|
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: 664.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKLWNTKHH 87
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 PEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSR 167
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 168 QIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEKYGRSPAQ 247
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSPAQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320202988 248 ILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVPMLTVDGKRVPR 312
Cdd:cd19106 241 ILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVPMITVDGKRVPR 305
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-299 |
1.39e-142 |
|
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: 404.49 E-value: 1.39e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKaVPREELFVTSKLWNTKHH 87
Cdd:cd19123 6 LSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGK-VKREDLWITSKLWNNSHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 PEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGdNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSR 167
Cdd:cd19123 85 PEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSVK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 168 QIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDR--AWRDPDEPVLLEEPVVLALAEKYGRSP 245
Cdd:cd19123 164 KLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRpaAMKAEGEPVLLEDPVINKIAEKHGASP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 320202988 246 AQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYI 299
Cdd:cd19123 244 AQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 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 |
1.82e-140 |
|
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: 397.24 E-value: 1.82e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 14 MPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTKHHPEDVEP 93
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRE-----SGVPREELFITTKLWPTDHGYERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 94 ALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPknadgticydsthYKETWKALEALVAKGLVQALGLSNFNSRQIDDIL 173
Cdd:cd19071 76 ALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEA-------------RLETWRALEELVDEGLVRSIGVSNFNVEHLEELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 174 SVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRawrdpdepVLLEEPVVLALAEKYGRSPAQILLRWQ 253
Cdd:cd19071 143 AAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR--------PLLDDPVLKEIAKKYGKTPAQVLLRWA 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 320202988 254 VQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLN 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 |
5.27e-139 |
|
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: 395.63 E-value: 5.27e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVgPGKAVPREELFVTSKLWNTKHHPED 90
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKI-KEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 91 VEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQID 170
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 171 DILSVASVR--PAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEKYGRSPAQI 248
Cdd:cd19107 160 RILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320202988 249 LLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVpmltvdgkrVPRDAGHPLYPFNDPY 325
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACA---------LLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
5-299 |
1.69e-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: 1.69e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 5 CVLLHTGQKMPLIGLGTWKS-EPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKaVPREELFVTSKLWN 83
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGV-VKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAF-ERGDNPFPKNADgticYDSTHYKETWKALEALVAKGLVQALGLS 162
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFkENNDSESNGDGS----LSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 163 NFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVlLEEPVVLALAEKYG 242
Cdd:cd19116 157 NFNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPR-LDDPTLVAIAKKYG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 320202988 243 RSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYI 299
Cdd:cd19116 236 KTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-301 |
1.75e-133 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 379.78 E-value: 1.75e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTKHHPED 90
Cdd:COG0656 2 GVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA-----SGVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 91 VEPALRKTLADLQLEYLDLYLMHWPYafergdnpfpknadgticydSTHYKETWKALEALVAKGLVQALGLSNFNSRQID 170
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPG--------------------PGPYVETWRALEELYEEGLIRAIGVSNFDPEHLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 171 DILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALAEKYGRSPAQILL 250
Cdd:COG0656 137 ELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQVVL 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 320202988 251 RWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVP 301
Cdd:COG0656 207 RWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLGPD 257
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-290 |
8.87e-132 |
|
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: 376.69 E-value: 8.87e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdVGPGKAVPREELFVTSKLWNTKHH 87
Cdd:cd19125 5 LNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKK-LFEDGVVKREDLFITSKLWCTDHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 PEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDnPFPKNADgticYDSTHYKETWKALEALVAKGLVQALGLSNFNSR 167
Cdd:cd19125 84 PEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA-HMPEPEE----VLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 168 QIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDepvLLEEPVVLALAEKYGRSPAQ 247
Cdd:cd19125 159 KLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKLGKTPAQ 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 320202988 248 ILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLN 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 |
3.02e-127 |
|
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: 365.58 E-value: 3.02e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 3 ASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKaVPREELFVTSKLW 82
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGV-VKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 83 NTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLS 162
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 163 NFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPD-----EPVLLEEPVVLAL 237
Cdd:cd19154 160 NFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKStgvspAPNLLQDPIVKAI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 238 AEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWR 297
Cdd:cd19154 240 AEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
5-299 |
3.52e-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: 345.37 E-value: 3.52e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 5 CVLLHTGQKMPLIGLGTWKSE---PGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGkAVPREELFVTSKL 81
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPEevpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADG-TVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGL 161
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 162 SNFNSRQIDDILSVASV--RPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSS-DRAWRDPDEPVLLEEPVVLALA 238
Cdd:cd19108 161 SNFNRRQLEMILNKPGLkyKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320202988 239 EKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYI 299
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-292 |
5.92e-119 |
|
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: 344.01 E-value: 5.92e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKLWNTKHH 87
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 PEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGT----ICYD-STHYKETWKALEALVAKGLVQALGLS 162
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLTAVPTnggeVDLDlSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 163 NFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAwrdpdEPVLLEEPVVLALAEKYG 242
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLAG-----LPLLVQHPEVKAIAAKLG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 320202988 243 RSPAQILLRWQVQRKVICIPKSITPSRILQNIKvfDFTFSPEEMKQLNAL 292
Cdd:cd19118 236 KTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-300 |
4.34e-114 |
|
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: 331.77 E-value: 4.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKaVPREELFVTSKLWNTKHHPED 90
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGK-LKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 91 VEPALRKTLADLQLEYLDLYLMHWPYAFE-RGDNPFPKNAdgticydSTHYKETWKALEALVAKGLVQALGLSNFNSRQI 169
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVnKKDKGERELA-------SSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 170 DDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRA--WRDPDEPVLLEEPVVLALAEKYGRSPAQ 247
Cdd:cd19111 153 NKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPAQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 320202988 248 ILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIV 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 |
1.39e-113 |
|
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: 331.38 E-value: 1.39e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGTW----KSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKaVPREELFVTSKLWNTKH 86
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGK-VKREDIFYCGKLWNTCH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 87 HPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNS 166
Cdd:cd19109 80 PPELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 167 RQIDDILSVASV--RPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSS-DRAWRDPDEPVLLEEPVVLALAEKYGR 243
Cdd:cd19109 160 RQLELILNKPGLkhKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320202988 244 SPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVPMLTVDgkrvprdagHPLYPF 321
Cdd:cd19109 240 TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRD---------HPEYPF 308
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-297 |
1.55e-113 |
|
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: 331.03 E-value: 1.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 4 SCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKaVPREELFVTSKLWN 83
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGK-VKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFE-RGDNPFPKNADGTICYD-STHYKETWKALEALVAKGLVQALGL 161
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 162 SNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDP-------DEPVLLEEPVV 234
Cdd:cd19155 161 SNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320202988 235 LALAEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWR 297
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-325 |
2.71e-110 |
|
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: 322.68 E-value: 2.71e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 12 QKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGkAVPREELFVTSKLWNTKHHPEDV 91
Cdd:cd19110 2 EDIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEG-VVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 92 EPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDD 171
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 172 ILSVAS--VRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRdpdepvLLEEPVVLALAEKYGRSPAQIL 249
Cdd:cd19110 161 LLNKPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVD------LIDDPVIQRIAKKHGKSPAQIL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320202988 250 LRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVpmltvdgkrVPRDAGHPLYPFNDPY 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 |
3.36e-108 |
|
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: 315.87 E-value: 3.36e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 5 CVLLHTGQKMPLIGLGTWKSEPGQ-VKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDvgpgkAVPREELFVTSKLWN 83
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKES-----GIPREELFITSKVWN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknadgticyDSTHYKETWKALEALVAKGLVQALGLSN 163
Cdd:cd19157 76 ADQGYDSTLKAFEASLERLGLDYLDLYLIHWP--------------------VKGKYKETWKALEKLYKDGRVRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 164 FNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALAEKYGR 243
Cdd:cd19157 136 FQVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEKYNK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 320202988 244 SPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRY 298
Cdd:cd19157 206 SVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
14-292 |
6.24e-104 |
|
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: 304.94 E-value: 6.24e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 14 MPLIGLGTWK---SEpgQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKeDVGPGKAVPREELFVTSKLWNTKHHPED 90
Cdd:cd19136 1 MPILGLGTFRlrgEE--EVRQAVDAALKAGYRLIDTASVYRNEADIGKALR-DLLPKYGLSREDIFITSKLAPKDQGYEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 91 VEPALRKTLADLQLEYLDLYLMHWP-YAFERGDNPfpKNADgticydstHYKETWKALEALVAKGLVQALGLSNFNSRQI 169
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHWPgVQGLKPSDP--RNAE--------LRRESWRALEDLYKEGKLRAIGVSNYTVRHL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 170 DDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdePVLLEEPVVLALAEKYGRSPAQIL 249
Cdd:cd19136 148 EELLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD--------LRLLEDPTVLAIAKKYGRTPAQVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 320202988 250 LRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNAL 292
Cdd:cd19136 220 LRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
2-298 |
1.02e-100 |
|
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: 298.57 E-value: 1.02e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 2 AASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGkAVPREELFVTSKL 81
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEG-IVKREDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDnP---FP---KNADGTICYDSTHYKETWKALEALVAKGL 155
Cdd:cd19115 80 WNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVD-PavrYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 156 VQALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLG-------SSDRAwrdPDEPVL 228
Cdd:cd19115 159 ARSIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsflelDLPGA---KDTPPL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 229 LEEPVVLALAEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRY 298
Cdd:cd19115 236 FEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-294 |
2.27e-100 |
|
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: 296.72 E-value: 2.27e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKeDVGpgkaVPREELFVTSKLWNTKHH 87
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK-DSG----VPREEIFITTKLWCTWHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 peDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPF-PKNADGT-ICYDSTHYKETWKALEALVAKGLVQALGLSNFN 165
Cdd:cd19117 83 --RVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFlFKKDDGTkDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 166 SRQIDDILS--VASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAwrdpdepvLLEEPVVLALAEKYGR 243
Cdd:cd19117 161 IKNLEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 320202988 244 SPAQILLRWQVQRKVICIPKSITPSRILQNIKVfdFTFSPEEMKQLNALNK 294
Cdd:cd19117 233 TPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-301 |
1.11e-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: 295.93 E-value: 1.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 4 SCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGkAVPREELFVTSKLWN 83
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTG-LVKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 84 TKHhpEDVEPALRKTLADLQLEYLDLYLMHWPYAFER---GDNPFPKNADGTICYDST-HYKETWKALEALVAKGLVQAL 159
Cdd:cd19112 80 SDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLDIDVTiSLETTWHAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 160 GLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLG--SSDRAWRDPDEPvlLEEPVVLAL 237
Cdd:cd19112 158 GISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWFGSVSP--LDDPVLKDL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320202988 238 AEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVP 301
Cdd:cd19112 236 AKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQP 299
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
6-293 |
5.74e-99 |
|
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: 292.17 E-value: 5.74e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 6 VLLHTGQKMPLIGLGTWK-SEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNT 84
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK-----SGIPREELFITTKLWIQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYaferGDnpfpknadgticydsthYKETWKALEALVAKGLVQALGLSNF 164
Cdd:cd19133 76 DAGYEKAKKAFERSLKRLGLDYLDLYLIHQPF----GD-----------------VYGAWRAMEELYKEGKIRAIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 165 NSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAwrdpdepvLLEEPVVLALAEKYGRS 244
Cdd:cd19133 135 YPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN--------LFENPVLTEIAEKYGKS 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 320202988 245 PAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN 293
Cdd:cd19133 207 VAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-301 |
8.55e-99 |
|
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: 293.58 E-value: 8.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 6 VLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGkAVPREELFVTSKLWNTK 85
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEG-LVKREELFLTSKLWNNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 86 HHPEDVEPALRKTLADLQLEYLDLYLMHWPYAF------ERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQAL 159
Cdd:cd19113 82 HDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFkfvpieEKYPPGFYCGDGDNFVYEDVPILDTWKALEKLVDAGKIKSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 160 GLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSD----RAWRDPDEPVLLEEPVVL 235
Cdd:cd19113 162 GVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSfvelNQGRALNTPTLFEHDTIK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320202988 236 ALAEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVP 301
Cdd:cd19113 242 SIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFNDP 307
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
6-293 |
2.91e-97 |
|
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: 287.80 E-value: 2.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 6 VLLHTGQKMPLIGLGTWKSEPG-QVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNT 84
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE-----SGVPREELFVTTKLWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnpfpknadgticydsTHYKETWKALEALVAKGLVQALGLSNF 164
Cdd:cd19126 76 DQRARRTEDAFQESLDRLGLDYVDLYLIHWPGK--------------------DKFIDTWKALEKLYASGKVKAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 165 NSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSdrawrdpdepVLLEEPVVLALAEKYGRS 244
Cdd:cd19126 136 QEHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----------GLLSNPVLAAIGEKYGKS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 320202988 245 PAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN 293
Cdd:cd19126 206 AAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-292 |
8.17e-97 |
|
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: 287.51 E-value: 8.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGkaVPREELFVTSKLWNTKHh 87
Cdd:cd19121 6 LNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG--VKREDLFVTTKLWSTYH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 pEDVEPALRKTLADLQLEYLDLYLMHWPYAF--ERGDNPFPKNADGTICYDST-HYKETWKALEALVAKGLVQALGLSNF 164
Cdd:cd19121 83 -RRVELCLDRSLKSLGLDYVDLYLVHWPVLLnpNGNHDLFPTLPDGSRDLDWDwNHVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 165 NSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAwrdpdepvLLEEPVVLALAEKYGRS 244
Cdd:cd19121 162 SIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEIAKKHNVG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 320202988 245 PAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTfsPEEMKQLNAL 292
Cdd:cd19121 234 PGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
10-292 |
1.53e-96 |
|
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: 286.86 E-value: 1.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTWKS--EPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKLWNTKHH 87
Cdd:cd19124 1 SGQTMPVIGMGTASDppSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 PEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDsthYKETWKALEALVAKGLVQALGLSNFNSR 167
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPFD---IKGVWEAMEECQRLGLTKAIGVSNFSCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 168 QIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDpdePVLLEEPVVLALAEKYGRSPAQ 247
Cdd:cd19124 158 KLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGS---NAVMESDVLKEIAAAKGKTVAQ 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 320202988 248 ILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNAL 292
Cdd:cd19124 235 VSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
6-293 |
1.84e-96 |
|
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: 285.81 E-value: 1.84e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 6 VLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTK 85
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA-----SGVPREELFITTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 86 HHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpFPKnadgticYDstHYKETWKALEALVAKGLVQALGLSNFN 165
Cdd:cd19131 77 QGYDSTLRAFDESLRKLGLDYVDLYLIHWP---------VPA-------QD--KYVETWKALIELKKEGRVKSIGVSNFT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 166 SRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALAEKYGRSP 245
Cdd:cd19131 139 IEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG----------LLSDPVIGEIAEKHGKTP 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 320202988 246 AQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN 293
Cdd:cd19131 209 AQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
5-292 |
2.81e-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: 285.76 E-value: 2.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 5 CVLLHTGQKMPLIGLGTWKSEpGQVKAAVKYALSV-GYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWN 83
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSG-GYSHEAVVYALKEcGYRHIDTAKRYGCEELLGKAIKE-----SGVPREDLFLTTKLWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNAdgticydsthykETWKALEALVAKGLVQALGLSN 163
Cdd:cd19135 78 SDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKETRA------------ETWRALEELYDEGLCRAIGVSN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 164 FNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSsdraWRdpdepvLLEEPVVLALAEKYGR 243
Cdd:cd19135 146 FLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAK----GK------ALEEPTVTELAKKYQK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 320202988 244 SPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNAL 292
Cdd:cd19135 216 TPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-293 |
3.70e-94 |
|
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: 280.45 E-value: 3.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTKHH 87
Cdd:cd19127 3 LNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRR-----SGVDRSDIFVTTKLWISDYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 PEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpFPKNADGTIcydsthykETWKALEALVAKGLVQALGLSNFNSR 167
Cdd:cd19127 78 YDKALRGFDASLRRLGLDYVDLYLLHWP---------VPNDFDRTI--------QAYKALEKLLAEGRVRAIGVSNFTPE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 168 QIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWR-DPDEPV-LLEEPVVLALAEKYGRSP 245
Cdd:cd19127 141 HLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGAsGPTGPGdVLQDPTITGLAEKYGKTP 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 320202988 246 AQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN 293
Cdd:cd19127 221 AQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-290 |
5.94e-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: 280.88 E-value: 5.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKaVPREELFVTSKLWNTKHHP 88
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGK-IRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 89 EDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDS-THYKETWKALEALVAKGLVQALGLSNFNSR 167
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 168 QIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSdrawrdpDEPVLLEEPVVLALAEKYGRSPAQ 247
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHG-------MEPKLLEDPVITAIARRVNKTPAQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 320202988 248 ILLRWQVQRKVICIPKSITPSRILQNikvFDFTFSPEE-MKQLN 290
Cdd:cd19129 233 VLLAWAIQRGTALLTTSKTPSRIREN---FDISTLPEDaMREIN 273
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
14-290 |
3.57e-93 |
|
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: 276.84 E-value: 3.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 14 MPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTKHHPEDVEP 93
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAE-----SGVPREDLFITTKVWRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 94 ALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgticydSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDIL 173
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLIHWP-------NP------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 174 SVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALAEKYGRSPAQILLRWQ 253
Cdd:cd19073 137 DISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE----------VLRDPVIQEIAEKYDKTPAQVALRWL 206
|
250 260 270
....*....|....*....|....*....|....*..
gi 320202988 254 VQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLN 290
Cdd:cd19073 207 VQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-292 |
1.55e-92 |
|
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: 276.71 E-value: 1.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 15 PLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGkAVPREELFVTSKLWNTKHHPEDVEPA 94
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDG-GVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 95 LRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILS 174
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 175 VASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSdrawRDPDEPVLLEEPVVLALAEKYGRSPAQILLRWQV 254
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGS----YGDGNLTFLNDSELKALATKYNTTPPQVIIAWHL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 320202988 255 QR---KVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNAL 292
Cdd:cd19128 237 QKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
6-298 |
4.50e-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: 275.17 E-value: 4.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 6 VLLHTGQKMPLIGLGTWKSEPGQVKA-AVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNT 84
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE-----SGVPREEVFVTTKLWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnpfpknadgticydsTHYKETWKALEALVAKGLVQALGLSNF 164
Cdd:cd19156 76 DQGYESTLAAFEESLEKLGLDYVDLYLIHWPVK--------------------GKFKDTWKAFEKLYKEKKVRAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 165 NSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALAEKYGRS 244
Cdd:cd19156 136 HEHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKYGKS 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 320202988 245 PAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRY 298
Cdd:cd19156 206 AAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
9-292 |
5.27e-91 |
|
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: 271.82 E-value: 5.27e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTKHHP 88
Cdd:cd19140 3 VNGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAA-----SGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 89 EDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpkNADGTIcydsthyKETWKALEALVAKGLVQALGLSNFNSRQ 168
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWP------------NKDVPL-------AETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 169 IDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALAEKYGRSPAQI 248
Cdd:cd19140 139 LREAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE----------VLKDPVLQEIGRKHGKTPAQV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 320202988 249 LLRWQVQR-KVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNAL 292
Cdd:cd19140 209 ALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
11-298 |
1.46e-86 |
|
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: 261.01 E-value: 1.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGT----WKSEPG--QVKAA--VKYALSVGYRHIDCAAIYGNEPEIGEALKEdVGpgkaVPREELFVTSKLW 82
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDdiQRDLVdsVKLALKAGFRHIDTAEMYGNEKEVGEALKE-SG----VPREDLFITTKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 83 ntkHHPEDVEPALRKTLADLQLEYLDLYLMHWPYafergdnpFPKNADGTIcydsthyKETWKALEALVAKGLVQALGLS 162
Cdd:cd19120 76 ---PGIKDPREALRKSLAKLGVDYVDLYLIHSPF--------FAKEGGPTL-------AEAWAELEALKDAGLVRSIGVS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 163 NFNSRQIDDILSVASVRPAVLQVECHPYLA--QNELIAHCQARGLEVTAYSPLGSsdrAWRDPDEPVlleEPVVLALAEK 240
Cdd:cd19120 138 NFRIEDLEELLDTAKIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSP---LTRDAGGPL---DPVLEKIAEK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 320202988 241 YGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRY 298
Cdd:cd19120 212 YGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-303 |
4.79e-85 |
|
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: 258.26 E-value: 4.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGkAVPREELFVTSKLWNTKHHPED 90
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEG-LVKREDLFIVTKLWNNFHGKDH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 91 VEPALRKTLADLQLEYLDLYLMHWPYAFERGD---NPFPKNADG---TICYDSTHYKETWKALEALVAKGLVQALGLSNF 164
Cdd:cd19114 80 VREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaeNYPFLWKDKelkKFPLEQSPMQECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 165 NSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSdrAWRDPDEPV-----LLEEPVVLALAE 239
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNA--VYTKVTKHLkhftnLLEHPVVKKLAD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320202988 240 KYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVPML 303
Cdd:cd19114 238 KHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPVV 301
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-293 |
9.83e-84 |
|
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: 253.35 E-value: 9.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTKHH 87
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR-----SGVPREELFVTTKLPGRHHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 PEDVEPALRKTLADLQLEYLDLYLMHWPyafergdNPFPKNadgticydsthYKETWKALEALVAKGLVQALGLSNFNSR 167
Cdd:cd19132 76 YEEALRTIEESLYRLGLDYVDLYLIHWP-------NPSRDL-----------YVEAWQALIEAREEGLVRSIGVSNFLPE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 168 QIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGssdrawRDPDepvLLEEPVVLALAEKYGRSPAQ 247
Cdd:cd19132 138 HLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG------RGSG---LLDEPVIKAIAEKHGKTPAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 320202988 248 ILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN 293
Cdd:cd19132 209 VVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-297 |
5.28e-83 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 252.30 E-value: 5.28e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTKHH 87
Cdd:PRK11565 9 LQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE-----ASVAREELFITTKLWNDDHK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 peDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknadgtiCYDSTHYKETWKALEALVAKGLVQALGLSNFNSR 167
Cdd:PRK11565 84 --RPREALEESLKKLQLDYVDLYLMHWP------------------VPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 168 QIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAwrdpdepvLLEEPVVLALAEKYGRSPAQ 247
Cdd:PRK11565 144 HLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG--------VFDQKVIRDLADKYGKTPAQ 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 320202988 248 ILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWR 297
Cdd:PRK11565 216 IVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-292 |
1.57e-82 |
|
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: 251.65 E-value: 1.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTW--KSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKaVPREELFVTSKLWNTK 85
Cdd:cd19119 6 LNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGS-IKREELFITTKVWPTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 86 HhpEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNP-----FPKNADGTICY-DSTHYKETWKALEALVAKGLVQAL 159
Cdd:cd19119 85 Y--DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDsgkpfTPVNDDGKTRYaASGDHITTYKQLEKIYLDGRAKAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 160 GLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAwrdpdepvLLEEPVVLALAE 239
Cdd:cd19119 163 GVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLVKKIAE 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 320202988 240 KYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTfsPEEMKQLNAL 292
Cdd:cd19119 235 KYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLT--KEDLQKLDDI 285
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-293 |
1.28e-78 |
|
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: 240.58 E-value: 1.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKedvgpGKAVPREELFVTSKLWNTKHH 87
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIA-----ASGIPRDELFVTTKLWNDRHD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 PEDVEPALRKTLADLQLEYLDLYLMHWPyAFERGDnpfpknadgticydsthYKETWKALEALVAKGLVQALGLSNFNSR 167
Cdd:cd19130 79 GDEPAAAFAESLAKLGLDQVDLYLVHWP-TPAAGN-----------------YVHTWEAMIELRAAGRTRSIGVSNFLPP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 168 QIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALAEKYGRSPAQ 247
Cdd:cd19130 141 HLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK----------LLGDPPVGAIAAAHGKTPAQ 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 320202988 248 ILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN 293
Cdd:cd19130 211 IVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
6-298 |
1.71e-75 |
|
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: 232.82 E-value: 1.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 6 VLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTK 85
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAA-----SGIPRGELFVTTKLATPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 86 HHPEDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnpfpknadgticyDSTHYKETWKALEALVAKGLVQALGLSNFN 165
Cdd:cd19134 78 QGFTASQAACRASLERLGLDYVDLYLIHWPAG------------------REGKYVDSWGGLMKLREEGLARSIGVSNFT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 166 SRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALAEKYGRSP 245
Cdd:cd19134 140 AEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR----------LLDNPAVTAIAAAHGRTP 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 320202988 246 AQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRY 298
Cdd:cd19134 210 AQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-294 |
2.52e-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: 230.59 E-value: 2.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 8 LHTGQKMPLIGLGTWKSE--PGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKLWNTK 85
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENPSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 86 HHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPK-NADG--TICYDSTHYKE-TWKALEALVAKGLVQALGL 161
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGkyVILKDLTENPEpTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 162 SNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEpvLLEEPVVLALAEKY 241
Cdd:cd19122 163 SNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGER--VSENPTLNEVAEKG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 320202988 242 GRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDftFSPEEMKQLNALNK 294
Cdd:cd19122 241 GYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQVAK 291
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
14-292 |
5.53e-67 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 210.29 E-value: 5.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 14 MPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTKHHPEDVEP 93
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE-----SGVPRDELFITTKIWIDNLSKDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 94 ALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgticYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDIL 173
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHWP-------SP----------NDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 174 SVASVRP-AVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGssdrawrdpdEPVLLEEPVVLALAEKYGRSPAQILLRW 252
Cdd:cd19139 139 AVVGAGAiATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA----------YGKVLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 320202988 253 QVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNAL 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 |
7.34e-66 |
|
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: 208.70 E-value: 7.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTW-------KSEPGQVKAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKEDvgpgkAVPREELFVTSKL----- 81
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDY-----PVKRDKVVIATKVpdgdg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 -WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAfergdnpfpknadgticydSTHYKETWKALEALVAKGLVQALG 160
Cdd:pfam00248 76 pWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-------------------DTPIEETWDALEELKKEGKIRAIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 161 LSNFNSRQIDDILSVASVRPAVLQVECHPY--LAQNELIAHCQARGLEVTAYSPLGS--------SDRAWRDPDEPVLLE 230
Cdd:pfam00248 137 VSNFDAEQIEKALTKGKIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytRDPDKGPGERRRLLK 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320202988 231 E---------PVVLALAEKYGRSPAQILLRW--QVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN 293
Cdd:pfam00248 217 KgtplnlealEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-290 |
2.13e-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: 204.00 E-value: 2.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGTWK---------SEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdvgpgkaVPREELFVT 78
Cdd:cd19072 1 GEEVPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG-------FDREDLFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 79 SKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgticydSTHYKETWKALEALVAKGLVQA 158
Cdd:cd19072 74 TKVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP-------NP------------SIPIEETLRAMEELVEEGKIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 159 LGLSNFNSRQIDDILSVASVRP-AVLQVECHPYL--AQNELIAHCQARGLEVTAYSPLGSSDRAwRDPDEPVLLEepvvl 235
Cdd:cd19072 135 IGVSNFSLEELEEAQSYLKKGPiVANQVEYNLFDreEESGLLPYCQKNGIAIIAYSPLEKGKLS-NAKGSPLLDE----- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 320202988 236 aLAEKYGRSPAQILLRWQVQRK-VICIPKSITPSRILQNIKVFDFTFSPEEMKQLN 290
Cdd:cd19072 209 -IAKKYGKTPAQIALNWLISKPnVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
13-301 |
7.03e-59 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 190.23 E-value: 7.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 13 KMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEdvgpgKAVPREELFVTSKLWNTKHHPEDVE 92
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE-----SGVPRDELFITTKIWIDNLAKDKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 93 PALRKTLADLQLEYLDLYLMHWPYafergdnpfPKNAdgticydsTHYKETWKALEALVAKGLVQALGLSNFN---SRQI 169
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHWPS---------PNDE--------VSVEEFMQALLEAKKQGLTREIGISNFTialMKQA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 170 DDILSVASVrpAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALAEKYGRSPAQIL 249
Cdd:PRK11172 140 IAAVGAENI--ATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK----------VLKDPVIARIAAKHNATPAQVI 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 320202988 250 LRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVP 301
Cdd:PRK11172 208 LAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSP 259
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-290 |
5.85e-57 |
|
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: 185.14 E-value: 5.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 5 CVLLHTGQKMPLIGLGTW-----KSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEDvgpgkavpREELF 76
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR--------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 77 VTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWpyafeRGDNPFpknadgticydsthyKETWKALEALVAKGLV 156
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHW-----RGGVPL---------------AETVAAMEELKKEGKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 157 QALGLSNFNSRQIDDILSVASVRP-AVLQVECHpyLAQ----NELIAHCQARGLEVTAYSPLGSSDRAWRDpdepvLLEE 231
Cdd:cd19138 134 RAWGVSNFDTDDMEELWAVPGGGNcAANQVLYN--LGSrgieYDLLPWCREHGVPVMAYSPLAQGGLLRRG-----LLEN 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 232 PVVLALAEKYGRSPAQILLRWQV-QRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLN 290
Cdd:cd19138 207 PTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-290 |
2.97e-52 |
|
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: 172.76 E-value: 2.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGTWK---------SEPGQVKAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKEdvgpgkaVPREELFVT 78
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD-------FPREDLFIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 79 SKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgticydSTHYKETWKALEALVAKGLVQA 158
Cdd:cd19137 74 TKVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP-------NP------------NIPLEETLSAMAEGVRQGLIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 159 LGLSNFNSRQIDDILSVASVRPAVLQVECHPY---LAQNELIAHCQARGLEVTAYSPLgssdrawrdpDEPVLLEEPVVL 235
Cdd:cd19137 135 IGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL----------RRGLEKTNRTLE 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 320202988 236 ALAEKYGRSPAQILLRWQVQR-KVICIPKSITPSRILQNIKVFDFTFSPEEMKQLN 290
Cdd:cd19137 205 EIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
9-292 |
2.43e-48 |
|
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: 164.20 E-value: 2.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGTW-------KSEPGQVKAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKEDvgpgkavPREELFVT 78
Cdd:COG0667 8 RSGLKVSRLGLGTMtfggpwgGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR-------PRDDVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 79 SKL--------WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknaDgticyDSTHYKETWKALEAL 150
Cdd:COG0667 81 TKVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP--------------D-----PDTPIEETLGALDEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 151 VAKGLVQALGLSNFNSRQIDDILSVAS--VRPAVLQVEchpY-----LAQNELIAHCQARGLEVTAYSPLGS-------- 215
Cdd:COG0667 142 VREGKIRYIGVSNYSAEQLRRALAIAEglPPIVAVQNE---YslldrSAEEELLPAARELGVGVLAYSPLAGglltgkyr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 216 -------SDRAWRDPDEPVLLEE-----PVVLALAEKYGRSPAQILLRWQVQRKVICIPksI----TPSRILQNIKVFDF 279
Cdd:COG0667 219 rgatfpeGDRAATNFVQGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSV--IpgarSPEQLEENLAAADL 296
|
330
....*....|...
gi 320202988 280 TFSPEEMKQLNAL 292
Cdd:COG0667 297 ELSAEDLAALDAA 309
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-290 |
5.80e-45 |
|
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: 155.08 E-value: 5.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTWK-----------SEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEDVgpgkavPREELFVTSKLW 82
Cdd:cd19093 5 LGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG------DRDEVVIATKFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 83 NT--KHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFpknadgticydsthyketWKALEALVAKGLVQALG 160
Cdd:cd19093 79 PLpwRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLVRAVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 161 LSNFNSRQI---DDILSVASVRPAVLQVE---CHPYLAQNELIAHCQARGLEVTAYSPLG--------SSDRAWRDPDEP 226
Cdd:cd19093 141 VSNYSADQLrraHKALKERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPPPGGRRR 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320202988 227 VLLEE------PVVLAL---AEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLN 290
Cdd:cd19093 221 LFGRKnlekvqPLLDALeeiAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-295 |
2.78e-42 |
|
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: 147.73 E-value: 2.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTW---------KSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdvgpgkavPREELFVTSKLWNT 84
Cdd:cd19085 4 LGLGCWqfgggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG--------RRDDVVIATKVSPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 85 KHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafeRGDNPFpknadgticydsthyKETWKALEALVAKGLVQALGLSNF 164
Cdd:cd19085 76 NLTPEDVRKSCERSLKRLGTDYIDLYQIHWP----SSDVPL---------------EETMEALEKLKEEGKIRAIGVSNF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 165 NSRQIDDILSVAsvRPAVLQVechPY-L----AQNELIAHCQARGLEVTAYSPL------GSSDRAWRDPDE------PV 227
Cdd:cd19085 137 GPAQLEEALDAG--RIDSNQL---PYnLlwraIEYEILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlFR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 228 LLEEPV----------VLALAEKYGRSPAQILLRWQVQRKVI--CIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKN 295
Cdd:cd19085 212 HFEPGAeeetfealekLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
17-290 |
1.15e-38 |
|
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: 138.43 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTW--------KSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEDvgpgkavpREELFVTSK---LW 82
Cdd:cd19084 7 IGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR--------RDDVVIATKcglRW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 83 NTKHH------PEDVEPALRKTLADLQLEYLDLYLMHWPyafergDNPFPKNadgticydsthykETWKALEALVAKGLV 156
Cdd:cd19084 79 DGGKGvtkdlsPESIRKEVEQSLRRLQTDYIDLYQIHWP------DPNTPIE-------------ETAEALEKLKKEGKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 157 QALGLSNFNSRQIDDILSVASVrpAVLQVechPY--LAQN---ELIAHCQARGLEVTAYSPLG---------------SS 216
Cdd:cd19084 140 RYIGVSNFSVEQLEEARKYGPI--VSLQP---PYsmLEREieeELLPYCRENGIGVLPYGPLAqglltgkykkeptfpPD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 217 DRAWRDPD--EPVLLEEPVVLA----LAEKYGRSPAQILLRWQVQRK----VICIPKsiTPSRILQNIKVFDFTFSPEEM 286
Cdd:cd19084 215 DRRSRFPFfrGENFEKNLEIVDklkeIAEKYGKSLAQLAIAWTLAQPgvtsAIVGAK--NPEQLEENAGALDWELTEEEL 292
|
....
gi 320202988 287 KQLN 290
Cdd:cd19084 293 KEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-275 |
1.83e-34 |
|
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: 125.71 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTW----KSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEDVgpgkavPREELFVTSKLWNTKH--- 86
Cdd:cd06660 3 LGLGTMtfggDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRG------NRDDVVIATKGGHPPGgdp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 87 -----HPEDVEPALRKTLADLQLEYLDLYLMHWpyafergDNPfpknadgticydSTHYKETWKALEALVAKGLVQALGL 161
Cdd:cd06660 77 srsrlSPEHIRRDLEESLRRLGTDYIDLYYLHR-------DDP------------STPVEETLEALNELVREGKIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 162 SNFNSRQIDDILSVAS----VRPAVLQVE---CHPYLAQNELIAHCQARGLEVTAYSPLgssdrawrdpdepvlleepvv 234
Cdd:cd06660 138 SNWSAERLAEALAYAKahglPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPL--------------------- 196
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 320202988 235 lalaekyGRSPAQILLRWQVQRK--VICIPKSITPSRILQNIK 275
Cdd:cd06660 197 -------ARGPAQLALAWLLSQPfvTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-292 |
1.26e-32 |
|
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: 122.78 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTWKSEPGQ------------VKAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKEdvgpgkavPREELFVTSK- 80
Cdd:cd19102 4 IGLGTWAIGGGGwgggwgpqddrdSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKG--------LRDRPIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 81 --LWNTKHH------PEDVEPALRKTLADLQLEYLDLYLMHWPYaferGDNPFpknadgticydsthyKETWKALEALVA 152
Cdd:cd19102 76 glLWDEEGRirrslkPASIRAECEASLRRLGVDVIDLYQIHWPD----PDEPI---------------EEAWGALAELKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 153 KGLVQALGLSNFNSRQIDDILSVASVrpAVLQVechPYLA-----QNELIAHCQARGLEVTAYSPLGS--------SDRA 219
Cdd:cd19102 137 EGKVRAIGVSNFSVDQMKRCQAIHPI--ASLQP---PYSLlrrgiEAEILPFCAEHGIGVIVYSPMQSglltgkmtPERV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 220 WRDPD------EPVLLEE---------PVVLALAEKYGRSPAQILLRWQVQRKVI--CIPKSITPSRILQNIKVFDFTFS 282
Cdd:cd19102 212 ASLPAddwrrrSPFFQEPnlarnlalvDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLT 291
|
330
....*....|
gi 320202988 283 PEEMKQLNAL 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 |
1.07e-27 |
|
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: 109.60 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGT----------WKSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdvgpgkAVPREEL 75
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKE------FAPRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 76 FVTSKLwntkHHPEDVEP------------ALRKTLADLQLEYLDLYLMHWPyafergdnpfpknaDgticyDSTHYKET 143
Cdd:cd19079 81 VIATKV----YFPMGDGPngrglsrkhimaEVDASLKRLGTDYIDLYQIHRW--------------D-----YETPIEET 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 144 WKALEALVAKGLVQALGLSNFNSRQIDDILSVASV----RPAVLQvechPYL------AQNELIAHCQARGLEVTAYSPL 213
Cdd:cd19079 138 LEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKngwtKFVSMQ----NHYnllyreEEREMIPLCEEEGIGVIPWSPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 214 ----------GSSDRAWRDPDEPVLLE-------EPV---VLALAEKYGRSPAQILLRWQVQRKVICIPksI----TPSR 269
Cdd:cd19079 214 argrlarpwgDTTERRRSTTDTAKLKYdyfteadKEIvdrVEEVAKERGVSMAQVALAWLLSKPGVTAP--IvgatKLEH 291
|
330 340
....*....|....*....|.
gi 320202988 270 ILQNIKVFDFTFSPEEMKQLN 290
Cdd:cd19079 292 LEDAVAALDIKLSEEEIKYLE 312
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-297 |
3.64e-25 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 103.75 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGTW----KSEPgQVKAAVKYALSVGYRHIDCAAIYGN-EPEIGEALKEdvgpgkavPREELFVTSKLWN 83
Cdd:COG1453 8 KTGLEVSVLGFGGMrlprKDEE-EAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG--------PRDKVILATKLPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 84 TKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNadgticydsthykETWKALEALVAKGLVQALGLSN 163
Cdd:COG1453 79 WVRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKPG-------------GALEALEKAKAEGKIRHIGFST 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 164 FNSrqIDDILS-VASVRPAVLQVECHP----YLAQNELIAHCQARGLEVTAYSPLGSSDrawrdpdepvLLEEPVVLALA 238
Cdd:COG1453 146 HGS--LEVIKEaIDTGDFDFVQLQYNYldqdNQAGEEALEAAAEKGIGVIIMKPLKGGR----------LANPPEKLVEL 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320202988 239 EKYGRSPAQILLRWQVQRKVICIPKS--ITPSRILQNIKVFD--FTFSPEEMKQLNALNKNWR 297
Cdd:COG1453 214 LCPPLSPAEWALRFLLSHPEVTTVLSgmSTPEQLDENLKTADnlEPLTEEELAILERLAEELG 276
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
14-282 |
4.01e-25 |
|
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: 101.53 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 14 MPLIGLGTWK--SEPGQVKAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKedvgpgkavPR-EELFVTSKL------ 81
Cdd:cd19088 9 MRLTGPGIWGppADREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALH---------PYpDDVVIATKGglvrtg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 ---WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPyafergDNPFPknadgticydsthYKETWKALEALVAKGLVQA 158
Cdd:cd19088 80 pgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI------DPKVP-------------FEEQLGALAELQDEGLIRH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 159 LGLSNFNSRQIDDILSVASVrpAVLQVECHPYLAQNE-LIAHCQARGLEVTAYSPLGSsdrawrdpdEPVLLEEPVVLAL 237
Cdd:cd19088 141 IGLSNVTVAQIEEARAIVRI--VSVQNRYNLANRDDEgVLDYCEAAGIAFIPWFPLGG---------GDLAQPGGLLAEV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 320202988 238 AEKYGRSPAQILLRWQVQRK--VICIPKSITPSRILQNIKVFDFTFS 282
Cdd:cd19088 210 AARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
17-284 |
5.29e-24 |
|
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: 99.20 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTWKSEPGQV-----KAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdvgpgkaVPREELFVTSKL-WNTKHH 87
Cdd:cd19074 7 LSLGTWLTFGGQVddedaKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG-------WPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 88 PED--------VEpALRKTLADLQLEYLDLYLMHwpyafeRGDnpfpknadgticyDSTHYKETWKALEALVAKGLVQAL 159
Cdd:cd19074 80 PNDrglsrkhiFE-SIHASLKRLQLDYVDIYYCH------RYD-------------PETPLEETVRAMDDLIRQGKILYW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 160 GLSNFNSRQIDDILSVAS----VRPAVLQVECHpYLAQ---NELIAHCQARGLEVTAYSPL-----------------GS 215
Cdd:cd19074 140 GTSEWSAEQIAEAHDLARqfglIPPVVEQPQYN-MLWReieEEVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsRS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320202988 216 SDRAWRDPDEPVLLEEPVVLA-------LAEKYGRSPAQILLRWQVQRKVIC--IPKSITPSRILQNIKVFDFTFSPE 284
Cdd:cd19074 219 RATDEDNRDKKRRLLTDENLEkvkklkpIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-285 |
1.32e-23 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 98.01 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 18 GLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEDvgPGKavpREELFVTSK----------LWNT 84
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN--PGL---REKIEIQTKcgirlgddprPGRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 85 KHH---PEDVEPALRKTLADLQLEYLDLYLMHWPYAFergdnpfpknadgticydsTHYKETWKALEALVAKGLVQALGL 161
Cdd:cd19092 90 KHYdtsKEHILASVEGSLKRLGTDYLDLLLLHRPDPL-------------------MDPEEVAEAFDELVKSGKVRYFGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 162 SNFNSRQIDDILSVASVRPAVLQVEC---HPYLAQNELIAHCQARGLEVTAYSPLG----SSDRAWRDPDEPVLLEEpvv 234
Cdd:cd19092 151 SNFTPSQIELLQSYLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGggrlFGGFDERFQRLRAALEE--- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 320202988 235 laLAEKYGRSPAQILLRWqVQR---KVICIPKSITPSRILQNIKVFDFTFSPEE 285
Cdd:cd19092 228 --LAEEYGVTIEAIALAW-LLRhpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
9-292 |
4.92e-23 |
|
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: 96.91 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGT--------WKSEPGQVKAA-----VKYALSVGYRHIDCAAIYGN-EPEI--GEALKEDvgpgkavpR 72
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggFFGAWGGVDQEeadrlVDIALDAGINFFDTADVYSEgESEEilGKALKGR--------R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 73 EELFVTSKLWN-----------TKHHpedVEPALRKTLADLQLEYLDLYLMHWpyafergdnpfpknadgticYDS-THY 140
Cdd:cd19091 80 DDVLIATKVRGrmgegpndvglSRHH---IIRAVEASLKRLGTDYIDLYQLHG--------------------FDAlTPL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 141 KETWKALEALVAKGLVQALGLSNFNSRQIDDILSVAS----VRPAVLQVecHPYLA----QNELIAHCQARGLEVTAYSP 212
Cdd:cd19091 137 EETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQA--YYSLLgrdlEHELMPLALDQGVGLLVWSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 213 LG--------------SSDRAWRD--PDEPVLLEE---PVVLAL---AEKYGRSPAQILLRWQVQRKVIcipKSI----- 265
Cdd:cd19091 215 LAggllsgkyrrgqpaPEGSRLRRtgFDFPPVDRErgyDVVDALreiAKETGATPAQVALAWLLSRPTV---SSViigar 291
|
330 340
....*....|....*....|....*..
gi 320202988 266 TPSRILQNIKVFDFTFSPEEMKQLNAL 292
Cdd:cd19091 292 NEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
15-278 |
3.01e-22 |
|
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: 93.78 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 15 PLIGLGT------WKSE--PGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdvgpgkaVPREELFVTSKL-W 82
Cdd:cd19096 1 SVLGFGTmrlpesDDDSidEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE-------GPREKFYLATKLpP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 83 NTKHHPEDVEPALRKTLADLQLEYLDLYLMH------WPYAFERGDnpfpknadgticydsthykeTWKALEALVAKGLV 156
Cdd:cd19096 74 WSVKSAEDFRRILEESLKRLGVDYIDFYLLHglnspeWLEKARKGG--------------------LLEFLEKAKKEGLI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 157 QALGLSnF--NSRQIDDILSVASVRPAVLQvecHPYLAQN-----ELIAHCQARGLEVTAYSPLGSSDRAWRdpdepvll 229
Cdd:cd19096 134 RHIGFS-FhdSPELLKEILDSYDFDFVQLQ---YNYLDQEnqagrPGIEYAAKKGMGVIIMEPLKGGGLANN-------- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 320202988 230 eEPVVLALAEKYGRSPAQILLRWQV-QRKVICIpkSI---TPSRILQNIKVFD 278
Cdd:cd19096 202 -PPEALAILCGAPLSPAEWALRFLLsHPEVTTV--LSgmsTPEQLDENIAAAD 251
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
10-290 |
1.02e-21 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 93.07 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLG----TWKSEP---GQVKAAVKYALSVGYRHIDCAAIYGNEPE------IGEALKedvgpgkAVP--REE 74
Cdd:cd19077 1 NGKLVGPIGLGlmglTWRPNPtpdEEAFETMKAALDAGSNLWNGGEFYGPPDPhanlklLARFFR-------KYPeyADK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 75 LFVTSKL-WNTKHH-----PEDVEPALRKTLADL-QLEYLDLYLMhwpyafERGDnpfpknadgticyDSTHYKETWKAL 147
Cdd:cd19077 74 VVLSVKGgLDPDTLrpdgsPEAVRKSIENILRALgGTKKIDIFEP------ARVD-------------PNVPIEETIKAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 148 EALVAKGLVQALGLSNFNSRQIDDILSVASVrpAVLQVECHPY---LAQNELIAHCQARGLEVTAYSPLGSS--DRAWRD 222
Cdd:cd19077 135 KELVKEGKIRGIGLSEVSAETIRRAHAVHPI--AAVEVEYSLFsreIEENGVLETCAELGIPIIAYSPLGRGllTGRIKS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 223 PDE--------------PVLLEEPVVLA-----LAEKYGRSPAQILLRW---QVQRKVICIPKSITPSRILQNIKVFDFT 280
Cdd:cd19077 213 LADipegdfrrhldrfnGENFEKNLKLVdalqeLAEKKGCTPAQLALAWilaQSGPKIIPIPGSTTLERVEENLKAANVE 292
|
330
....*....|
gi 320202988 281 FSPEEMKQLN 290
Cdd:cd19077 293 LTDEELKEIN 302
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
44-290 |
1.24e-21 |
|
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: 93.05 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 44 IDCAAIYGN---EPEIGEALKEDvgpgkavpREELFVTSKL-WNTkhHPEDVEP----------ALRKTLADLQLEYLDL 109
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAGN--------RDRIVLATKYtMNR--RPGDPNAggnhrknlrrSVEASLRRLQTDYIDL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 110 YLMHWPyafergdnpfpknaDGTicydsTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVR----PAVLQV 185
Cdd:cd19080 118 LYVHAW--------------DFT-----TPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRgwspFVALQI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 186 ECHpyLAQ----NELIAHCQARGLEVTAYSPLGS--------------SDRAWRDPDEPVLLEE------PVVLALAEKY 241
Cdd:cd19080 179 EYS--LLErtpeRELLPMARALGLGVTPWSPLGGglltgkyqrgeegrAGEAKGVTVGFGKLTErnwaivDVVAAVAEEL 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 320202988 242 GRSPAQILLRWQVQRKVICIPkSITPSRILQ---NIKVFDFTFSPEEMKQLN 290
Cdd:cd19080 257 GRSAAQVALAWVRQKPGVVIP-IIGARTLEQlkdNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
40-290 |
2.87e-21 |
|
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: 91.89 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 40 GYRHIDCAAIY--------GNEPE--IGEALKedvgpgKAVPREELFVTSKL-WNTKH-----HPEDVEPALRKTLADLQ 103
Cdd:cd19081 39 GGNFIDTADVYsawvpgnaGGESEtiIGRWLK------SRGKRDRVVIATKVgFPMGPngpglSRKHIRRAVEASLRRLQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 104 LEYLDLYLMHWPyafergdnpfpknaDgticyDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVAS----VR 179
Cdd:cd19081 113 TDYIDLYQAHWD--------------D-----PATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhglPR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 180 PAVLQVECHPY---LAQNELIAHCQARGLEVTAYSPLGS-------------SDRAWRDPDEPVLLEEP------VVLAL 237
Cdd:cd19081 174 YVSLQPEYNLVdreSFEGELLPLCREEGIGVIPYSPLAGgfltgkyrseadlPGSTRRGEAAKRYLNERglrildALDEV 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 320202988 238 AEKYGRSPAQILLRWQVQRKVICIPksI----TPSRILQNIKVFDFTFSPEEMKQLN 290
Cdd:cd19081 254 AAEHGATPAQVALAWLLARPGVTAP--IagarTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
9-289 |
4.71e-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: 91.57 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGTW---------KSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKedvgpGKavpREELF 76
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIK-----GR---RDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 77 VTSK---LWNTK---HHPEDVEPALRK-------------TLADLQLEYLDLYLMHWPyafergDNPFPknadgticyds 137
Cdd:cd19149 78 LATKcglRWDREggsFFFVRDGVTVYKnlspesireeveqSLKRLGTDYIDLYQTHWQ------DVETP----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 138 thYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVrpAVLQVechPY-----LAQNELIAHCQARGLEVTAYSP 212
Cdd:cd19149 141 --IEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQE---KYsmldrGIEKELLPYCKKNNIAFQAYSP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 213 LGS-------------------SDRAWRDPD--EPV--LLEEpvVLALAEKYGRSPAQILLRWQVQR----KVICipKSI 265
Cdd:cd19149 214 LEQglltgkitpdrefdagdarSGIPWFSPEnrEKVlaLLEK--WKPLCEKYGCTLAQLVIAWTLAQpgitSALC--GAR 289
|
330 340
....*....|....*....|....
gi 320202988 266 TPSRILQNIKVFDFTFSPEEMKQL 289
Cdd:cd19149 290 KPEQAEENAKAGDIRLSAEDIATM 313
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
36-289 |
5.75e-21 |
|
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: 91.12 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 36 ALSVGYRHIDCAAIYG---NEPEIGEALKEdvgpgkavPREELFVTSK---LWNTKHH-------PEDVEPALRKTLADL 102
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKD--------RRDEVVIATKfgiVRDPGSGfrgvdgrPEYVRAACEASLKRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 103 QLEYLDLYLMHwpyafeRGDnpfpknadgticyDSTHYKETWKALEALVAKGLVQALGLSNFNSrqiDDILSVASVRP-A 181
Cdd:cd19076 113 GTDVIDLYYQH------RVD-------------PNVPIEETVGAMAELVEEGKVRYIGLSEASA---DTIRRAHAVHPiT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 182 VLQVECHPYL--AQNELIAHCQARGLEVTAYSPLGssdR-----AWRDPDEP---------------------VLLEEpv 233
Cdd:cd19076 171 AVQSEYSLWTrdIEDEVLPTCRELGIGFVAYSPLG---RgfltgAIKSPEDLpeddfrrnnprfqgenfdknlKLVEK-- 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 320202988 234 VLALAEKYGRSPAQILLRWQVQRK--VICIPKSITPSRILQNIKVFDFTFSPEEMKQL 289
Cdd:cd19076 246 LEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-291 |
3.02e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 89.19 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 20 GTW---------KSEPGQVKAAVKYAlSVGYRHIDCAAIYGN-EPEIGEALKEDVGPG----------KAVPR-EELFVT 78
Cdd:cd19101 8 GMWqlsgghggiRDEDAAVRAMAAYV-DAGLTTFDCADIYGPaEELIGEFRKRLRRERdaaddvqihtKWVPDpGELTMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 79 sklwntkhhPEDVEPALRKTLADLQLEYLDLYLMHWpyafergdnpfpknADgticYDSTHYKETWKALEALVAKGLVQA 158
Cdd:cd19101 87 ---------RAYVEAAIDRSLKRLGVDRLDLVQFHW--------------WD----YSDPGYLDAAKHLAELQEEGKIRH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 159 LGLSNFNSRQIDDILSvASVRPAVLQVEcHPYL---AQNELIAHCQARGLEVTAYSPLGS---SDRaWRDPDEPV----- 227
Cdd:cd19101 140 LGLTNFDTERLREILD-AGVPIVSNQVQ-YSLLdrrPENGMAALCEDHGIKLLAYGTLAGgllSEK-YLGVPEPTgpale 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 228 ----------------------LLEepVVLALAEKYGRSPAQILLRWQVQRKviCIPKSITPSR----ILQNIKVFDFTF 281
Cdd:cd19101 217 trslqkyklmidewggwdlfqeLLR--TLKAIADKHGVSIANVAVRWVLDQP--GVAGVIVGARnsehIDDNVRAFSFRL 292
|
330
....*....|
gi 320202988 282 SPEEMKQLNA 291
Cdd:cd19101 293 DDEDRAAIDA 302
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-252 |
5.37e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 87.25 E-value: 5.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTwKSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdvgpgkaVPREELFVTSKLWNTKH 86
Cdd:cd19105 9 TGLKVSRLGFGG-GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG-------LRRDKVFLATKASPRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 87 H--PEDVEPALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgTICYDSTHYK--ETWKALEALVAKGLVQALGls 162
Cdd:cd19105 81 KkdKAELLKSVEESLKRLQTDYIDIYQLH------------------GVDTPEERLLneELLEALEKLKKEGKVRFIG-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 163 nfnsrqiddiLSVASVRPAVLQ--VECHPY----LAQN---------ELIAHCQARGLEVTAYSPLGSsdRAWRDPDEPV 227
Cdd:cd19105 141 ----------FSTHDNMAEVLQaaIESGWFdvimVAYNflnqpaeleEALAAAAEKGIGVVAMKTLAG--GYLQPALLSV 208
|
250 260
....*....|....*....|....*
gi 320202988 228 LLEEpvvlalaekyGRSPAQILLRW 252
Cdd:cd19105 209 LKAK----------GFSLPQAALKW 223
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
30-292 |
7.21e-20 |
|
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: 88.01 E-value: 7.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 30 KAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEDvgpgkavpREELFVTSKLwntkHHPEDVEP------------A 94
Cdd:cd19087 33 FAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR--------RDDIVLATKV----FGPMGDDPndrglsrrhirrA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 95 LRKTLADLQLEYLDLYLMHwpyafergdNPFPKnadgticydsTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILS 174
Cdd:cd19087 101 VEASLRRLQTDYIDLYQMH---------HFDRD----------TPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 175 VASVRP-AVLQVECHPY-----LAQNELIAHCQARGLEVTAYSPLG--------------SSDRAWRDPDEPVLLEEPVV 234
Cdd:cd19087 162 IAARRGlLRFVSEQPMYnllkrQAELEILPAARAYGLGVIPYSPLAgglltgkygkgkrpESGRLVERARYQARYGLEEY 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320202988 235 LALAEKY-------GRSPAQILLRWQVQRKVICIPkSITPSRILQ---NIKVFDFTFSPEEMKQLNAL 292
Cdd:cd19087 242 RDIAERFealaaeaGLTPASLALAWVLSHPAVTSP-IIGPRTLEQledSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
10-287 |
9.92e-20 |
|
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: 87.70 E-value: 9.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTWK-----SEPGQVKAAVKYALSVGYRHIDCAAIYGNEP-----EIGEALKEDVGPgkavPREELFVTS 79
Cdd:cd19089 7 SGLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYGPPPgsaeeNFGRILKRDLRP----YRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 80 KL-----------WNTKHHpedVEPALRKTLADLQLEYLDLYLMHwpyafergdnpfpknadgtiCYD-STHYKETWKAL 147
Cdd:cd19089 83 KAgygmwpgpygdGGSRKY---LLASLDQSLKRMGLDYVDIFYHH--------------------RYDpDTPLEETMTAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 148 EALVAKGLVQALGLSNFNS---RQIDDILSVASVRPAVLQVechPY-----LAQNELIAHCQARGLEVTAYSPLGS---S 216
Cdd:cd19089 140 ADAVRSGKALYVGISNYPGakaRRAIALLRELGVPLIIHQP---RYslldrWAEDGLLEVLEEAGIGFIAFSPLAQgllT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 217 DRAWRDPDE------------PVLLEEPVVLAL------AEKYGRSPAQILLRWQVQRKVIC---IPKSiTPSRILQNIK 275
Cdd:cd19089 217 DKYLNGIPPdsrraaeskfltEEALTPEKLEQLrklnkiAAKRGQSLAQLALSWVLRDPRVTsvlIGAS-SPSQLEDNVA 295
|
330
....*....|...
gi 320202988 276 VFDFT-FSPEEMK 287
Cdd:cd19089 296 ALKNLdFSEEELA 308
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-226 |
1.03e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 86.38 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 6 VLLHTGQKMPLIGLGT---WKSEPGQVKAAVKYALSVGYRHIDCAAIYGN-EPEIGEALKEdvgpgkavPREELFVTSKL 81
Cdd:cd19100 3 RLGRTGLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG--------RRDKVFLATKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 WNTKhhPEDVEPALRKTLADLQLEYLDLYLMH-------WPYAFERGdnpfpknadgticydsthykETWKALEALVAKG 154
Cdd:cd19100 75 GARD--YEGAKRDLERSLKRLGTDYIDLYQLHavdteedLDQVFGPG--------------------GALEALLEAKEEG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320202988 155 LVQALGLSNFNsrqiDDILSVASVRPA--VLQVECHPYLAQN-----ELIAHCQARGLEVTAYSPLGSSDRAWRDPDEP 226
Cdd:cd19100 133 KIRFIGISGHS----PEVLLRALETGEfdVVLFPINPAGDHIdsfreELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP 207
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
17-276 |
1.21e-19 |
|
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: 85.99 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTW--------KSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdvgpgkavPREELFVTSKLWNTK 85
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG--------RRDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 86 HH---------PEDVEPALRKTLADLQLEYLDLYLMH-WPYAFERGDnpfpknadgticydsthykETWKALEALVAKGL 155
Cdd:cd19086 78 DGgperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDND-------------------ELFEALEKLKQEGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 156 VQALGLSnfnSRQIDDILSVASVRPA-VLQV-----ECHPYlaqNELIAHCQARGLEVTAYSPLGSSdrawrdpdepvll 229
Cdd:cd19086 139 IRAYGVS---VGDPEEALAALRRGGIdVVQViynllDQRPE---EELFPLAEEHGVGVIARVPLASG------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 320202988 230 eepvvlALAEKygrsPAQILLRWQVQRKVIC--IPKSITPSRILQNIKV 276
Cdd:cd19086 200 ------LLTGK----LAQAALRFILSHPAVStvIPGARSPEQVEENAAA 238
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-276 |
2.30e-19 |
|
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: 85.75 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTWK-------SEPGQVKAAVKYALSVGYRHIDCAAIYGN-EPEIGEALKEdvgpgkaVPREELFVTSKLW------ 82
Cdd:cd19095 3 LGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG-------LRRDDLFIATKVGthgegg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 83 -NTKHH-PEDVEPALRKTLADLQLEYLDLYLMHwpyaferGDNPfPKNADGTIcydsthyketwKALEALVAKGLVQALG 160
Cdd:cd19095 76 rDRKDFsPAAIRASIERSLRRLGTDYIDLLQLH-------GPSD-DELTGEVL-----------ETLEDLKAAGKVRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 161 LSNFNSRqIDDILsvASVRPAVLQVechPY--LAQNE--LIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLA 236
Cdd:cd19095 137 VSGDGEE-LEAAI--ASGVFDVVQL---PYnvLDREEeeLLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 320202988 237 LAEKYG-RSPAQILLRWQVQRKVI--CIPKSITPSRILQNIKV 276
Cdd:cd19095 211 FAAEIGgATWAQAALRFVLSHPGVssAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
17-292 |
2.58e-18 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 83.62 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGT-----------WKSEPGqvKAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKEDVgpgkavpREELFVTSK-- 80
Cdd:cd19083 14 IGLGTnavgghnlypnLDEEEG--KDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYN-------RNEVVIATKga 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 81 LWNTKH------HPEDVEPALRKTLADLQLEYLDLYLMHWPyafergDNPFPKNadgticydsthykETWKALEALVAKG 154
Cdd:cd19083 85 HKFGGDgsvlnnSPEFLRSAVEKSLKRLNTDYIDLYYIHFP------DGETPKA-------------EAVGALQELKDEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 155 LVQALGLSNFNSRQI-----DDILSVASVRPAVLQVEchpylAQNELIAHCQARGLEVTAYSPLGS-------------S 216
Cdd:cd19083 146 KIRAIGVSNFSLEQLkeankDGYVDVLQGEYNLLQRE-----AEEDILPYCVENNISFIPYFPLASgllagkytkdtkfP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 217 DRAWRDpDEPVLLEEPV---------VLALAEKYGRSPAQILLRWQVQRKVI--CIPKSITPSRILQNIKVFDFTFSPEE 285
Cdd:cd19083 221 DNDLRN-DKPLFKGERFsenldkvdkLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEE 299
|
....*..
gi 320202988 286 MKQLNAL 292
Cdd:cd19083 300 IAFIDAL 306
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-289 |
4.48e-18 |
|
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: 83.26 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGTW-------KSEPGQVKAAV-KYALSVGYRHIDCAAIYG-NEPEIGEALKEDvgPGKavpREELFVTSKL 81
Cdd:cd19144 10 GPSVPALGFGAMglsafygPPKPDEERFAVlDAAFELGCTFWDTADIYGdSEELIGRWFKQN--PGK---REKIFLATKF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 WNTKH----------HPEDVEPALRKTLADLQLEYLDLYLMHwpyafeRGDNPFPknadgticydsthYKETWKALEALV 151
Cdd:cd19144 85 GIEKNvetgeysvdgSPEYVKKACETSLKRLGVDYIDLYYQH------RVDGKTP-------------IEKTVAAMAELV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 152 AKGLVQALGLSNFNSrqiDDILSVASVRP-AVLQVECHPYL-----AQNELIAHCQARGLEVTAYSPLGSS--DRAWRDP 223
Cdd:cd19144 146 QEGKIKHIGLSECSA---ETLRRAHAVHPiAAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRGflTGAIRSP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 224 DE----------PVLLEE--PVVL-------ALAEKYGRSPAQILLRWQVQRK--VICIPKSITPSRILQNIKVFDFTFS 282
Cdd:cd19144 223 DDfeegdfrrmaPRFQAEnfPKNLelvdkikAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLT 302
|
....*..
gi 320202988 283 PEEMKQL 289
Cdd:cd19144 303 EEEEKEI 309
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-252 |
6.67e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 82.75 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTWKSEPG-----QVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEDVGPGKaVPREELFVTSK-------- 80
Cdd:cd19099 6 LGLGTYRGDSDdetdeEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGG-IKRDEVVIVTKagyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 81 -----------------LWNTK------H--HPEDVEPALRKTLADLQLEYLDLYLMHWPYAF--ERGDNPFpknadgti 133
Cdd:cd19099 85 deplrplkyleeklgrgLIDVAdsaglrHciSPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQllELGEEEF-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 134 cYDstHYKETWKALEALVAKGLVQALGLSNFN-------SRQIDDILSVASVRPAVLQVECH------PY-LAQNE---- 195
Cdd:cd19099 157 -YD--RLEEAFEALEEAVAEGKIRYYGISTWDgfrappaLPGHLSLEKLVAAAEEVGGDNHHfkviqlPLnLLEPEalte 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320202988 196 ----------LIAHCQARGLEVTAYSPL--GSSDRAWRDPDEPvlleepvvlalAEKYGRSPAQILLRW 252
Cdd:cd19099 234 kntvkgealsLLEAAKELGLGVIASRPLnqGQLLGELRLADLL-----------ALPGGATLAQRALQF 291
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
11-213 |
2.88e-17 |
|
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: 80.81 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 11 GQKMPLIGLGTWK--------SEPGQVKAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKEdvgpgkAVPREELFVTS 79
Cdd:cd19148 1 DLPVSRIALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKE------YGKRDRVVIAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 80 KL---WNTKHHP----------EDVEPALRKtladLQLEYLDLYLMHWPyafergdnpfpknaDgticyDSTHYKETWKA 146
Cdd:cd19148 75 KVgleWDEGGEVvrnssparirKEVEDSLRR----LQTDYIDLYQVHWP--------------D-----PLVPIEETAEA 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320202988 147 LEALVAKGLVQALGLSNFNSRQIDDILSVASVrpAVLQVechPY-----LAQNELIAHCQARGLEVTAYSPL 213
Cdd:cd19148 132 LKELLDEGKIRAIGVSNFSPEQMETFRKVAPL--HTVQP---PYnlferEIEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
28-290 |
4.01e-17 |
|
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: 80.35 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 28 QVKAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKEdvgpgkavPREELFVTSK----LWNTKHH-------PEDVEP 93
Cdd:cd19078 26 EMIELIRKAVELGITFFDTAEVYGpytNEELVGEALKP--------FRDQVVIATKfgfkIDGGKPGplgldsrPEHIRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 94 ALRKTLADLQLEYLDLYLMHwpyafeRGDnpfpknadgticyDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDIL 173
Cdd:cd19078 98 AVEGSLKRLQTDYIDLYYQH------RVD-------------PNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 174 SVASVrpAVLQVECH-----PylaQNELIAHCQARGLEVTAYSPLG----------------SSDRAW--RDPDEPV--- 227
Cdd:cd19078 159 AVCPV--TAVQSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGkgfltgkidentkfdeGDDRASlpRFTPEALean 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320202988 228 --LLEepVVLALAEKYGRSPAQILLRWQVQRK--VICIPKSITPSRILQNIKVFDFTFSPEEMKQLN 290
Cdd:cd19078 234 qaLVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
35-292 |
1.22e-16 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 79.15 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 35 YALSVGYRHIDCAAIY---------G-NEPEIGEALKedvgpgKAVPREELFVTSKL--------W----NTKHHPEDVE 92
Cdd:cd19094 26 YAFDEGVNFIDTAEMYpvppspetqGrTEEIIGSWLK------KKGNRDKVVLATKVagpgegitWprggGTRLDRENIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 93 PALRKTLADLQLEYLDLYLMHWPyafERGDNPFPKNADGTICY--DSTHYKETWKALEALVAKGLVQALGLSNFNSRQID 170
Cdd:cd19094 100 EAVEGSLKRLGTDYIDLYQLHWP---DRYTPLFGGGYYTEPSEeeDSVSFEEQLEALGELVKAGKIRHIGLSNETPWGVM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 171 DILSVASV----RPAVLQvecHPY--LAQNELIAH---CQARGLEVTAYSPLGS-------SDRAWRDPD---------- 224
Cdd:cd19094 177 KFLELAEQlglpRIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLAGgvltgkyLDGAARPEGgrlnlfpgym 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320202988 225 ---EPVLLEEPV--VLALAEKYGRSPAQILLRWQVQRKVIC--IpksITPSRILQ---NIKVFDFTFSPEEMKQLNAL 292
Cdd:cd19094 254 aryRSPQALEAVaeYVKLARKHGLSPAQLALAWVRSRPFVTstI---IGATTLEQlkeNIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
17-252 |
6.90e-15 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 73.74 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALkedvgpgkaVPREELFVTSK---LWNTKHHPED 90
Cdd:cd19075 10 FGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELG---------LGERGFKIDTKanpGVGGGLSPEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 91 VEPALRKTLADLQLEYLDLYLMHWPyafergdnpfpknaDgticyDSTHYKETWKALEALVAKGLVQALGLSNFNSRQID 170
Cdd:cd19075 81 VRKQLETSLKRLKVDKVDVFYLHAP--------------D-----RSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 171 DILSVAS----VRPAVLQ---------VEchpylaqNELIAHCQARGLEVTAYSPLG--------------------SSD 217
Cdd:cd19075 142 EIVEICKengwVLPTVYQgmynaitrqVE-------TELFPCLRKLGIRFYAYSPLAggfltgkykysedkagggrfDPN 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 320202988 218 RAWRDP-----DEPVLLEE-PVVLALAEKYGRSPAQILLRW 252
Cdd:cd19075 215 NALGKLyrdryWKPSYFEAlEKVEEAAEKEGISLAEAALRW 255
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
18-289 |
1.07e-14 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 73.24 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 18 GLGTWKSEPGQVkAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKEDvgpgkavPREELFVTSKLWNT---------K 85
Cdd:cd19145 25 DYGAPKPEEEGI-ALIHHAFNSGVTFLDTSDIYGpntNEVLLGKALKDG-------PREKVQLATKFGIHeiggsgvevR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 86 HHPEDVEPALRKTLADLQLEYLDLYLMHwpyafeRGDNPFPknadgticydsthYKETWKALEALVAKGLVQALGLSNFN 165
Cdd:cd19145 97 GDPAYVRAACEASLKRLDVDYIDLYYQH------RIDTTVP-------------IEITMGELKKLVEEGKIKYIGLSEAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 166 SrqiDDILSVASVRP-AVLQVECHPYL--AQNELIAHCQARGLEVTAYSPLG-----SSDRAWRDPDE-------PVLLE 230
Cdd:cd19145 158 A---DTIRRAHAVHPiTAVQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLGrgffaGKAKLEELLENsdvrkshPRFQG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 231 EPV---------VLALAEKYGRSPAQILLRWQVQR--KVICIPKSITPSRILQNIKVFDFTFSPEEMKQL 289
Cdd:cd19145 235 ENLeknkvlyerVEALAKKKGCTPAQLALAWVLHQgeDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-292 |
1.09e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 73.14 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 13 KMPLIGLGTWK----SEPGQV-----------KAAVKYALSVGYRHIDCAAIYG---NEPEIGEALKEdvgpgkaVPREE 74
Cdd:cd19103 3 KLPKIALGTWSwgsgGAGGDQvfgnhldedtlKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR-------YPRED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 75 LFVTSKLWNTKHHPED--VEPALRKTLADLQLEYLDLYLMHWPYAFERgdnpfpknadgticydsthyketW-KALEALV 151
Cdd:cd19103 76 YIISTKFTPQIAGQSAdpVADMLEGSLARLGTDYIDIYWIHNPADVER-----------------------WtPELIPLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 152 AKGLVQALGLSNFNSRQI---DDILSVASVRpaVLQVECHPYL-----AQNELIAHCQARGLEVTAYSPL------GSSD 217
Cdd:cd19103 133 KSGKVKHVGVSNHNLAEIkraNEILAKAGVS--LSAVQNHYSLlyrssEEAGILDYCKENGITFFAYMVLeqgalsGKYD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 218 RAWRDPDE--------PVL--LEE--PVVLALAEKYGRSPAQILLRWqvqrkviCIPKSITP-------SRILQNIKVFD 278
Cdd:cd19103 211 TKHPLPEGsgraetynPLLpqLEEltAVMAEIGAKHGASIAQVAIAW-------AIAKGTTPiigvtkpHHVEDAARAAS 283
|
330
....*....|....
gi 320202988 279 FTFSPEEMKQLNAL 292
Cdd:cd19103 284 ITLTDDEIKELEQL 297
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-251 |
1.88e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 72.68 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLG------TW-KSEPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEDvgpgkavpREELFVTS 79
Cdd:cd19104 8 TGLKVSELTFGgggiggLMgRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL--------PAGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 80 KLWNTKHHPED----VEPALRKTLADLQLEYLDLYLMHWPYAFERgdnpfPKNADGTICYDSTHYK-ETWKALEALVAKG 154
Cdd:cd19104 80 KVRLDPDDLGDiggqIERSVEKSLKRLKRDSVDLLQLHNRIGDER-----DKPVGGTLSTTDVLGLgGVADAFERLRSEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 155 LVQALGLSNF-NSRQIDDILsvASVRPAVLQV----------ECHP--YLAQN--ELIAHCQARGLEVTAYSPLGS---S 216
Cdd:cd19104 155 KIRFIGITGLgNPPAIRELL--DSGKFDAVQVyynllnpsaaEARPrgWSAQDygGIIDAAAEHGVGVMGIRVLAAgalT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 320202988 217 DRAWRDPDEPVLLEEPV---------VLALAEKYGRSPAQILLR 251
Cdd:cd19104 233 TSLDRGREAPPTSDSDVaidfrraaaFRALAREWGETLAQLAHR 276
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-251 |
1.94e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 72.17 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGTW--------KSEPGQVKAA-----VKYALSVGYRHIDCAAIYGN-EPEIGEALKEDvgpgkavprEELFVTSKLW 82
Cdd:cd19097 3 LALGTAqfgldygiANKSGKPSEKeakkiLEYALKAGINTLDTAPAYGDsEKVLGKFLKRL---------DKFKIITKLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 83 NTKHHPEDVEPA----LRKTLADLQLEYLDLYLMHWPYAFERgdnpfpknadgticydstHYKETWKALEALVAKGLVQA 158
Cdd:cd19097 74 PLKEDKKEDEAAieasVEASLKRLKVDSLDGLLLHNPDDLLK------------------HGGKLVEALLELKKEGLIRK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 159 LGLSNFNSRQIDDILSvaSVRPAVLQVechPY------LAQNELIAHCQARGLEVTAYSPL--GssdrawrdpdepVLLE 230
Cdd:cd19097 136 IGVSVYSPEELEKALE--SFKIDIIQL---PFnildqrFLKSGLLAKLKKKGIEIHARSVFlqG------------LLLM 198
|
250 260 270
....*....|....*....|....*....|....*.
gi 320202988 231 EPVVL---------------ALAEKYGRSPAQILLR 251
Cdd:cd19097 199 EPDKLpakfapakpllkklhELAKKLGLSPLELALG 234
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-277 |
3.69e-14 |
|
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: 71.43 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGT--WKSEPGQV-----KAAVKYALSVGYRHIDCAAIYGN-EPEIGEALKEdvgpgkaVPREELFVTSKLWNtkhHP 88
Cdd:cd19090 3 LGLGTagLGGVFGGVdddeaVATIRAALDLGINYIDTAPAYGDsEERLGLALAE-------LPREPLVLSTKVGR---LP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 89 EDVEP----ALRKTLAD----LQLEYLDLYLMHWPYAFERGDNPFPknaDGTIcydsthyketwKALEALVAKGLVQALG 160
Cdd:cd19090 73 EDTADysadRVRRSVEEslerLGRDRIDLLMIHDPERVPWVDILAP---GGAL-----------EALLELKEEGLIKHIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 161 LSnfnSRQIDDILS-VASVRPAVLQVECHPYL----AQNELIAHCQARGLEVTAYSPLGS------------SDRAWRDP 223
Cdd:cd19090 139 LG---GGPPDLLRRaIETGDFDVVLTANRYTLldqsAADELLPAAARHGVGVINASPLGMgllagrppervrYTYRWLSP 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 320202988 224 DEPVLLEEpvVLALAEKYGRSPAQILLRWQVQ----RKVICIPKSitPSRILQNIKVF 277
Cdd:cd19090 216 ELLDRAKR--LYELCDEHGVPLPALALRFLLRdpriSTVLVGASS--PEELEQNVAAA 269
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
37-275 |
2.03e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 66.59 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 37 LSVGYRHIDCAAIYG----------NEPEIGEALKEDvgpGKavpREELFVTSKL---------WNTKHH---PEDVEPA 94
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGRWLKDR---GN---RDDVVIATKVgagprdpdgGPESPEglsAETIEQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 95 LRKTLADLQLEYLDLYLMHwpyaferGDNPfpknadgticydSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILS 174
Cdd:cd19752 101 IDKSLRRLGTDYIDLYYAH-------VDDR------------DTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 175 VASVR----PAVLQVEcHPYL-------------AQNELIAHCQARG-LEVTAYSPL--GSSDRAWR-------DPDEPV 227
Cdd:cd19752 162 IARQQgwaeFSAIQQR-HSYLrprpgadfgvqriVTDELLDYASSRPdLTLLAYSPLlsGAYTRPDRplpeqydGPDSDA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 320202988 228 LLEepVVLALAEKYGRSPAQILLRWQVQRKVICIP--KSITPSRILQNIK 275
Cdd:cd19752 241 RLA--VLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
14-293 |
2.13e-12 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 66.53 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 14 MPLIGLGTW--KSEPGQVKAAVKYALSVGYRHIDCAAIYGnePEIGEAL-KEDVGPGkavpREELFVTSKL--------- 81
Cdd:PRK10376 25 MQLAGPGVFgpPKDRDAAIAVLREAVALGVNHIDTSDFYG--PHVTNQLiREALHPY----PDDLTIVTKVgarrgedgs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 WNTKHHPEDVEPALRKTLADLQLEYLD---LYLMhwpyaferGDNPFPknADGTIcydsthyKETWKALEALVAKGLVQA 158
Cdd:PRK10376 99 WLPAFSPAELRRAVHDNLRNLGLDVLDvvnLRLM--------GDGHGP--AEGSI-------EEPLTVLAELQRQGLVRH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 159 LGLSNFNSRQIDDILSVASvrpaVLQVECHPYLAQ---NELIAHCQARGLEVTAYSPLGSSdrawrDPdepvlLEEPVVL 235
Cdd:PRK10376 162 IGLSNVTPTQVAEARKIAE----IVCVQNHYNLAHradDALIDALARDGIAYVPFFPLGGF-----TP-----LQSSTLS 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 236 ALAEKYGRSPAQILLRWQVQR--KVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN 293
Cdd:PRK10376 228 DVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIA 287
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
44-272 |
2.90e-12 |
|
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: 66.04 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 44 IDCAAIYGN-------EPEIGEALKEDvgpGKavpREELFVTSK--------LWNTKHHPEDVEPALRKTLADLQLEYLD 108
Cdd:cd19082 34 IDTARVYGDwvergasERVIGEWLKSR---GN---RDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGTDYID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 109 LYLMHwpyafeRgDNP-FPknADGTIcydsthyketwKALEALVAKGLVQALGLSN----------------------FN 165
Cdd:cd19082 108 LYFLH------R-DDPsVP--VGEIV-----------DTLNELVRAGKIRAFGASNwsteriaeanayakahglpgfaAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 166 SRQiddiLSVASVRPAVLQVECHPYLAQNELIAHCQaRGLEVTAYSPLGS---SDRAWRDPDEPVLLEEP---------- 232
Cdd:cd19082 168 SPQ----WSLARPNEPPWPGPTLVAMDEEMRAWHEE-NQLPVFAYSSQARgffSKRAAGGAEDDSELRRVyyseenferl 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 320202988 233 -VVLALAEKYGRSPAQILLRWQVQRKVICIPkSITPSRILQ 272
Cdd:cd19082 243 eRAKELAEEKGVSPTQIALAYVLNQPFPTVP-IIGPRTPEQ 282
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
9-301 |
6.97e-12 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 65.26 E-value: 6.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGTW----KSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPE----------IGEALKEDVGpgkavpREE 74
Cdd:PRK10625 8 HSSLEVSTLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPRpetqgltetyIGNWLAKRGS------REK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 75 LFVTSKLWN-TKHHPEDVEP-----------ALRKTLADLQLEYLDLYLMHWPyafERGDNPFpknadGTICYDSTHYK- 141
Cdd:PRK10625 82 LIIASKVSGpSRNNDKGIRPnqaldrknireALHDSLKRLQTDYLDLYQVHWP---QRPTNCF-----GKLGYSWTDSAp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 142 -----ETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVR--PAVLQVEcHPYLAQNE-----LIAHCQARGLEVTA 209
Cdd:PRK10625 154 avsllETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHdlPRIVTIQ-NPYSLLNRsfevgLAEVSQYEGVELLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 210 YSPLGSS--------------------DRAWRDPDEPVLLEEPVVLALAEKYGRSPAQILLRWQVQRKVIC--IPKSITP 267
Cdd:PRK10625 233 YSCLAFGtltgkylngakpagarntlfSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVAstLLGATTM 312
|
330 340 350
....*....|....*....|....*....|....
gi 320202988 268 SRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVP 301
Cdd:PRK10625 313 EQLKTNIESLHLTLSEEVLAEIEAVHQVYTYPAP 346
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
31-224 |
6.21e-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: 59.29 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 31 AAVKYALSVGYRHIDCAAIYG---NEPEIGEALKedvgpgkAVPREELFVTSKLWNTKHHPEDVEPA------------- 94
Cdd:cd19162 23 ATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA-------RHPRAEYVVSTKVGRLLEPGAAGRPAgadrrfdfsadgi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 95 ---LRKTLADLQLEYLDLYLMHWPyafERgdnpfpknadgticYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDD 171
Cdd:cd19162 96 rrsIEASLERLGLDRLDLVFLHDP---DR--------------HLLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 320202988 172 ILSVASVRpAVLQVECHPYL---AQNELIAHCQARGLEVTAYSPLGSSDRAWRDPD 224
Cdd:cd19162 159 AARRADVD-VVMVAGRYTLLdrrAATELLPLCAAKGVAVVAAGVFNSGILATDDPA 213
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
17-214 |
1.13e-09 |
|
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: 58.32 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 17 IGLGT------WKSEPGQVKA--AVKYALSVGYRHIDCAAIYGNEPE---IGEALKedvgpGKAVPREELFVTSKLWNTK 85
Cdd:cd19153 15 VGLGTaalggvYGDGLEQDEAvaIVAEAFAAGINHFDTSPYYGAESSeavLGKALA-----ALQVPRSSYTVATKVGRYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 86 -----HHPEDVEPALRKTLADLQLEYLDLYLMHwpyafergDNPFPKNAdgticydsTHYKETWKALEALVAKGLVQALG 160
Cdd:cd19153 90 dsefdYSAERVRASVATSLERLHTTYLDVVYLH--------DIEFVDYD--------TLVDEALPALRTLKDEGVIKRIG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 320202988 161 LSNFNSRQIDDILSVASVRPA-VLQVECHPYLAQNELIA----HCQARGLEVTAYSPLG 214
Cdd:cd19153 154 IAGYPLDTLTRATRRCSPGSLdAVLSYCHLTLQDARLESdapgLVRGAGPHVINASPLS 212
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-287 |
3.27e-09 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 56.79 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGT--WKSEPGQVK-----AAVKYALSVGYRHIDCAAIYGN---EPEIGEALKedvgpgkAVPREELFVT 78
Cdd:cd19163 8 KTGLKVSKLGFGAspLGGVFGPVDeeeaiRTVHEALDSGINYIDTAPWYGQgrsETVLGKALK-------GIPRDSYYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 79 SKLWNTKHHPED--------VEPALRKTLADLQLEYLDLYLMHwpyafergDNPFPKNADGTIcydsthyKETWKALEAL 150
Cdd:cd19163 81 TKVGRYGLDPDKmfdfsaerITKSVEESLKRLGLDYIDIIQVH--------DIEFAPSLDQIL-------NETLPALQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 151 VAKGLVQALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQN---ELIAHCQARGLEVTAYSPLGS---SDR---AWR 221
Cdd:cd19163 146 KEEGKVRFIGITGYPLDVLKEVLERSPVKIDTVLSYCHYTLNDTsllELLPFFKEKGVGVINASPLSMgllTERgppDWH 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320202988 222 DPDEPVLLEEPVVLALAEKYGRSPAQILLRWQVQRKVI--CIPKSITPSRILQNIKVFDFTFSPEEMK 287
Cdd:cd19163 226 PASPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIatTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
9-287 |
7.87e-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: 55.87 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGTWKSEPG-----QVKAAVKYALSVGYRHIDCAAIYGNEP-----EIGEALKEDVGPGkavpREELFVT 78
Cdd:cd19151 7 RSGLKLPAISLGLWHNFGDvdryeNSRAMLRRAFDLGITHFDLANNYGPPPgsaeeNFGRILKEDLKPY----RDELIIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 79 SKL-----------WNTKHHpedVEPALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgticydSTHYKETWKAL 147
Cdd:cd19151 83 TKAgytmwpgpygdWGSKKY---LIASLDQSLKRMGLDYVDIFYHHRP-------DP------------ETPLEETMGAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 148 EALVAKGLVQALGLSNFNS---RQIDDILSVASVRPAVLQVECHPYLAQNE--LIAHCQARGLEVTAYSPLG-------- 214
Cdd:cd19151 141 DQIVRQGKALYVGISNYPPeeaREAAAILKDLGTPCLIHQPKYSMFNRWVEegLLDVLEEEGIGCIAFSPLAqglltdry 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 215 ----------SSDRAWRDPDE--PVLLEEPVVL-ALAEKYGRSPAQILLRWQVQRKVIC---IPKSiTPSRILQNIKVFD 278
Cdd:cd19151 221 lngipedsraAKGSSFLKPEQitEEKLAKVRRLnEIAQARGQKLAQMALAWVLRNKRVTsvlIGAS-KPSQIEDAVGALD 299
|
330
....*....|
gi 320202988 279 FT-FSPEEMK 287
Cdd:cd19151 300 NReFSEEELA 309
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
9-252 |
1.25e-08 |
|
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: 55.29 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGTWKSEPGQV-----KAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEDVgpgkaVPREELFVTSK 80
Cdd:cd19143 8 RSGLKVSALSFGSWVTFGNQVdvdeaKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELG-----WPRSDYVVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 81 L-W------------NTKHHPEdvepALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgticydSTHYKETWKAL 147
Cdd:cd19143 83 IfWggggpppndrglSRKHIVE----GTKASLKRLQLDYVDLVFCHRP-------DP------------ATPIEETVRAM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 148 EALVAKGLVQALGLSNFNSRQIDDILSVAS----VRPAVLQVE---CHPYLAQNELIAHCQARGLEVTAYSPLGS----- 215
Cdd:cd19143 140 NDLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQynlFHRERVEVEYAPLYEKYGLGTTTWSPLASglltg 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 320202988 216 -------SDRAWRDPDEPVLLEEPVVL------------ALAEKYGRSPAQILLRW 252
Cdd:cd19143 220 kynngipEGSRLALPGYEWLKDRKEELgqekiekvrklkPIAEELGCSLAQLAIAW 275
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
10-290 |
2.31e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 54.61 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTWKSEpGQV------KAAVKYALSVGYRHIDCAAIYGNEP-----EIGEALKEDVGPgkavPREELFVT 78
Cdd:PRK09912 21 SGLRLPALSLGLWHNF-GHVnalesqRAILRKAFDLGITHFDLANNYGPPPgsaeeNFGRLLREDFAA----YRDELIIS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 79 SK----LW----NTKHHPEDVEPALRKTLADLQLEYLDLYLMHwpyafeRGDnpfpknadgticyDSTHYKETWKALEAL 150
Cdd:PRK09912 96 TKagydMWpgpyGSGGSRKYLLASLDQSLKRMGLEYVDIFYSH------RVD-------------ENTPMEETASALAHA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 151 VAKGLVQALGLSNFNSRQIDDILSVASVRPAVLQVECHPY------LAQNELIAHCQARGLEVTAYSPLGS--------- 215
Cdd:PRK09912 157 VQSGKALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYnllnrwVDKSGLLDTLQNNGVGCIAFTPLAQglltgkyln 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 216 ----SDRAWRDPDEPVLLEEPVVLA-----------LAEKYGRSPAQILLRWQV--QRKVICIPKSITPSRILQNIKVF- 277
Cdd:PRK09912 237 gipqDSRMHREGNKVRGLTPKMLTEanlnslrllneMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALn 316
|
330
....*....|...
gi 320202988 278 DFTFSPEEMKQLN 290
Cdd:PRK09912 317 NLTFSTEELAQID 329
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
9-287 |
7.06e-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: 53.23 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 9 HTGQKMPLIGLGTWKS----EPGQVKAAV-KYALSVGYRHIDCAAIYGNEP-----EIGEALKEDVGPgkavPREELFVT 78
Cdd:cd19150 7 KSGLKLPALSLGLWHNfgddTPLETQRAIlRTAFDLGITHFDLANNYGPPPgsaeeNFGRILREDFAG----YRDELIIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 79 SKL-----------WNTKHHpedVEPALRKTLADLQLEYLDLYLMHwpyafeRGDnpfpknadgticyDSTHYKETWKAL 147
Cdd:cd19150 83 TKAgydmwpgpygeWGSRKY---LLASLDQSLKRMGLDYVDIFYSH------RFD-------------PDTPLEETMGAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 148 EALVAKGLVQALGLSNFNS---RQIDDILSVASVrPAVLQVECHPYL----AQNELIAHCQARGLEVTAYSPLG------ 214
Cdd:cd19150 141 DHAVRSGKALYVGISSYSPertREAAAILRELGT-PLLIHQPSYNMLnrwvEESGLLDTLQELGVGCIAFTPLAqglltd 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 215 -------SSDRAWRDPD-EPVLLEEPVVL------ALAEKYGRSPAQILLRWQVQRKVIC---IPKSiTPSRILQNIKVF 277
Cdd:cd19150 220 kylngipEGSRASKERSlSPKMLTEANLNsiralnEIAQKRGQSLAQMALAWVLRDGRVTsalIGAS-RPEQLEENVGAL 298
|
330
....*....|.
gi 320202988 278 D-FTFSPEEMK 287
Cdd:cd19150 299 DnLTFSADELA 309
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
10-190 |
2.84e-06 |
|
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: 48.23 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTWKS-----EPGQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdvgpgKAVPREELFVTSKL 81
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaiSEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKK-----KGWKRSSYIVSTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 -WNT---------KHHPEDVEPALRKtladLQLEYLDLYLMHwpyafeRGDNPFPknadgticydsthYKETWKALEALV 151
Cdd:cd19142 84 yWSYgseerglsrKHIIESVRASLRR----LQLDYIDIVIIH------KADPMCP-------------MEEVVRAMSYLI 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 320202988 152 AKGLVQALGLSNFNSRQIDDILSVAS----VRPAVLQVECHPY 190
Cdd:cd19142 141 DNGLIMYWGTSRWSPVEIMEAFSIARqfncPTPICEQSEYHMF 183
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
10-197 |
4.81e-06 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 47.73 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTWKSEPGQVKAAVKYAL-SVGYRH----IDCAAIYG---NEPEIGEALKEdvgpgKAVPREELFVTSKL 81
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGQISDEVAERLmTIAYESgvnlFDTAEVYAagkAEVILGSIIKK-----KGWRRSSLVITTKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 -WNTKHHPE------DVEPALRKTLADLQLEYLDLYLMHWPyafergDNPFPknadgticydsthYKETWKALEALVAKG 154
Cdd:cd19159 84 yWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDVVFANRP------DSNTP-------------MEEIVRAMTHVINQG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 320202988 155 LVQALGLSNFNSRQIDDILSVAS----VRPAVLQVECHpyLAQNELI 197
Cdd:cd19159 145 MAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKV 189
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
32-113 |
5.80e-06 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 47.27 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 32 AVKYALSVGYRHIDCAAIYGNEPEI-GEALKEDVGPgkaVPREELFVTSK-----LWNTKHHPEDVEPALRKTLADLQLE 105
Cdd:cd19164 39 IVRRALELGIRAFDTSPYYGPSEIIlGRALKALRDE---FPRDTYFIITKvgrygPDDFDYSPEWIRASVERSLRRLHTD 115
|
....*...
gi 320202988 106 YLDLYLMH 113
Cdd:cd19164 116 YLDLVYLH 123
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
10-188 |
4.12e-05 |
|
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: 44.75 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTWKSEPGQVKAAV-KYALSVGYRH----IDCAAIY-GNEPEI--GEALKEdvgpgKAVPREELFVTSKL 81
Cdd:cd19141 8 SGLRVSCLGLGTWVTFGSQISDEVaEELVTLAYENginlFDTAEVYaAGKAEIvlGKILKK-----KGWRRSSYVITTKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 -WNTKHHPE------DVEPALRKTLADLQLEYLDLYlmhwpyafergdnpFPKNADGTicydsTHYKETWKALEALVAKG 154
Cdd:cd19141 83 fWGGKAETErglsrkHIIEGLKASLERLQLEYVDIV--------------FANRPDPN-----TPMEEIVRAFTHVINQG 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 320202988 155 LVQALGLSNFNSRQIDDILSVAS----VRPAVLQVECH 188
Cdd:cd19141 144 MAMYWGTSRWSAMEIMEAYSVARqfnlIPPIVEQAEYH 181
|
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| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
10-190 |
4.97e-05 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 44.31 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTWKSEPGQV-----KAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdvgpgKAVPREELFVTSKL 81
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGQItdemaEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKK-----KGWRRSSLVITTKI 83
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 -WNTKHHPE------DVEPALRKTLADLQLEYLDLYLMHWPyafergdNPfpknadgticydSTHYKETWKALEALVAKG 154
Cdd:cd19158 84 fWGGKAETErglsrkHIIEGLKASLERLQLEYVDVVFANRP-------DP------------NTPMEETVRAMTHVINQG 144
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170 180 190 200
....*....|....*....|....*....|....*....|
gi 320202988 155 LVQALGLSNFNSRQIDDILSVAS----VRPAVLQVECHPY 190
Cdd:cd19158 145 MAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMF 184
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| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
15-284 |
9.22e-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: 43.37 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 15 PLIGLGT------WKSEP-GQVKAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKEdVGPGKAV-------------P 71
Cdd:cd19152 1 PKLGFGTaplgnlYEAVSdEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE-LGREDYVistkvgrllvplqE 79
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 72 REELFVTSKLWNTKHHP------EDVEPALRKTLADLQLEYLDLYLMHWPyafergDNPFPKNADGTICYDSThyKETWK 145
Cdd:cd19152 80 VEPTFEPGFWNPLPFDAvfdysyDGILRSIEDSLQRLGLSRIDLLSIHDP------DEDLAGAESDEHFAQAI--KGAFR 151
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 146 ALEALVAKGLVQALGL-SNFnSRQIDDILSVAsvRPAVLQVEC------HPylAQNELIAHCQARGLEVTAYSPL----- 213
Cdd:cd19152 152 ALEELREEGVIKAIGLgVND-WEVILRILEEA--DLDWVMLAGrytlldHS--AARELLPECEKRGVKVVNAGPFnsgfl 226
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250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320202988 214 --GSSDRAWRDPDEPVLLEEPV--VLALAEKYGRSPA----QILLRWQVQRKVicIPKSITPSRILQNIKVFDFTFSPE 284
Cdd:cd19152 227 agGDNFDYYEYGPAPPELIARRdrIEALCEQHGVSLAaaalQFALAPPAVASV--APGASSPERVEENVALLATEIPAA 303
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| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
10-188 |
1.59e-04 |
|
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: 43.05 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTWKSEPGQVKAAV-KYALSVGYRH----IDCAAIYGN---EPEIGEALKEdvgpgKAVPREELFVTSKL 81
Cdd:cd19160 11 SGLRVSCLGLGTWVTFGSQISDETaEDLLTVAYEHgvnlFDTAEVYAAgkaERTLGNILKS-----KGWRRSSYVVTTKI 85
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 82 -WNTKHHPE------DVEPALRKTLADLQLEYLDLYLMHwpyafeRGDNPFPknadgticydsthYKETWKALEALVAKG 154
Cdd:cd19160 86 yWGGQAETErglsrkHIIEGLRGSLDRLQLEYVDIVFAN------RSDPNSP-------------MEEIVRAMTYVINQG 146
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170 180 190
....*....|....*....|....*....|....*...
gi 320202988 155 LVQALGLSNFNSRQIDDILSVAS----VRPAVLQVECH 188
Cdd:cd19160 147 MAMYWGTSRWSAMEIMEAYSVARqfnlIPPVCEQAEYH 184
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| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
10-113 |
1.93e-03 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 39.38 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 10 TGQKMPLIGLGTwkSEPGQV---------KAAVKYALSVGYRHIDCAAIYGN---EPEIGEALKedvgpGKAVPREELFV 77
Cdd:PLN02587 7 TGLKVSSVGFGA--SPLGSVfgpvseedaIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALK-----ALGIPREKYVV 79
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90 100 110 120
....*....|....*....|....*....|....*....|
gi 320202988 78 TSKLWNTKH----HPEDVEPALRKTLADLQLEYLDLYLMH 113
Cdd:PLN02587 80 STKCGRYGEgfdfSAERVTKSVDESLARLQLDYVDILHCH 119
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|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-292 |
7.75e-03 |
|
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: 381324 [Multi-domain] Cd Length: 318 Bit Score: 37.71 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 36 ALSVGYRHIDCAAIYGNEPE-IGEALKedvgpGKAVPREELFVTSKL-------WNTKHHPEDVE----PALRKTL---A 100
Cdd:cd19098 44 AWAAGVRYFDAARSYGRAEEfLGSWLR-----SRNIAPDAVFVGSKWgytytadWQVDAAVHEVKdhslARLLKQWeetR 118
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 101 DLQLEYLDLYLMHwPYAFERG--DNpfpknadgticydsthyKETWKALEALVAKGLvqALGLSNFNSRQIDDILSVASV 178
Cdd:cd19098 119 SLLGKHLDLYQIH-SATLESGvlED-----------------ADVLAALAELKAEGV--KIGLSLSGPQQAETLRRALEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320202988 179 RPA-------------VLQVECHPYLAQneliAHcqARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEKYGRSP 245
Cdd:cd19098 179 EIDgarlfdsvqatwnLLEQSAGEALEE----AH--EAGMGVIVKEALANGRLTDRNPSPELAPLMAVLKAVADRLGVTP 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 320202988 246 AQILLRWQVQRKVICIPKS--ITPSRILQNIKVFDFTFSPEEMKQLNAL 292
Cdd:cd19098 253 DALALAAVLAQPFVDVVLSgaATPEQLRSNLRALDVSLDLELLAALADL 301
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