|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
10-316 |
0e+00 |
|
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: 620.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSLV 89
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 90 KKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIER 169
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 170 LLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPEDPLLLEIPKIKEIAAKHKRTAAQVL 249
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71067102 250 IRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRACGLFAASHNEDFPFHAEY 316
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
7-299 |
5.19e-153 |
|
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: 430.65 E-value: 5.19e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 7 LLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQE-KAVKREDLFIVSKLWSTFFE 85
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPgKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 86 KSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHF 165
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 166 QIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPEDPLLLEIPKIKEIAAKHKRTA 245
Cdd:cd19106 161 QIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 71067102 246 AQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRAC 299
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-316 |
2.78e-150 |
|
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: 423.60 E-value: 2.78e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 12 KMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSLVKK 91
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 92 AFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIERLL 171
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 172 NKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGspdrpsAKPEDPLLLEIPKIKEIAAKHKRTAAQVLIR 251
Cdd:cd19110 163 NKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG------GSCEGVDLIDDPVIQRIAKKHGKSPAQILIR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71067102 252 FHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRACGLFAASHNEDFPFHAEY 316
Cdd:cd19110 237 FQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
4-297 |
6.60e-133 |
|
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: 379.65 E-value: 6.60e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 4 FVTLLTGAKMPIVGLGTWKS---PPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLW 80
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPeevPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 81 STFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVS 160
Cdd:cd19108 82 CTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 161 NFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSpDRPSA--KPEDPLLLEIPKIKEIA 238
Cdd:cd19108 162 NFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGS-QRDKEwvDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 71067102 239 AKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-289 |
5.28e-123 |
|
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: 352.55 E-value: 5.28e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 13 MPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIqekaVKREDLFIVSKLWSTFFEKSLVKKA 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 93 FQNTLSDLKLDYLDLYLIHWPQGFQSGnvflptddkgsilSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEG-------------GSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 173 KPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPsakpedplLLEIPKIKEIAAKHKRTAAQVLIRF 252
Cdd:cd19071 144 AA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP--------LLDDPVLKEIAKKYGKTPAQVLLRW 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 71067102 253 HIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19071 214 ALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
10-312 |
5.57e-122 |
|
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: 352.18 E-value: 5.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTW----KSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFE 85
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 86 KSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHF 165
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 166 QIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPS-AKPEDPLLLEIPKIKEIAAKHKRT 244
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIwVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71067102 245 AAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRACGLFAASHNEDFPF 312
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
10-299 |
7.98e-122 |
|
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: 351.20 E-value: 7.98e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWKS-PPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSL 88
Cdd:cd19116 8 GNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 89 VKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNvflPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIE 168
Cdd:cd19116 88 VEPALRESLKRLGLDYVDLYLIHWPVAFKENN---DSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 169 RLLNkpGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrPSAKPEDPLLLEIPKIKEIAAKHKRTAAQV 248
Cdd:cd19116 165 RLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLV-PRGQTNPPPRLDDPTLVAIAKKYGKTTAQI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 71067102 249 LIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRAC 299
Cdd:cd19116 242 VLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-297 |
2.73e-116 |
|
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: 337.46 E-value: 2.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 1 MAAFvTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLW 80
Cdd:cd19123 1 MKTL-PLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 81 STFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGnVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVS 160
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 161 NFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSA-KPED-PLLLEIPKIKEIA 238
Cdd:cd19123 159 NFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAmKAEGePVLLEDPVINKIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 71067102 239 AKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19123 237 EKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
10-297 |
1.24e-115 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 333.95 E-value: 1.24e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTFFEKSLV 89
Cdd:COG0656 2 GVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS----GVPREELFVTTKVWNDNHGYDDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 90 KKAFQNTlsdlkldyldlylIHWPqgfqsgnvflptddkgsilsSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIER 169
Cdd:COG0656 78 LAAFEESlerlgldyldlylIHWP--------------------GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 170 LLNKPGlkHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAKHKRTAAQVL 249
Cdd:COG0656 138 LLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQVV 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 71067102 250 IRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:COG0656 206 LRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGER 253
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
5-299 |
6.10e-112 |
|
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: 326.68 E-value: 6.10e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFF 84
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 85 EKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNH 164
Cdd:cd19154 84 APEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 165 FQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPED-----PLLLEIPKIKEIAA 239
Cdd:cd19154 164 DQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspaPNLLQDPIVKAIAE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 240 KHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRAC 299
Cdd:cd19154 242 KHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
4-289 |
8.69e-105 |
|
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: 307.74 E-value: 8.69e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 4 FVTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTF 83
Cdd:cd19125 2 FFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 84 FEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNV------FLPTDDKGSilsskytfldaWEAMEELVDQGLVKAL 157
Cdd:cd19125 82 HAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHmpepeeVLPPDIPST-----------WKAMEKLVDSGKVRAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 158 GVSNFNHFQIERLLNKPGLkhKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPEdplLLEIPKIKEI 237
Cdd:cd19125 151 GVSNFSVKKLEDLLAVARV--PPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKV 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 71067102 238 AAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19125 226 AEKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKF 277
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-299 |
1.84e-98 |
|
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: 292.51 E-value: 1.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 4 FVTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTF 83
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 84 FEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQS---GNVFLptDDKGSILSSKYT-FLDAWEAMEELVDQGLVKALGV 159
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSkedDSGKL--DPTGEHKQDYTTdLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 160 SNFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKP-------EDPLLLEIP 232
Cdd:cd19155 161 SNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71067102 233 KIKEIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRAC 299
Cdd:cd19155 239 VVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-297 |
6.44e-97 |
|
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: 287.86 E-value: 6.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSLV 89
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 90 KKAFQNTLSDLKLDYLDLYLIHWPQGFQSgnvflpTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIER 169
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVN------KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 170 LLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRP--SAKPEDPLLLEIPKIKEIAAKHKRTAAQ 247
Cdd:cd19111 155 ILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPAQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 71067102 248 VLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19111 233 VLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-289 |
1.49e-93 |
|
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: 278.91 E-value: 1.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 7 LLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEK-AVKREDLFIVSKLWSTFFE 85
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEpGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 86 KSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGN-----VFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGdlnplTAVPTNGGEVDLDLSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 161 NFNHFQIERLLNKPGLkhKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSpdrpSAKPEdPLLLEIPKIKEIAAK 240
Cdd:cd19118 161 NFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN----NLAGL-PLLVQHPEVKAIAAK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71067102 241 HKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDfqLSEEDMAAI 289
Cdd:cd19118 234 LGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAV 280
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-289 |
3.48e-89 |
|
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: 267.85 E-value: 3.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 14 PIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSLVKKAF 93
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 94 QNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIERLLNK 173
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 174 pgLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKpedpLLLEIPKIKEIAAKHKRTAAQVLIRFH 253
Cdd:cd19128 162 --CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNL----TFLNDSELKALATKYNTTPPQVIIAWH 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 71067102 254 IER---NVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19128 236 LQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-289 |
7.09e-89 |
|
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: 266.16 E-value: 7.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTFF 84
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRAS----GVPREELFITTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 85 EKSLVKKAFQNTLSDLKLDYLDLYLIHWPQgfqsgnvflPTDDKgsilsskytFLDAWEAMEELVDQGLVKALGVSNFNH 164
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWPV---------PAQDK---------YVETWKALIELKKEGRVKSIGVSNFTI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 165 FQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAKHKRT 244
Cdd:cd19131 140 EHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG----------LLSDPVIGEIAEKHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 71067102 245 AAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19131 208 PAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAI 252
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
6-289 |
9.33e-89 |
|
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: 267.06 E-value: 9.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 6 TLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTFFE 85
Cdd:cd19117 7 KLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDS----GVPREEIFITTKLWCTWHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 86 KslVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNV-FLPTDDKGS-ILSSKYTFLDAWEAMEELVDQGLVKALGVSNFN 163
Cdd:cd19117 83 R--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNdFLFKKDDGTkDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 164 HFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPsakpedplLLEIPKIKEIAAKHKR 243
Cdd:cd19117 161 IKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGK 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 71067102 244 TAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVfdFQLSEEDMAAI 289
Cdd:cd19117 233 TPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEI 276
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
5-297 |
2.83e-85 |
|
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: 258.95 E-value: 2.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTff 84
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 85 EKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPT----DDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVS 160
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGVGTTGsalgEDGVLDIDVTISLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 161 NFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPEDPLLLEIPKIKEIAAK 240
Cdd:cd19112 161 NYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEWFGSVSPLDDPVLKDLAKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 71067102 241 HKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-297 |
3.26e-85 |
|
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: 257.32 E-value: 3.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 4 FVTLLTGAKMPIVGLGTWKSPPAK-VREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIqekaVKREDLFIVSKLWST 82
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESG----IPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 83 --FFEKSLvkKAFQNTLSDLKLDYLDLYLIHWPQGfqsgnvflptddkgsilsSKYTflDAWEAMEELVDQGLVKALGVS 160
Cdd:cd19157 77 dqGYDSTL--KAFEASLERLGLDYLDLYLIHWPVK------------------GKYK--ETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 161 NFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAK 240
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEK 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 71067102 241 HKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19157 203 YNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLR 259
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-291 |
7.39e-85 |
|
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: 256.02 E-value: 7.39e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 13 MPIVGLGTWK-SPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSLVKK 91
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 92 AFQNTLSDLKLDYLDLYLIHWP--QGFQsgnvflPTDDKGSILSSkytflDAWEAMEELVDQGLVKALGVSNFNHFQIER 169
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgvQGLK------PSDPRNAELRR-----ESWRALEDLYKEGKLRAIGVSNYTVRHLEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 170 LLNKPGLkhKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPdrpsakpeDPLLLEIPKIKEIAAKHKRTAAQVL 249
Cdd:cd19136 150 LLKYCEV--PPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG--------DLRLLEDPTVLAIAKKYGRTPAQVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 71067102 250 IRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILS 291
Cdd:cd19136 220 LRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
6-292 |
2.99e-84 |
|
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: 255.15 E-value: 2.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 6 TLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIqEKAVKREDLFIVSKLWSTFFE 85
Cdd:cd19121 5 KLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTYHR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 86 KslVKKAFQNTLSDLKLDYLDLYLIHWPQGFQ-SGN-VFLPTDDKGS-ILSSKYTFLDAWEAMEELVDQGLVKALGVSNF 162
Cdd:cd19121 84 R--VELCLDRSLKSLGLDYVDLYLVHWPVLLNpNGNhDLFPTLPDGSrDLDWDWNHVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 163 NHFQIERLLnkPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPsakpedplLLEIPKIKEIAAKHK 242
Cdd:cd19121 162 SIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEIAKKHN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 71067102 243 RTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFqlSEEDMAAILSF 292
Cdd:cd19121 232 VGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-297 |
3.83e-84 |
|
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: 256.19 E-value: 3.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 1 MAAFVTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLW 80
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 81 STFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQ--SGNVFLP---TDDKGSILSSKYTFLDAWEAMEELVDQGLVK 155
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvDPAVRYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 156 ALGVSNFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGsP------DRPSAKpEDPLLL 229
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PqsflelDLPGAK-DTPPLF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71067102 230 EIPKIKEIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-289 |
5.46e-83 |
|
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: 250.65 E-value: 5.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 13 MPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTFFEKSLVKKA 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 93 FQNTLSDLKLDYLDLYLIHWPqgfqsgnvflptddkgsilSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWP-------------------NPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 173 KPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLgspdrpsAKPEdplLLEIPKIKEIAAKHKRTAAQVLIRF 252
Cdd:cd19073 138 ISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-------ARGE---VLRDPVIQEIAEKYDKTPAQVALRW 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 71067102 253 HIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19073 206 LVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-293 |
7.68e-83 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 250.82 E-value: 7.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWKSPPA-KVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTF 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRES----GVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 84 FEKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflpTDDKgsilsskytFLDAWEAMEELVDQGLVKALGVSNFN 163
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWP-----------GKDK---------FIDTWKALEKLYASGKVKAIGVSNFQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 164 HFQIERLLnkpglKH---KPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAK 240
Cdd:cd19126 137 EHHLEELL-----AHadvVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG----------LLSNPVLAAIGEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 71067102 241 HKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFN 293
Cdd:cd19126 202 YGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-297 |
7.79e-83 |
|
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: 252.75 E-value: 7.79e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFF 84
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 85 EKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQsgnvFLPTDDK----------GSILSSKYTFLDAWEAMEELVDQGLV 154
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFK----FVPIEEKyppgfycgdgDNFVYEDVPILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 155 KALGVSNFNHFQIERLLNkpGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSP-----DRPSAKpEDPLLL 229
Cdd:cd19113 159 KSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL-NTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71067102 230 EIPKIKEIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-293 |
1.58e-81 |
|
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: 247.49 E-value: 1.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWK-SPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIqekaVKREDLFIVSKLWSTF 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSG----IPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 84 FEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGfqsgnvflptDDKGsilsskytfldAWEAMEELVDQGLVKALGVSNFN 163
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG----------DVYG-----------AWRAMEELYKEGKIRAIGVSNFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 164 HFQIERLLnkPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedPLLLEIPKIKEIAAKHKR 243
Cdd:cd19133 136 PDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGR--------NNLFENPVLTEIAEKYGK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 71067102 244 TAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFN 293
Cdd:cd19133 206 SVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
1-292 |
3.86e-80 |
|
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: 244.16 E-value: 3.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 1 MAAFVTLLTGAKMPIVGLGTWKSPpAKVREAVKVAI-DAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKL 79
Cdd:cd19135 1 GTPTVRLSNGVEMPILGLGTSHSG-GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKES----GVPREDLFLTTKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 80 WSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNvflptddkgsilSSKYTFLDAWEAMEELVDQGLVKALGV 159
Cdd:cd19135 76 WPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGK------------NVKETRAETWRALEELYDEGLCRAIGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 160 SNFNHFQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLgspdrpsAKPEdplLLEIPKIKEIAA 239
Cdd:cd19135 144 SNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-------AKGK---ALEEPTVTELAK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 71067102 240 KHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSF 292
Cdd:cd19135 212 KYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
5-297 |
1.59e-78 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 240.11 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWKSPPAKVRE-AVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWST- 82
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWNSd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 83 -FFEKSLvkKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflptddkgsilsSKYTFLDAWEAMEELVDQGLVKALGVSN 161
Cdd:cd19156 77 qGYESTL--AAFEESLEKLGLDYVDLYLIHWP--------------------VKGKFKDTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 162 FNHFQIERLLNKpgLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAKH 241
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 71067102 242 KRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19156 203 GKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-289 |
7.60e-77 |
|
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: 235.76 E-value: 7.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTFF 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 85 EKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvfLPTDDKGSIlsskytflDAWEAMEELVDQGLVKALGVSNFNH 164
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWP---------VPNDFDRTI--------QAYKALEKLLAEGRVRAIGVSNFTP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 165 FQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSP--DRPSAKPEDPLLLEIPKIKEIAAKHK 242
Cdd:cd19127 140 EHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVmrYGASGPTGPGDVLQDPTITGLAEKYG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 71067102 243 RTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19127 218 KTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
7-289 |
1.53e-76 |
|
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: 234.47 E-value: 1.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 7 LLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTFFEK 86
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRS----GVPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 87 SLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvfLPTDDKgsilsskytFLDAWEAMEELVDQGLVKALGVSNFNHFQ 166
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWP---------NPSRDL---------YVEAWQALIEAREEGLVRSIGVSNFLPEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 167 IERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGspdRPSAkpedplLLEIPKIKEIAAKHKRTAA 246
Cdd:cd19132 139 LDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG---RGSG------LLDEPVIKAIAEKHGKTPA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 71067102 247 QVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19132 208 QVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAI 250
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-297 |
1.94e-76 |
|
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: 235.91 E-value: 1.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSLV 89
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 90 KKAFQNTLSDLKLDYLDLYLIHWP--QGFQSGNVFLPTDDKGSILSS----KYTFLDAWEAMEELVDQGLVKALGVSNFN 163
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPipAAYVDPAENYPFLWKDKELKKfpleQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 164 HFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSP---DRPSAKPEDPLLLEIPKIKEIAAK 240
Cdd:cd19114 161 VQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTNLLEHPVVKKLADK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 71067102 241 HKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19114 239 HKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-294 |
3.15e-75 |
|
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: 232.77 E-value: 3.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWkSPPAK---VREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWS 81
Cdd:cd19119 4 FKLNTGASIPALGLGTA-SPHEDraeVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 82 TFFEKslVKKAFQNTLSDLKLDYLDLYLIHWPQGFQ-----SGNVFLPTDDKGSILSSK-YTFLDAWEAMEELVDQGLVK 155
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAAsGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 156 ALGVSNFNHFQIERLLNKpgLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPsakpedplLLEIPKIK 235
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLVK 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 71067102 236 EIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVfdFQLSEEDMAAILSFNR 294
Cdd:cd19119 231 KIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-289 |
5.39e-75 |
|
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: 230.61 E-value: 5.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAiqekIQEKAVKREDLFIVSKLWSTFFEKSLV 89
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEA----IAASGVPRDELFLTTKVWPDNYSPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 90 KKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflptddkgsilSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIER 169
Cdd:cd19140 81 LASVEESLRKLRTDYVDLLLLHWP-------------------NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 170 LLNKPGLkhKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAKHKRTAAQVL 249
Cdd:cd19140 142 AVELSEA--PLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE----------VLKDPVLQEIGRKHGKTPAQVA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 71067102 250 IRFHIER-NVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19140 210 LRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-289 |
2.68e-74 |
|
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: 229.85 E-value: 2.68e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGTWKSP--PAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVK-REDLFIVSKLWSTFFE 85
Cdd:cd19124 1 SGQTMPVIGMGTASDPpsPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 86 KSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNV--------FLPTDDKGsilsskytfldAWEAMEELVDQGLVKAL 157
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFsfpieeedFLPFDIKG-----------VWEAMEECQRLGLTKAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 158 GVSNFNHFQIERLL---NKPglkhkPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPEdplLLEIPKI 234
Cdd:cd19124 150 GVSNFSCKKLQELLsfaTIP-----PAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGSNA---VMESDVL 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 71067102 235 KEIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19124 222 KEIAAAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKI 276
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-289 |
3.65e-71 |
|
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: 221.34 E-value: 3.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGT----WKSPPA----KVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWS 81
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDdiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 82 TffeKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflPTDDKGsilssKYTFLDAWEAMEELVDQGLVKALGVSN 161
Cdd:cd19120 77 G---IKDPREALRKSLAKLGVDYVDLYLIHSP----------FFAKEG-----GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 162 FNHFQIERLLNKPglKHKPVTNQVECHPYLT--QEKLIQYCHSKGITITAYSPLGSPDRPSAKPEDPLLleipkiKEIAA 239
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPLTRDAGGPLDPVL------EKIAE 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 71067102 240 KHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19120 211 KYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEI 260
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
10-289 |
8.72e-70 |
|
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: 218.87 E-value: 8.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSLV 89
Cdd:cd19129 3 SGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 90 KKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGS-ILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIE 168
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNvIYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 169 RLLNKPGLkhKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSakpedplLLEIPKIKEIAAKHKRTAAQV 248
Cdd:cd19129 163 EIFEAARI--KPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPK-------LLEDPVITAIARRVNKTPAQV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 71067102 249 LIRFHIERNVVVIPKSVTPSRIQENiqvFDFQ-LSEEDMAAI 289
Cdd:cd19129 234 LLAWAIQRGTALLTTSKTPSRIREN---FDIStLPEDAMREI 272
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
4-289 |
2.65e-69 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 216.86 E-value: 2.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 4 FVTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTf 83
Cdd:PRK11565 6 VIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA----SVAREELFITTKLWND- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 84 fEKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvfLPTDDkgsilsskyTFLDAWEAMEELVDQGLVKALGVSNFN 163
Cdd:PRK11565 81 -DHKRPREALEESLKKLQLDYVDLYLMHWP---------VPAID---------HYVEAWKGMIELQKEGLIKSIGVCNFQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 164 HFQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPL-----GSPDRPSakpedpllleipkIKEIA 238
Cdd:PRK11565 142 IHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLaqggkGVFDQKV-------------IRDLA 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 71067102 239 AKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:PRK11565 207 DKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEI 257
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
5-293 |
1.70e-67 |
|
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: 211.69 E-value: 1.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTFF 84
Cdd:cd19130 2 IVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAAS----GIPRDELFVTTKLWNDRH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 85 EKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflptddkgsiLSSKYTFLDAWEAMEELVDQGLVKALGVSNFNH 164
Cdd:cd19130 78 DGDEPAAAFAESLAKLGLDQVDLYLVHWP------------------TPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 165 FQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAKHKRT 244
Cdd:cd19130 140 PHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK----------LLGDPPVGAIAAAHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71067102 245 AAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFN 293
Cdd:cd19130 208 PAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
6-289 |
4.68e-66 |
|
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: 209.02 E-value: 4.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 6 TLLTGAKMPIVGLGTWKSPPAK--VREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEK-AVKREDLFIVSKLWST 82
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEGAKgeTYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 83 FFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnVFLPTDDKGSIL---SSKYTFLDA--------WEAMEELVDQ 151
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWP-------IAAEKNDQRSPKlgpDGKYVILKDltenpeptWRAMEEIYES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 152 GLVKALGVSNFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPEDplLLEI 231
Cdd:cd19122 155 GKAKAIGVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGER--VSEN 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 71067102 232 PKIKEIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDfqLSEEDMAAI 289
Cdd:cd19122 231 PTLNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAI 286
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-289 |
1.02e-59 |
|
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: 191.41 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 13 MPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAiqekIQEKAVKREDLFIVSKLWSTFFEKSLVKKA 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 93 FQNTLSDLKLDYLDLYLIHWPqgfqSGNVFLPTDDkgsilsskytFLdawEAMEELVDQGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWP----SPNDEVPVEE----------YI---GALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 173 KPGlKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAKHKRTAAQVLIRF 252
Cdd:cd19139 140 VVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK----------VLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 71067102 253 HIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAI 245
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-289 |
9.65e-58 |
|
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: 186.67 E-value: 9.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWK-----SPPA----KVREAVKVAIDAGYRHIDCAYVYQN---ESEVGEAIqekiqeKAVKREDLFIVS 77
Cdd:cd19072 1 GEEVPVLGLGTWGigggmSKDYsddkKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI------KGFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 78 KLWSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgNVFLPtddkgsilsskytFLDAWEAMEELVDQGLVKAL 157
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP------NPSIP-------------IEETLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 158 GVSNFNHFQIERLLNKPGlKHKPVTNQVECHpYLTQE---KLIQYCHSKGITITAYSPLGSPDRPSAKPedpllleIPKI 234
Cdd:cd19072 136 GVSNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEKGKLSNAKG-------SPLL 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 71067102 235 KEIAAKHKRTAAQVLIRFHIER-NVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19072 207 DEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-289 |
1.64e-57 |
|
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: 187.13 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 16 VGLGTW-------KSPPAKVREAVKVAIDAGYRHIDCAYVY---QNESEVGEAIQEKiqekAVKREDLFIVSKL------ 79
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 80 WSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGfqsgnvflptddkgsilssKYTFLDAWEAMEELVDQGLVKALGV 159
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-------------------DTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 160 SNFNHFQIERLLNKPglKHKPVTNQVECHPY--LTQEKLIQYCHSKGITITAYSPLGSP----------------DRPSA 221
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgeRRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71067102 222 KPEDPLLLE-IPKIKEIAAKHKRTAAQVLIRFHI--ERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:pfam00248 216 KKGTPLNLEaLEALEEIAKEHGVSPAQVALRWALskPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-289 |
2.51e-56 |
|
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: 183.13 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTFF 84
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 85 EKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSgnvflptddkgsilsskyTFLDAWEAMEELVDQGLVKALGVSNFNH 164
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWPAGREG------------------KYVDSWGGLMKLREEGLARSIGVSNFTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 165 FQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAKHKRT 244
Cdd:cd19134 141 EHLENLIDLTFFT--PAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR----------LLDNPAVTAIAAAHGRT 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 71067102 245 AAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-289 |
4.54e-53 |
|
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: 174.74 E-value: 4.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 5 VTLLTGAKMPIVGLGTW-----KSPPAKVREAVKVAIDAGYRHIDCAYVYQN---ESEVGEAIQEKiqekavkREDLFIV 76
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 77 SKLWSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsGNVFLPTddkgsilsskyTFldawEAMEELVDQGLVKA 156
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR-----GGVPLAE-----------TV----AAMEELKKEGKIRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 157 LGVSNFNHFQIERLLNKPGlKHKPVTNQVECHpyLTQE----KLIQYCHSKGITITAYSPLGSPDRPSAKpedplLLEIP 232
Cdd:cd19138 136 WGVSNFDTDDMEELWAVPG-GGNCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLRRG-----LLENP 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 71067102 233 KIKEIAAKHKRTAAQVLIRFHI-ERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19138 208 TLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-297 |
1.63e-50 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 168.28 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 12 KMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKiqekAVKREDLFIVSKLWSTFFEKSLVKK 91
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 92 AFQNTLSDLKLDYLDLYLIHWPQgfqsgnvflPTDDkgsilsskytfLDAWEAMEELVD---QGLVKALGVSNFNHFQIE 168
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWPS---------PNDE-----------VSVEEFMQALLEakkQGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 169 RLLNKPGlKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDrpsakpedplLLEIPKIKEIAAKHKRTAAQV 248
Cdd:PRK11172 138 QAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK----------VLKDPVIARIAAKHNATPAQV 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71067102 249 LIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:PRK11172 207 ILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-289 |
7.11e-49 |
|
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: 163.90 E-value: 7.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWK---------SPPAKVREAVKVAIDAGYRHIDCAYVY---QNESEVGEAIqekiqeKAVKREDLFIVS 77
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAI------KDFPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 78 KLWSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgNVFLPTDDKGSilsskytfldaweAMEELVDQGLVKAL 157
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP------NPNIPLEETLS-------------AMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 158 GVSNFNHFQIERLLNKpgLKHKPVTNQVECHPY---LTQEKLIQYCHSKGITITAYSPLgspDRPSAKPEDPLlleipki 234
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL---RRGLEKTNRTL------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 71067102 235 KEIAAKHKRTAAQVLIRFHIER-NVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19137 204 EEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-289 |
2.41e-41 |
|
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: 145.06 E-value: 2.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 12 KMPIVGLGTWK-----------SPPAKVREAVKVAIDAGYRHIDCAYVYQN-ESE--VGEAIQEKiqekaVKREDLFIVS 77
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYGTgRSErlLGRFLKEL-----GDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 78 K---LWSTFFEKSLVKkAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLptddkgsilsskytfldaWEAMEELVDQGLV 154
Cdd:cd19093 76 KfapLPWRLTRRSVVK-ALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 155 KALGVSNFNHFQIER---LLNKPGlkHKPVTNQVE---CHPYLTQEKLIQYCHSKGITITAYSPLG--------SPDRP- 219
Cdd:cd19093 137 RAVGVSNYSADQLRRahkALKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 220 ----------SAKPEDPLLLEipKIKEIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19093 215 pggrrrlfgrKNLEKVQPLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
9-289 |
2.14e-36 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 132.61 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGTW-------KSPPAKVREAVKVAIDAGYRHIDCAYVY---QNESEVGEAIqekiqeKAVKREDLFIVSK 78
Cdd:COG0667 9 SGLKVSRLGLGTMtfggpwgGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEAL------KGRPRDDVVIATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 79 LWSTFFEKSL--------VKKA---------------FQntlsdlkldyldlylIHWPqgfqsgnvflptDDKGSILssk 135
Cdd:COG0667 83 VGRRMGPGPNgrglsrehIRRAveaslrrlgtdyidlYQ---------------LHRP------------DPDTPIE--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 136 ytflDAWEAMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVEchpY--LTQ---EKLIQYCHSKGITITAY 210
Cdd:COG0667 133 ----ETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 211 SPLGS------PDRPSAKPED---------PLLLE-----IPKIKEIAAKHKRTAAQVLIRF--HIERNVVVIPKSVTPS 268
Cdd:COG0667 206 SPLAGglltgkYRRGATFPEGdraatnfvqGYLTErnlalVDALRAIAAEHGVTPAQLALAWllAQPGVTSVIPGARSPE 285
|
330 340
....*....|....*....|.
gi 71067102 269 RIQENIQVFDFQLSEEDMAAI 289
Cdd:COG0667 286 QLEENLAAADLELSAEDLAAL 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-289 |
8.16e-30 |
|
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: 114.61 E-value: 8.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 14 PIVGLGTWK------SPPAKVREAVKV---AIDAGYRHIDCAYVYQN-ESE--VGEAIQEKiqekavkREDLFIVSKLWS 81
Cdd:cd19085 2 SRLGLGCWQfgggywWGDQDDEESIATihaALDAGINFFDTAEAYGDgHSEevLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 82 TFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflptddkgsilSSKYTFLDAWEAMEELVDQGLVKALGVSN 161
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP-------------------SSDVPLEETMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 162 FNHFQIERLLnKPGlkhKPVTNQVECHPYLTQ-EK-LIQYCHSKGITITAYSPL------GSPDRPSAKPED-------- 225
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQLPYNLLWRAiEYeILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlfr 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71067102 226 -------PLLLE-IPKIKEIAAKHKRTAAQVLIRFHIERNVV--VIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19085 212 hfepgaeEETFEaLEKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-289 |
8.88e-29 |
|
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: 111.85 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTW--------KSPPAKVREAVKVAIDAGYRHIDCAYVYQN-ESE--VGEAIQEKiqekavkREDLFIVSK 78
Cdd:cd19084 1 DLKVSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFgHSEeiLGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 79 ---LW--STFFEKSL----VKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflptDDKGSIlsskytfLDAWEAMEELV 149
Cdd:cd19084 74 cglRWdgGKGVTKDLspesIRKEVEQSLRRLQTDYIDLYQIHWP------------DPNTPI-------EETAEALEKLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 150 DQGLVKALGVSNFNHFQIERLLNkpglKHKPVTNQVechPY--LTQ---EKLIQYCHSKGITITAYSPLG---------- 214
Cdd:cd19084 135 KEGKIRYIGVSNFSVEQLEEARK----YGPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAqglltgkykk 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 215 -----SPDRPSAKP--EDPLLLEIPKI----KEIAAKHKRTAAQVLIRFHIERN--VVVIPKSVTPSRIQENIQVFDFQL 281
Cdd:cd19084 208 eptfpPDDRRSRFPffRGENFEKNLEIvdklKEIAEKYGKSLAQLAIAWTLAQPgvTSAIVGAKNPEQLEENAGALDWEL 287
|
....*...
gi 71067102 282 SEEDMAAI 289
Cdd:cd19084 288 TEEELKEI 295
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
17-285 |
3.05e-26 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 105.23 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 17 GLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVY---QNESEVGEAIQEKiqekAVKREDLFIVSK--------------- 78
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYggyTCEALFGEALKLS----PSLREKIELQTKcgirlpseardnrvk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 79 ---------LWSTffEKSLvkkafQNtlsdlkldyldlylihwpqgfqsgnvfLPTDdkgsilsskY----------TFL 139
Cdd:COG4989 98 hydtskehiIASV--EGSL-----RR---------------------------LGTD---------YldllllhrpdPLM 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 140 DAWE---AMEELVDQGLVKALGVSNFNHFQIErLLNKpGLKHKPVTNQVECHPYLTQ---EKLIQYCHSKGITITAYSPL 213
Cdd:COG4989 135 DPEEvaeAFDELKASGKVRHFGVSNFTPSQFE-LLQS-ALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWSPL 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71067102 214 GSPDRpsAKPEDPLLLEI-PKIKEIAAKHKRTAAQVLIRFhIER---NVVVIPKSVTPSRIQENIQVFDFQLSEED 285
Cdd:COG4989 213 AGGRL--FGGFDEQFPRLrAALDELAEKYGVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
17-285 |
1.26e-24 |
|
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: 100.71 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 17 GLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQN---ESEVGEAIQEKiqekAVKREDLFIVSKlwstffekSLVKKAF 93
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTK--------CGIRLGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 94 QNTLsdlkldyldlyliHWPQGFQSgnvflptdDKGSILSS----------KY----------TFLDAWE---AMEELVD 150
Cdd:cd19092 83 DPRP-------------GRIKHYDT--------SKEHILASvegslkrlgtDYldllllhrpdPLMDPEEvaeAFDELVK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 151 QGLVKALGVSNFNHFQIErLLNKpGLKHKPVTNQVEC---HPYLTQEKLIQYCHSKGITITAYSPLGSpDRpSAKPEDPL 227
Cdd:cd19092 142 SGKVRYFGVSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGG-GR-LFGGFDER 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71067102 228 LLEIPK-IKEIAAKHKRTAAQVLIRF---HIERNVVVIpKSVTPSRIQENIQVFDFQLSEED 285
Cdd:cd19092 218 FQRLRAaLEELAEEYGVTIEAIALAWllrHPARIQPIL-GTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-289 |
8.72e-24 |
|
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: 98.51 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 16 VGLGTWKS----------PPA--KVREAVKVAIDAGYRHIDCAYVY---QNESEVGEAIQEKiqekavkREDLFIVSK-- 78
Cdd:cd19102 4 IGLGTWAIggggwgggwgPQDdrDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 79 -LW------STFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvfLPTDDkgsilsskytFLDAWEAMEELVDQ 151
Cdd:cd19102 77 lLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWP---------DPDEP----------IEEAWGALAELKEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 152 GLVKALGVSNFNHFQIERLlnkpgLKHKPVT-NQVechPY--LTQE---KLIQYCHSKGITITAYSPLGS--------PD 217
Cdd:cd19102 138 GKVRAIGVSNFSVDQMKRC-----QAIHPIAsLQP---PYslLRRGieaEILPFCAEHGIGVIVYSPMQSglltgkmtPE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 218 RPSAKPED-----------PLLLEIPKI----KEIAAKHKRTAAQVLIRFHIERNVV--VIPKSVTPSRIQENIQVFDFQ 280
Cdd:cd19102 210 RVASLPADdwrrrspffqePNLARNLALvdalRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLR 289
|
....*....
gi 71067102 281 LSEEDMAAI 289
Cdd:cd19102 290 LTPEELAEI 298
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-275 |
5.94e-20 |
|
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: 86.80 E-value: 5.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 16 VGLGTW----KSPPAKVREAVKVAIDAGYRHIDCAYVYQN-ESE--VGEAIQEKiqekaVKREDLFIVSKLWSTF----- 83
Cdd:cd06660 3 LGLGTMtfggDGDEEEAFALLDAALEAGGNFFDTADVYGDgRSErlLGRWLKGR-----GNRDDVVIATKGGHPPggdps 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 84 ------------FEKSLvkKA--------FqntlsdlkldyldlyLIHWPqgfqsgNVFLPTDdkgsilsskytflDAWE 143
Cdd:cd06660 78 rsrlspehirrdLEESL--RRlgtdyidlY---------------YLHRD------DPSTPVE-------------ETLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 144 AMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHK--PVTNQVE---CHPYLTQEKLIQYCHSKGITITAYSPLGspdr 218
Cdd:cd06660 122 ALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLpgFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA---- 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 71067102 219 psakpedpllleipkikeiaakhkRTAAQVLIRF--HIERNVVVIPKSVTPSRIQENIQ 275
Cdd:cd06660 198 ------------------------RGPAQLALAWllSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
29-291 |
8.33e-20 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 87.86 E-value: 8.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 29 REAVKVAIDAGYRHIDCAYVY---QNESEVGEAIQEKiqekavKREDLFIVSKLWSTFFEKSLV--------KKAFQNTL 97
Cdd:cd19083 36 KDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKFGGDGSVlnnspeflRSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 98 SDLKLDYLDLYLIHWPQGfqsgnvFLPTDdkgsilsskytflDAWEAMEELVDQGLVKALGVSNFNHFQIERlLNKPGLk 177
Cdd:cd19083 110 KRLNTDYIDLYYIHFPDG------ETPKA-------------EAVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDGY- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 178 hkpvTNQVEcHPY-LTQ----EKLIQYCHSKGITITAYSPL------GSPDRPSAKPEDPLLLEIP-------------- 232
Cdd:cd19083 169 ----VDVLQ-GEYnLLQreaeEDILPYCVENNISFIPYFPLasgllaGKYTKDTKFPDNDLRNDKPlfkgerfsenldkv 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71067102 233 -KIKEIAAKHKRTAAQVLIRFHIERNVV--VIPKSVTPSRIQENIQVFDFQLSEEDMAAILS 291
Cdd:cd19083 244 dKLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
10-282 |
2.44e-19 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 85.35 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAkMPIVGLGTWKSPP--AKVREAVKVAIDAGYRHIDCAYVYqnesevGEAIQEKIQEKAVK--REDLFIVSKL------ 79
Cdd:cd19088 7 GA-MRLTGPGIWGPPAdrEEAIAVLRRALELGVNFIDTADSY------GPDVNERLIAEALHpyPDDVVIATKGglvrtg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 80 ---WSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflptddkgsilSSKYTFLDAWEAMEELVDQGLVKA 156
Cdd:cd19088 80 pgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI-------------------DPKVPFEEQLGALAELQDEGLIRH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 157 LGVSNFNHFQIERLLNKPGLkhkpVTNQVECHPYLTQ-EKLIQYCHSKGITITAYSPLGSpdRPSAKPEDPLlleipkiK 235
Cdd:cd19088 141 IGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG--GDLAQPGGLL-------A 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71067102 236 EIAAKHKRTAAQVLIRFHIER--NVVVIPKSVTPSRIQENIQVFDFQLS 282
Cdd:cd19088 208 EVAARLGATPAQVALAWLLARspVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
9-289 |
1.00e-18 |
|
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: 84.94 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGT----------WKSPPAKVREAVKVAIDAGYRHIDCAYVYQN-ESE--VGEAIQEKIqekavKREDLFI 75
Cdd:cd19079 8 SGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgASEeiLGRALKEFA-----PRDEVVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 76 VSKlwstffekslvkkafqntlsdlkldyldlylihwpqgfqsgnVFLPTDD--KGSILSSKYTF--LDA---------- 141
Cdd:cd19079 83 ATK------------------------------------------VYFPMGDgpNGRGLSRKHIMaeVDAslkrlgtdyi 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 142 -------W----------EAMEELVDQGLVKALGVSNFNHFQIERLLN---KPGLkHKPVTNQvecHPY--LTQE---KL 196
Cdd:cd19079 121 dlyqihrWdyetpieetlEALHDVVKSGKVRYIGASSMYAWQFAKALHlaeKNGW-TKFVSMQ---NHYnlLYREeerEM 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 197 IQYCHSKGITITAYSPL----------GSPDRPSAKPEDPLLLE----------IPKIKEIAAKHKRTAAQVLIRFHIER 256
Cdd:cd19079 197 IPLCEEEGIGVIPWSPLargrlarpwgDTTERRRSTTDTAKLKYdyfteadkeiVDRVEEVAKERGVSMAQVALAWLLSK 276
|
330 340 350
....*....|....*....|....*....|....*
gi 71067102 257 NVVVIP--KSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19079 277 PGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
143-289 |
5.16e-16 |
|
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: 76.89 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 143 EAMEELVDQGLVKALGVSNFNHFQIERLLNKpglkHKPVTNQVECHPyLTQEKL----IQYCHSKGITITAYSPLG---- 214
Cdd:cd19077 132 KALKELVKEGKIRGIGLSEVSAETIRRAHAV----HPIAAVEVEYSL-FSREIEengvLETCAELGIPIIAYSPLGrgll 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 215 SPDRPSAK--PEDPLLLEIP---------------KIKEIAAKHKRTAAQVLIRFHIERN---VVVIPKSVTPSRIQENI 274
Cdd:cd19077 207 TGRIKSLAdiPEGDFRRHLDrfngenfeknlklvdALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENL 286
|
170
....*....|....*
gi 71067102 275 QVFDFQLSEEDMAAI 289
Cdd:cd19077 287 KAANVELTDEELKEI 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-289 |
6.15e-16 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 77.55 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGTW---KSPPAKVREAVKVAIDAGYRHIDCAYVY-QNESEVGEAIQEKiqekavkREDLFIVSKL--WS- 81
Cdd:COG1453 9 TGLEVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLppWVr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 82 ------TFFEKSLvkKAFQ----NtlsdlkldyldLYLIH-------WPQGFQSGnvflptddkgsilsskytflDAWEA 144
Cdd:COG1453 82 dpedmrKDLEESL--KRLQtdyiD-----------LYLIHglnteedLEKVLKPG--------------------GALEA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 145 MEELVDQGLVKALGVSNFNHFQ-IERLLNkpglkhkpvTNQVEC---------HPYLTQEKLIQYCHSKGITITAYSPLG 214
Cdd:COG1453 129 LEKAKAEGKIRHIGFSTHGSLEvIKEAID---------TGDFDFvqlqynyldQDNQAGEEALEAAAEKGIGVIIMKPLK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 215 spdrpsakpeDPLLLEIP-KIKEIaAKHKRTAAQVLIRF--HIERNVVVIPKSVTPSRIQENIQVFD--FQLSEEDMAAI 289
Cdd:COG1453 200 ----------GGRLANPPeKLVEL-LCPPLSPAEWALRFllSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAIL 268
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
144-289 |
6.91e-14 |
|
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: 70.93 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 144 AMEELVDQGLVKALGVSNFNHFQIERllnkpglKHK--PVTN-QVECHPYLT-----QEKLIQYCHSKGITITAYSPLG- 214
Cdd:cd19144 140 AMAELVQEGKIKHIGLSECSAETLRR-------AHAvhPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGr 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 215 --------SPD----------RPSAKPED-PLLLE-IPKIKEIAAKHKRTAAQVLIRFHIER--NVVVIPKSVTPSRIQE 272
Cdd:cd19144 213 gfltgairSPDdfeegdfrrmAPRFQAENfPKNLElVDKIKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRLEE 292
|
170
....*....|....*..
gi 71067102 273 NIQVFDFQLSEEDMAAI 289
Cdd:cd19144 293 NLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
16-289 |
9.89e-14 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 70.41 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 16 VGLGTWK--------SPPAKVREAVKVAIDAGYRHIDCAYVY---QNESEVGEAIQEKiqekaVKREDLFIVSKL---W- 80
Cdd:cd19148 7 IALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEY-----GKRDRVVIATKVgleWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 81 --------STffeKSLVKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflptDDKgsilsskYTFLDAWEAMEELVDQG 152
Cdd:cd19148 82 eggevvrnSS---PARIRKEVEDSLRRLQTDYIDLYQVHWP------------DPL-------VPIEETAEALKELLDEG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 153 LVKALGVSNFNHFQIERLLNKPGLKhkpvTNQVechPY-----LTQEKLIQYCHSKGITITAYSPL------GSPDRPSA 221
Cdd:cd19148 140 KIRAIGVSNFSPEQMETFRKVAPLH----TVQP---PYnlferEIEKDVLPYARKHNIVTLAYGALcrgllsGKMTKDTK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 222 KPEDPLLLEIPKIKE------IAA----------KHKRTAAQVLIRFHIERNVVVIP--KSVTPSRIQENIQVFDFQLSE 283
Cdd:cd19148 213 FEGDDLRRTDPKFQEprfsqyLAAveeldklaqeRYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLND 292
|
....*.
gi 71067102 284 EDMAAI 289
Cdd:cd19148 293 EDMKEI 298
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
140-289 |
1.15e-13 |
|
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: 70.32 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 140 DAWEAMEELVDQGLVKALGVSNFNHFQIERllnkpglKHK--PVTN-QVECHPYLT--QEKLIQYCHSKGITITAYSPLG 214
Cdd:cd19076 133 ETVGAMAELVEEGKVRYIGLSEASADTIRR-------AHAvhPITAvQSEYSLWTRdiEDEVLPTCRELGIGFVAYSPLG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 215 ------SPDRPSAKPEDPLLLEIP---------------KIKEIAAKHKRTAAQ-----VLirfHIERNVVVIPKSVTPS 268
Cdd:cd19076 206 rgfltgAIKSPEDLPEDDFRRNNPrfqgenfdknlklveKLEAIAAEKGCTPAQlalawVL---AQGDDIVPIPGTKRIK 282
|
170 180
....*....|....*....|.
gi 71067102 269 RIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19076 283 YLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
138-289 |
1.47e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 69.93 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 138 FLDAWEAMEELVDQGLVKALGVSNFNHFQIERLLNKPGlkhKPVTNQVEC-----HPyltQEKLIQYCHSKGITITAYSP 212
Cdd:cd19101 121 YLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAGV---PIVSNQVQYslldrRP---ENGMAALCEDHGIKLLAYGT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 213 LGSP-------DRPSAKPEDPL----------------------LLEipKIKEIAAKHKRTAAQVLIRFHIERNVV--VI 261
Cdd:cd19101 195 LAGGllsekylGVPEPTGPALEtrslqkyklmidewggwdlfqeLLR--TLKAIADKHGVSIANVAVRWVLDQPGVagVI 272
|
170 180
....*....|....*....|....*...
gi 71067102 262 PKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19101 273 VGARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-284 |
4.11e-13 |
|
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: 68.39 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAKMPIVGLGTWKSPPAKV-----REAVKVAIDAGYRHIDCAYVY---QNESEVGEAIQEkiqekaVKREDLFIVSKlws 81
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVddedaKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG------WPRESYVISTK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 82 tffekslvkkafqntlsdlkldyldlylIHWPQGfQSGNvflptdDKGsiLSSKYTF--------------LDAW----- 142
Cdd:cd19074 72 ----------------------------VFWPTG-PGPN------DRG--LSRKHIFesihaslkrlqldyVDIYychry 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 143 ----------EAMEELVDQGLVKALGVSNFNHFQIE---RLLNKPGLkHKPVTNQVECHpYLTQEK---LIQYCHSKGIT 206
Cdd:cd19074 115 dpetpleetvRAMDDLIRQGKILYWGTSEWSAEQIAeahDLARQFGL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 207 ITAYSPLGS-------------PDRPSAKPE-----------DPLLLEIPKIKEIAAKHKRTAAQVLIRFHIERNVV--V 260
Cdd:cd19074 193 LVVWSPLAQglltgkyrdgippPSRSRATDEdnrdkkrrlltDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVssA 272
|
330 340
....*....|....*....|....
gi 71067102 261 IPKSVTPSRIQENIQVFDFQLSEE 284
Cdd:cd19074 273 IIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-276 |
5.11e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 67.61 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGTWKSPPAKVrEAVKVAIDAGYRHIDCAYVYQN---ESEVGEAIqekiqeKAVKREDLFIVSKLWSTF-- 83
Cdd:cd19105 9 TGLKVSRLGFGGGGLPRESP-ELLRRALDLGINYFDTAEGYGNgnsEEIIGEAL------KGLRRDKVFLATKASPRLdk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 84 ---------FEKSLvkKAFQNTLSDlkldyldLYLIHwpqgfqsgnvfLPTDDKGSILSskytflDAW-EAMEELVDQGL 153
Cdd:cd19105 82 kdkaellksVEESL--KRLQTDYID-------IYQLH-----------GVDTPEERLLN------EELlEALEKLKKEGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 154 VKALGVSnfNHFQIERLLNKpglkhkpvtnQVECHPY---------LTQ----EKLIQYCHSKGITITAYSPLGspdrpS 220
Cdd:cd19105 136 VRFIGFS--THDNMAEVLQA----------AIESGWFdvimvaynfLNQpaelEEALAAAAEKGIGVVAMKTLA-----G 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 71067102 221 AKPEDPLLLEIPKIKEiaakhkrTAAQVLIRFHI-ERNV-VVIPKSVTPSRIQENIQV 276
Cdd:cd19105 199 GYLQPALLSVLKAKGF-------SLPQAALKWVLsNPRVdTVVPGMRNFAELEENLAA 249
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
9-291 |
5.75e-13 |
|
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: 68.07 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGTW---------KSPPAKVREAVKVAIDAGYRHIDCAYVY-QNESE--VGEAIQEKiqekavkREDLFIV 76
Cdd:cd19149 7 SGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYgFGHSEeiVGKAIKGR-------RDKVVLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 77 SK---LWST----FFEKSLVKKAFQNTLSDLKLDYLDLY------------LIHWPqgfqsgnvflptddkgsilSSKYT 137
Cdd:cd19149 80 TKcglRWDReggsFFFVRDGVTVYKNLSPESIREEVEQSlkrlgtdyidlyQTHWQ-------------------DVETP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 138 FLDAWEAMEELVDQGLVKALGVSNFNHFQIERLlnkpgLKHKPV-TNQVechPY-----LTQEKLIQYCHSKGITITAYS 211
Cdd:cd19149 141 IEETMEALEELKRQGKIRAIGASNVSVEQIKEY-----VKAGQLdIIQE---KYsmldrGIEKELLPYCKKNNIAFQAYS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 212 PLGS--------PDRP----SAKPEDPL-----------LLEipKIKEIAAKHKRTAAQVLIR--FHIERNVVVIPKSVT 266
Cdd:cd19149 213 PLEQglltgkitPDREfdagDARSGIPWfspenrekvlaLLE--KWKPLCEKYGCTLAQLVIAwtLAQPGITSALCGARK 290
|
330 340
....*....|....*....|....*
gi 71067102 267 PSRIQENIQVFDFQLSEEDMAAILS 291
Cdd:cd19149 291 PEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
9-289 |
6.64e-13 |
|
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: 68.02 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGT--------WKSPPAKV--REA---VKVAIDAGYRHIDCAYVYQN-ESEV--GEAIQEKiqekavkRED 72
Cdd:cd19091 9 SGLKVSELALGTmtfgggggFFGAWGGVdqEEAdrlVDIALDAGINFFDTADVYSEgESEEilGKALKGR-------RDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 73 LFIVSKlwstffekslvkkafqntlsdlkldyldlylihwpqgfqsgnVFLPTDD--------KGSILSS---------- 134
Cdd:cd19091 82 VLIATK------------------------------------------VRGRMGEgpndvglsRHHIIRAveaslkrlgt 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 135 KYT---FLDAW----------EAMEELVDQGLVKALGVSNFNHFQIERLL---NKPGLKhKPVTNQVechpYLT------ 192
Cdd:cd19091 120 DYIdlyQLHGFdaltpleetlRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdl 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 193 QEKLIQYCHSKGITITAYSPLG--------SPDRPSAK------------PEDPLLLE--IPKIKEIAAKHKRTAAQVLI 250
Cdd:cd19091 195 EHELMPLALDQGVGLLVWSPLAggllsgkyRRGQPAPEgsrlrrtgfdfpPVDRERGYdvVDALREIAKETGATPAQVAL 274
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 71067102 251 RFHIERNVV--VIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19091 275 AWLLSRPTVssVIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
110-289 |
2.29e-12 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 66.43 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 110 IHWP---QGFQSGNVFLPTDDKGSILSskytFLDAWEAMEELVDQGLVKALGVSNFNHFQIERLLN---KPGLKhKPVTN 183
Cdd:cd19094 119 LHWPdryTPLFGGGYYTEPSEEEDSVS----FEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLElaeQLGLP-RIVSI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 184 QvecHPY--LTQ---EKLIQYCHSKGITITAYSPLG----------SPDRPS-----------AKPEDPLLLE-IPKIKE 236
Cdd:cd19094 194 Q---NPYslLNRnfeEGLAEACHRENVGLLAYSPLAggvltgkyldGAARPEggrlnlfpgymARYRSPQALEaVAEYVK 270
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71067102 237 IAAKHKRTAAQVLIRFHIERNVV--VIPKSVTPSRIQENIQVFDFQLSEEDMAAI 289
Cdd:cd19094 271 LARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELLAEI 325
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-226 |
3.27e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 65.20 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGTWKSPPAKVREAVKV---AIDAGYRHIDCAYVYQN-ESEVGEAIQEKiqekavkREDLFIVSKLWSTFF 84
Cdd:cd19100 7 TGLKVSRLGFGGGPLGRLSQEEAAAIirrALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGARDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 85 EKslVKKAFQNTLSDLKLDYLDLYLIH------WPQgfqsgnvfLPTDDKGsilsskytfldAWEAMEELVDQGLVKALG 158
Cdd:cd19100 80 EG--AKRDLERSLKRLGTDYIDLYQLHavdteeDLD--------QVFGPGG-----------ALEALLEAKEEGKIRFIG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 159 VSNFNHFQIERLLNKPGLK--HKPVtNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPEDP 226
Cdd:cd19100 139 ISGHSPEVLLRALETGEFDvvLFPI-NPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP 207
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-289 |
4.91e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 65.43 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 12 KMPIVGLGTWK--SP-------------PAKVREAVKVAIDAGYRHIDCAYVY---QNESEVGEAIqekiqeKAVKREDL 73
Cdd:cd19103 3 KLPKIALGTWSwgSGgaggdqvfgnhldEDTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFL------KRYPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 74 FIVSKLWSTFFEKSL--VKKAFQNTLSDLKLDYLDLYLIHwpqgfqsgnvfLPTDdkgsilsskytfLDAW-EAMEELVD 150
Cdd:cd19103 77 IISTKFTPQIAGQSAdpVADMLEGSLARLGTDYIDIYWIH-----------NPAD------------VERWtPELIPLLK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 151 QGLVKALGVSNFNHFQIER---LLNKPGLKHKPVTNqvecH---PYLTQEK--LIQYCHSKGITITAYSPL------GSP 216
Cdd:cd19103 134 SGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQN----HyslLYRSSEEagILDYCKENGITFFAYMVLeqgalsGKY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 217 DRPSAKPED--------PLLLEI----PKIKEIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEE 284
Cdd:cd19103 210 DTKHPLPEGsgraetynPLLPQLeeltAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDD 289
|
....*
gi 71067102 285 DMAAI 289
Cdd:cd19103 290 EIKEL 294
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-284 |
2.13e-11 |
|
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: 63.34 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 14 PIVGLGT------WKS-PPAKVREAVKVAIDAGYRHIDCAYVYqNESE--VGEAIQEkiqekaVKREDLFIVSKL----- 79
Cdd:cd19090 1 SALGLGTaglggvFGGvDDDEAVATIRAALDLGINYIDTAPAY-GDSEerLGLALAE------LPREPLVLSTKVgrlpe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 80 WSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFlptdDKGSILsskytfldawEAMEELVDQGLVKALGV 159
Cdd:cd19090 74 DTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIL----APGGAL----------EALLELKEEGLIKHIGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 160 SNFNHFQIERLLNkpglkhkpvTNQVEC----HPY--LTQE---KLIQYCHSKGITITAYSPLGS-------PDRPSAKP 223
Cdd:cd19090 140 GGGPPDLLRRAIE---------TGDFDVvltaNRYtlLDQSaadELLPAAARHGVGVINASPLGMgllagrpPERVRYTY 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71067102 224 EDPLLLEIP---KIKEIAAKHKRTAAQVLIRFHI--ERNVVVIPKSVTPSRIQENIQVFDFQLSEE 284
Cdd:cd19090 211 RWLSPELLDrakRLYELCDEHGVPLPALALRFLLrdPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
143-275 |
1.43e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 60.81 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 143 EAMEELVDQGLVKALGVSNFNHFQIER---LLNKPGLkHKPVTNQVEcHPYL--------------TQEkLIQYCHSKG- 204
Cdd:cd19752 132 EAFNELVKAGKVRAIGASNFAAWRLERarqIARQQGW-AEFSAIQQR-HSYLrprpgadfgvqrivTDE-LLDYASSRPd 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 205 ITITAYSPL-----GSPDRPSAKPED--PLLLEIPKIKEIAAKHKRTAAQVLIRFHIERNVVVIP--KSVTPSRIQENIQ 275
Cdd:cd19752 209 LTLLAYSPLlsgayTRPDRPLPEQYDgpDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-276 |
1.88e-10 |
|
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: 60.33 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 14 PIVGLGTWK-------SPPAKVREAVKVAIDAGYRHIDCAYVYQN-ESEVGEAIqekiqeKAVKREDLFIVSKLWSTF-- 83
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL------AGLRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 84 ---------------FEKSLVK------KAFQntlsdlkldyldlylIHWPQgfqsgnvflPTDDKGSILsskytfldaw 142
Cdd:cd19095 75 grdrkdfspaairasIERSLRRlgtdyiDLLQ---------------LHGPS---------DDELTGEVL---------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 143 EAMEELVDQGLVKALGVSNFNHfQIERLLNKPGLKhkpvTNQVechPY----LTQEKLIQYCHSKGITITAYSPLGSPDR 218
Cdd:cd19095 121 ETLEDLKAAGKVRYIGVSGDGE-ELEAAIASGVFD----VVQL---PYnvldREEEELLPLAAEAGLGVIVNRPLANGRL 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71067102 219 PSAKPEDPLLLEIPKIKEIAAKHK-RTAAQVLIRF--HIERNVVVIPKSVTPSRIQENIQV 276
Cdd:cd19095 193 RRRVRRRPLYADYARRPEFAAEIGgATWAQAALRFvlSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-252 |
1.94e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 60.79 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 16 VGLGTWKSPP-----AKVREAVKVAIDAGYRHIDCAYVYQN-ESE--VGEAIQEKIQEKAVKREDLFIVSK--LWSTFFE 85
Cdd:cd19099 6 LGLGTYRGDSddetdEEYREALKAALDSGINVIDTAINYRGgRSErlIGKALRELIEKGGIKRDEVVIVTKagYIPGDGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 86 KSLVKKAFQNTLSDLKLDYLDLYL-------------------------------IHWPQGFQSgnvflptDDKGSILSS 134
Cdd:cd19099 86 EPLRPLKYLEEKLGRGLIDVADSAglrhcispayledqierslkrlgldtidlylLHNPEEQLL-------ELGEEEFYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 135 KytFLDAWEAMEELVDQGLVKALGVSNFN----------HFQIERLL--------NKPGLKHkpVtnQVECHPYLTQ--- 193
Cdd:cd19099 159 R--LEEAFEALEEAVAEGKIRYYGISTWDgfrappalpgHLSLEKLVaaaeevggDNHHFKV--I--QLPLNLLEPEalt 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71067102 194 ---------EKLIQYCHSKGITITAYSPLGSPDrpsakpedpLLLEIPKIKEIAAKHKRTAAQVLIRF 252
Cdd:cd19099 233 ekntvkgeaLSLLEAAKELGLGVIASRPLNQGQ---------LLGELRLADLLALPGGATLAQRALQF 291
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
143-289 |
1.04e-09 |
|
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: 58.38 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 143 EAMEELVDQGLVKALGVSNFNHFQIERLLN---KPGLKhKPVTNQVEchpY------LTQEKLIQYCHSKGITITAYSPL 213
Cdd:cd19081 135 GALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGLP-RYVSLQPE---YnlvdreSFEGELLPLCREEGIGVIPYSPL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 214 G---------SPDRPSAKPEDPLLLE----------IPKIKEIAAKHKRTAAQVLIRFHIERNVV--VIPKSVTPSRIQE 272
Cdd:cd19081 211 AggfltgkyrSEADLPGSTRRGEAAKrylnerglriLDALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLED 290
|
170
....*....|....*..
gi 71067102 273 NIQVFDFQLSEEDMAAI 289
Cdd:cd19081 291 LLAAAGLRLTDEEVARL 307
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
24-278 |
1.54e-09 |
|
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: 57.57 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 24 PPAKVREAVKVAIDAGYRHIDCAYVY---QNESEVGEAIqekiqeKAVKREDLFIVSKL--WST--------FFEKSLVK 90
Cdd:cd19096 19 DEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEAL------KEGPREKFYLATKLppWSVksaedfrrILEESLKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 91 ---KAFQNtlsdlkldyldlYLIHWpqgFQSGNVFLptddkgsilssKYTFLDAWEAMEELVDQGLVKALGVSnfnhF-- 165
Cdd:cd19096 93 lgvDYIDF------------YLLHG---LNSPEWLE-----------KARKGGLLEFLEKAKKEGLIRHIGFS----Fhd 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 166 ---QIERLLNkpglkhkpvTNQVEC----HPYLTQE-----KLIQYCHSKGITITAYSPLGSPDrpsakpedpLLLEIPK 233
Cdd:cd19096 143 speLLKEILD---------SYDFDFvqlqYNYLDQEnqagrPGIEYAAKKGMGVIIMEPLKGGG---------LANNPPE 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 71067102 234 IKEIAAKHKRTAAQVLIRF---HIERNVVVIPKSvTPSRIQENIQVFD 278
Cdd:cd19096 205 ALAILCGAPLSPAEWALRFllsHPEVTTVLSGMS-TPEQLDENIAAAD 251
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-215 |
1.92e-09 |
|
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: 57.10 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 16 VGLGTW--------KSPPAKVREAVKVAIDAGYRHIDCAYVYQN-ESE--VGEAIQEKiqekavkREDLFIVSKL----- 79
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYGDgHSErlLGKALKGR-------RDKVVIATKFgnrfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 80 ----WSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHwpqgfqsgNVFLPTDDKGsilsskytflDAWEAMEELVDQGLVK 155
Cdd:cd19086 79 ggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLH--------NPPDEVLDND----------ELFEALEKLKQEGKIR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71067102 156 ALGVSNFNHFQIERLLNKPGLkhkpVTNQV-----ECHPYltqEKLIQYCHSKGITITAYSPLGS 215
Cdd:cd19086 141 AYGVSVGDPEEALAALRRGGI----DVVQViynllDQRPE---EELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-278 |
2.79e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 50.99 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 17 GLGTW-------------KSPPAKVREAVKVAIDAGYRHIDCAYVYqnesevGEAiQEKIQEKAVKREDLFIVSKL---- 79
Cdd:cd19097 4 ALGTAqfgldygianksgKPSEKEAKKILEYALKAGINTLDTAPAY------GDS-EKVLGKFLKRLDKFKIITKLpplk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 80 WSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNvflptddkgsilsskytfLDAWEAMEELVDQGLVKALGV 159
Cdd:cd19097 77 EDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHG------------------GKLVEALLELKKEGLIRKIGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 160 SNFNHFQIERLLNKPGLKHkpVtnQVECHPY---LTQEKLIQYCHSKGITITAYSP------LGSPDRPSAKPED--PLL 228
Cdd:cd19097 139 SVYSPEELEKALESFKIDI--I--QLPFNILdqrFLKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLPAKFAPakPLL 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 71067102 229 LeipKIKEIAAKHKRTAAQVLIRF-----HIERNVVVIpksVTPSRIQENIQVFD 278
Cdd:cd19097 215 K---KLHELAKKLGLSPLELALGFvlslpEIDKIVVGV---DSLEQLKEIIAAFK 263
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
144-289 |
1.17e-06 |
|
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: 49.35 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 144 AMEELVDQGLVKALGVSNFNHFQIERllnkpglKH--KPVTN-QVECHPYL--TQEKLIQYCHSKGITITAYSPLG---- 214
Cdd:cd19145 138 ELKKLVEEGKIKYIGLSEASADTIRR-------AHavHPITAvQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLGrgff 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 215 --SPDRPSAKPEDPLLLEIP---------------KIKEIAAKHKRTAAQVLIRF--HIERNVVVIPKSVTPSRIQENIQ 275
Cdd:cd19145 211 agKAKLEELLENSDVRKSHPrfqgenleknkvlyeRVEALAKKKGCTPAQLALAWvlHQGEDVVPIPGTTKIKNLNQNIG 290
|
170
....*....|....
gi 71067102 276 VFDFQLSEEDMAAI 289
Cdd:cd19145 291 ALSVKLTKEDLKEI 304
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
144-289 |
1.39e-06 |
|
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: 49.14 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 144 AMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHK--PVTNQVECHpyLTQ----EKLIQYCHSKGITITAYSPLGS-- 215
Cdd:cd19080 135 ALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWspFVALQIEYS--LLErtpeRELLPMARALGLGVTPWSPLGGgl 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 216 -----------------PDRPSAKPEDPLLLEI-PKIKEIAAKHKRTAAQVLIRFHIERNVVVIP--KSVTPSRIQENIQ 275
Cdd:cd19080 213 ltgkyqrgeegrageakGVTVGFGKLTERNWAIvDVVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLG 292
|
170
....*....|....
gi 71067102 276 VFDFQLSEEDMAAI 289
Cdd:cd19080 293 ALDLTLSPEQLARL 306
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
9-287 |
1.18e-05 |
|
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: 46.10 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGTWK-----SPPAKVREAVKVAIDAGYRHIDCAYVY-----QNESEVGEAIQekiQEKAVKREDLFIvsk 78
Cdd:cd19089 7 SGLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILK---RDLRPYRDELVI--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 79 lwSTffekslvkKAFQNTlsdlkldyldlylihWPqgfqsgnvfLPTDDKGS---ILSS-----KYTFLD---------- 140
Cdd:cd19089 81 --ST--------KAGYGM---------------WP---------GPYGDGGSrkyLLASldqslKRMGLDyvdifyhhry 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 141 --------AWEAMEELVDQGlvKAL--GVSNFNHFQIER---LLNKpgLKHKPVTNQVechPY--LTQ---EKLIQYCHS 202
Cdd:cd19089 127 dpdtpleeTMTALADAVRSG--KALyvGISNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 203 KGITITAYSPL-----------GSPDRPSAKPEDPLLLE----------IPKIKEIAAKHKRTAAQVLIRFHIERNVV-- 259
Cdd:cd19089 200 AGIGFIAFSPLaqglltdkylnGIPPDSRRAAESKFLTEealtpekleqLRKLNKIAAKRGQSLAQLALSWVLRDPRVts 279
|
330 340
....*....|....*....|....*....
gi 71067102 260 VIPKSVTPSRIQENIQVFD-FQLSEEDMA 287
Cdd:cd19089 280 VLIGASSPSQLEDNVAALKnLDFSEEELA 308
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-289 |
1.81e-05 |
|
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: 45.72 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLG------TW-KSPPAKVREAVKVAIDAGYRHIDCAYVY-QNESEV--GEAIQEKiqekavkREDLFIVSK 78
Cdd:cd19104 8 TGLKVSELTFGgggiggLMgRTTREEQIAAVRRALDLGINFFDTAPSYgDGKSEEnlGRALKGL-------PAGPYITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 79 ----------LWSTF---FEKSLVK------KAFQntlsdlkldyldlylIHwpqgfqsgNVFLPTDDKGSILSSKYT-F 138
Cdd:cd19104 81 vrldpddlgdIGGQIersVEKSLKRlkrdsvDLLQ---------------LH--------NRIGDERDKPVGGTLSTTdV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 139 L---DAWEAMEELVDQGLVKALGVSNFNHFQ-----IER-----------LLNKP-GLKHKPVtnqvecHPYLTQEKLIQ 198
Cdd:cd19104 138 LglgGVADAFERLRSEGKIRFIGITGLGNPPairelLDSgkfdavqvyynLLNPSaAEARPRG------WSAQDYGGIID 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 199 YCHSKGITITAYSPL------GSPDRPsakPEDPLLLEIP---------KIKEIAAKHKRTAAQVLIRFHIERNVV--VI 261
Cdd:cd19104 212 AAAEHGVGVMGIRVLaagaltTSLDRG---REAPPTSDSDvaidfrraaAFRALAREWGETLAQLAHRFALSNPGVstVL 288
|
330 340
....*....|....*....|....*....
gi 71067102 262 PKSVTPSRIQENIQVFDF-QLSEEDMAAI 289
Cdd:cd19104 289 VGVKNREELEEAVAAEAAgPLPAENLARL 317
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
35-289 |
6.36e-05 |
|
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: 44.10 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 35 AIDAGYRHIDCAYVYQN-ESE--VGEAIQEKiqekavkREDLFIVSKlwstffekslvkkafqntlsdlkldyldlylih 111
Cdd:cd19087 39 ALDAGINFFDTADVYGGgRSEeiIGRWIAGR-------RDDIVLATK--------------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 112 wpqgfqsgnVFLPTD----DKGSilsSKYTFLDA------------------------------WEAMEELVDQGLVKAL 157
Cdd:cd19087 79 ---------VFGPMGddpnDRGL---SRRHIRRAveaslrrlqtdyidlyqmhhfdrdtpleetLRALDDLVRQGKIRYI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 158 GVSNFNHFQIERLLN---KPGLKH----KPVTNQVECHPYLtqeKLIQYCHSKGITITAYSPLGS-----PDRPSAKPED 225
Cdd:cd19087 147 GVSNFAAWQIAKAQGiaaRRGLLRfvseQPMYNLLKRQAEL---EILPAARAYGLGVIPYSPLAGglltgKYGKGKRPES 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 226 PLLLE----------------IPKIKEIAAKHKRTAAQVLIRFHIERNVV---VI-PKsvTPSRIQENIQVFDFQLSEED 285
Cdd:cd19087 224 GRLVEraryqarygleeyrdiAERFEALAAEAGLTPASLALAWVLSHPAVtspIIgPR--TLEQLEDSLAALEITLTPEL 301
|
....
gi 71067102 286 MAAI 289
Cdd:cd19087 302 LAEI 305
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
10-287 |
9.47e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 43.42 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 10 GAkMPIVGLGTWkSPPAKVREAVKV---AIDAGYRHIDCAYVYqnesevGEAIQEKIQEKAVK--REDLFIVSKL----- 79
Cdd:PRK10376 23 GA-MQLAGPGVF-GPPKDRDAAIAVlreAVALGVNHIDTSDFY------GPHVTNQLIREALHpyPDDLTIVTKVgarrg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 80 ----WSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHwpqgfQSGNVFLPTDdkGSILsskytflDAWEAMEELVDQGLVK 155
Cdd:PRK10376 95 edgsWLPAFSPAELRRAVHDNLRNLGLDVLDVVNLR-----LMGDGHGPAE--GSIE-------EPLTVLAELQRQGLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 156 ALGVSNFNHFQIER---------LLNKPGLKHKpvtnqvechpylTQEKLIQYCHSKGITITAYSPLG--SPDRPSAkpe 224
Cdd:PRK10376 161 HIGLSNVTPTQVAEarkiaeivcVQNHYNLAHR------------ADDALIDALARDGIAYVPFFPLGgfTPLQSST--- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71067102 225 dpllleipkIKEIAAKHKRTAAQVLIRFHIER--NVVVIPKSVTPSRIQENIQVFDFQLSEEDMA 287
Cdd:PRK10376 226 ---------LSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLA 281
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-253 |
4.37e-04 |
|
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: 41.39 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 15 IVGLGTW-----KSPPAKVREAVKVAIDAGYRHIDCAYVYQN-ESE--VGEAiqeKIQEKAVKredlfIVSKlWSTFFEK 86
Cdd:cd19075 4 ILGTMTFgsqgrFTTAEAAAELLDAFLERGHTEIDTARVYPDgTSEelLGEL---GLGERGFK-----IDTK-ANPGVGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 87 SL----VKKAFQNTLSDLkldyldlylihwpqGFQSGNVF-LPTDDKGSILSskytflDAWEAMEELVDQGLVKALGVSN 161
Cdd:cd19075 75 GLspenVRKQLETSLKRL--------------KVDKVDVFyLHAPDRSTPLE------ETLAAIDELYKEGKFKEFGLSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 162 FNHFQIERLLN--------KP----GLkHKPVTNQVEchpyltqEKLIQYCHSKGITITAYSPL------GSPDRPSAKP 223
Cdd:cd19075 135 YSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLaggfltGKYKYSEDKA 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 71067102 224 ED-------------------PLLLE-IPKIKEIAAKHKRTAAQVLIR---FH 253
Cdd:cd19075 207 GGgrfdpnnalgklyrdrywkPSYFEaLEKVEEAAEKEGISLAEAALRwlyHH 259
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
16-294 |
7.51e-04 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 40.61 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 16 VGLGTW----KSPPAKVREAVKVAIDAGYRHIDCAYVYQ----------NESEVGEAIQekiqeKAVKREDLFIVSKLW- 80
Cdd:PRK10625 16 LGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLA-----KRGSREKLIIASKVSg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 81 -----------STFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQgfQSGNVFLP-----TDDKGSIlsskyTFLDAWEA 144
Cdd:PRK10625 91 psrnndkgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQ--RPTNCFGKlgyswTDSAPAV-----SLLETLDA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 145 MEELVDQGLVKALGVSNFNHFQIERLLNKPGlKH---KPVTNQvecHPYLTQEK-----LIQYCHSKGITITAYSPLG-- 214
Cdd:PRK10625 164 LAEQQRAGKIRYIGVSNETAFGVMRYLHLAE-KHdlpRIVTIQ---NPYSLLNRsfevgLAEVSQYEGVELLAYSCLAfg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 215 ---SPDRPSAKPEDP---------------LLLEIPKIKEIAAKHKRTAAQVLIRFHIERNVV--VIPKSVTPSRIQENI 274
Cdd:PRK10625 240 tltGKYLNGAKPAGArntlfsrftrysgeqTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNI 319
|
330 340
....*....|....*....|
gi 71067102 275 QVFDFQLSEEDMAAILSFNR 294
Cdd:PRK10625 320 ESLHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
9-213 |
7.04e-03 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 37.83 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 9 TGAKMPIVGLGTWKSPPAKVREA-----VKVAIDAGYRHIDCAYVYQN---ESEVGeAIqekIQEKAVKREDLFIVSKL- 79
Cdd:cd19142 9 SGLRVSNVGLGTWSTFSTAISEEqaeeiVTLAYENGINYFDTSDAFTSgqaETELG-RI---LKKKGWKRSSYIVSTKIy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 80 WSTF-FEKSLVKKafqntlsdlkldyldlyliHWPQGFQSGNVFLPTDDKGSILSSKytfLDAWEAMEE-------LVDQ 151
Cdd:cd19142 85 WSYGsEERGLSRK-------------------HIIESVRASLRRLQLDYIDIVIIHK---ADPMCPMEEvvramsyLIDN 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71067102 152 GLVKALGVSNFNH------FQIERLLNKPglkhKPVTNQVECHPyLTQEKLIQYC----HSKGITITAYSPL 213
Cdd:cd19142 143 GLIMYWGTSRWSPveimeaFSIARQFNCP----TPICEQSEYHM-FCREKMELYMpelyNKVGVGLITWSPL 209
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
15-279 |
8.86e-03 |
|
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: 37.20 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 15 IVGLGTW-----KSPPAKVREAVKVAIDAGYRHIDCAYVYQN---ESEVGEAIQEKIQEKAV-------KREDLFIVSKL 79
Cdd:cd19152 4 GFGTAPLgnlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRELGREDYVistkvgrLLVPLQEVEPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 80 WSTFFEKSL------------VKKAFQNTLSDLKLDYLDLYLIHWPqgfqsgnvflptDDKGSILSSKYTF----LDAWE 143
Cdd:cd19152 84 FEPGFWNPLpfdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDP------------DEDLAGAESDEHFaqaiKGAFR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 144 AMEELVDQGLVKALGV--------------SNFNHFQIER---LLNKPGLKhkpvtnqvechpyltqeKLIQYCHSKGIT 206
Cdd:cd19152 152 ALEELREEGVIKAIGLgvndwevilrileeADLDWVMLAGrytLLDHSAAR-----------------ELLPECEKRGVK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71067102 207 ITAYSPLGS--------PDRPSAKPEDPLLLE-IPKIKEIAAKHKRTAAQVLIRFHIERNVV--VIPKSVTPSRIQENIQ 275
Cdd:cd19152 215 VVNAGPFNSgflaggdnFDYYEYGPAPPELIArRDRIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVA 294
|
....
gi 71067102 276 VFDF 279
Cdd:cd19152 295 LLAT 298
|
|
| |
