGQKMPLIGLGTwkSEPGQV---------KAAIKHALSAGYRHIDCASVYGN---ETEIGEALKESvgsgkAVPREELFV 77
Cdd:PLN02587 7 TGLKVSSVGFGA--SPLGSVfgpvseedaIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL-----GIPREKYVV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 10946870 78 TSKLWNTKH----HPEDVEPALRKTLADLQLEYLDLYLMH 113
Cdd:PLN02587 80 STKCGRYGEgfdfSAERVTKSVDESLARLQLDYVDILHCH 119
|
|
| |
