|
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: 655.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 10 KAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLV 89
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 90 RKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIER 169
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 170 LLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTTAQVL 249
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538612546 250 IRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDFKEFSHLEDFPFDAEY 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 |
1.94e-164 |
|
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: 459.54 E-value: 1.94e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 7 LSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQE-KAVMREDLFIVSKVWPTFFE 85
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPgKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 86 RPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHF 165
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 166 QIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTT 245
Cdd:cd19106 161 QIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1538612546 246 AQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAF 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 |
3.05e-151 |
|
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: 426.30 E-value: 3.05e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRK 91
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 92 AFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLL 171
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 172 NKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrpwAKPEDPSLLEDPKIKEIAAKHKKTTAQVLIR 251
Cdd:cd19110 163 NKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG------GSCEGVDLIDDPVIQRIAKKHGKSPAQILIR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1538612546 252 FHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDFKEFSHLEDFPFDAEY 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) ... |
3-301 |
1.10e-140 |
|
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: 399.30 E-value: 1.10e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 3 TFVELSTKAKMPIVGLGTWRS---LLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKV 79
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPeevPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGV 159
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 160 SNFNHFQIERLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP-DRPWAKPEDPSLLEDPKIKEIA 238
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538612546 239 AKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDF 301
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-289 |
1.57e-136 |
|
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: 386.84 E-value: 1.57e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 13 MPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIqekaVMREDLFIVSKVWPTFFERPLVRKA 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 93 FEKTLKDLKLSYLDVYLIHWPQGFKTGDDffpkddkgnmisgKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEGGS-------------KEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 173 KPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAKHKKTTAQVLIRF 252
Cdd:cd19071 144 AA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP--------LLDDPVLKEIAKKYGKTPAQVLLRW 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 1538612546 253 HIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 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 ... |
13-312 |
3.41e-132 |
|
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: 377.99 E-value: 3.41e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 13 MPIVGLGTWRSL----LGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPL 88
Cdd:cd19109 4 IPIIGLGTYSEPkttpKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHPPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 89 VRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIE 168
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRRQLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 169 RLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP-DRPWAKPEDPSLLEDPKIKEIAAKHKKTTAQ 247
Cdd:cd19109 164 LILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNKTAAQ 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1538612546 248 VLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDFKEFSHLEDFPF 312
Cdd:cd19109 244 VVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
12-299 |
6.73e-130 |
|
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: 371.61 E-value: 6.73e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWRSLL-GKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVR 90
Cdd:cd19116 10 EIPAIALGTWKLKDdEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHEREQVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 91 KAFEKTLKDLKLSYLDVYLIHWPQGFK-TGDDFFPKDDKGNMISgkgtFLDAWEAMEELVDEGLVKALGVSNFNHFQIER 169
Cdd:cd19116 90 PALRESLKRLGLDYVDLYLIHWPVAFKeNNDSESNGDGSLSDID----YLETWRGMEDLVKLGLTRSIGVSNFNSEQINR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 170 LLNkpGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSlLEDPKIKEIAAKHKKTTAQVL 249
Cdd:cd19116 166 LLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPR-LDDPTLVAIAKKYGKTTAQIV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1538612546 250 IRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAF 299
Cdd:cd19116 243 LRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-299 |
2.56e-126 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 361.29 E-value: 2.56e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 11 AKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFFERPLVR 90
Cdd:COG0656 3 VEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS----GVPREELFVTTKVWNDNHGYDDTL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 91 KAFEKTLKDLKLSYLDVYLIHWPqgfktgddffpkddkgnmisGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERL 170
Cdd:COG0656 79 AAFEESLERLGLDYLDLYLIHWP--------------------GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 171 LNKPGlkYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAKHKKTTAQVLI 250
Cdd:COG0656 139 LAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQVVL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1538612546 251 RFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAF 299
Cdd:COG0656 207 RWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLG 255
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-299 |
1.82e-122 |
|
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: 352.87 E-value: 1.82e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 1 MATFvELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVW 80
Cdd:cd19123 1 MKTL-PLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 81 PTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGdDFFPKdDKGNMISGKGTFL-DAWEAMEELVDEGLVKALGV 159
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPE-SGEDLLSLSPIPLeDTWRAMEELVDKGLCRHIGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 160 SNFNHFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWA-KPED-PSLLEDPKIKEI 237
Cdd:cd19123 158 SNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAmKAEGePVLLEDPVINKI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1538612546 238 AAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAF 299
Cdd:cd19123 236 AEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-301 |
3.08e-119 |
|
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: 345.17 E-value: 3.08e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 2 ATFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWP 81
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 82 TFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSN 161
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 162 FNHFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPED-----PSLLEDPKIKE 236
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspaPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1538612546 237 IAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDF 301
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLFLF 303
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
3-309 |
1.46e-116 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 337.78 E-value: 1.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 3 TFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPT 82
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 83 FFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDK-GNMISGkgtfldAWEAMEELVDEGLVKALGVSN 161
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEEVlPPDIPS------TWKAMEKLVDSGKVRAIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 162 FNHFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEdpsLLEDPKIKEIAAKH 241
Cdd:cd19125 155 FSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538612546 242 KKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEematilsfnrnwrafDFKEFSHLED 309
Cdd:cd19125 230 GKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEE---------------DFAKFSSIEQ 282
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-301 |
5.34e-103 |
|
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: 304.06 E-value: 5.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 4 FVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTF 83
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKT-GDDFFPKDDKGNMISGKGT-FLDAWEAMEELVDEGLVKALGVSN 161
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSkEDDSGKLDPTGEHKQDYTTdLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 162 FNHFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKP-------EDPSLLEDPKI 234
Cdd:cd19155 163 FNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538612546 235 KEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDF 301
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGRTF 307
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-301 |
8.21e-102 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 300.18 E-value: 8.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRK 91
Cdd:cd19111 3 PMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDTEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 92 AFEKTLKDLKLSYLDVYLIHWPQGFKTgddffpKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLL 171
Cdd:cd19111 83 SLEKSLENLKLPYVDLYLIHHPCGFVN------KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 172 NKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRP--WAKPEDPSLLEDPKIKEIAAKHKKTTAQVL 249
Cdd:cd19111 157 AYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPAQVL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1538612546 250 IRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDF 301
Cdd:cd19111 235 LRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFDF 286
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-289 |
1.69e-100 |
|
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: 296.63 E-value: 1.69e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 7 LSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEK-AVMREDLFIVSKVWPTFFE 85
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEpGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 86 RPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDD----FFPKDDKGNM-ISGKGTFLDAWEAMEELVDEGLVKALGVS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDlnplTAVPTNGGEVdLDLSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 161 NFNHFQIERLLNKPGLkyKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwAKPEDPSLLEDPKIKEIAAK 240
Cdd:cd19118 161 NFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-----NLAGLPLLVQHPEVKAIAAK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1538612546 241 HKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDfkLSDEEMATI 289
Cdd:cd19118 234 LGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAV 280
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-289 |
1.53e-97 |
|
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: 289.40 E-value: 1.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 7 LSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFFER 86
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDS----GVPREEIFITTKLWCTWHRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 87 PlvRKAFEKTLKDLKLSYLDVYLIHWPQGFKT-GDDFFPKDDKGNMISGKG-TFLDAWEAMEELVDEGLVKALGVSNFNH 164
Cdd:cd19117 84 V--EEALDQSLKKLGLDYVDLYLMHWPVPLDPdGNDFLFKKDDGTKDHEPDwDFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 165 FQIERLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAKHKKT 244
Cdd:cd19117 162 KNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGKT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1538612546 245 TAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDfkLSDEEMATI 289
Cdd:cd19117 234 PAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEI 276
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-291 |
2.13e-97 |
|
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: 287.99 E-value: 2.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 13 MPIVGLGTWRslLGKVKEAVKV---AIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLV 89
Cdd:cd19136 1 MPILGLGTFR--LRGEEEVRQAvdaALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 90 RKAFEKTLKDLKLSYLDVYLIHWP--QGFKTgddffpkDDKGNMISGKGTfldaWEAMEELVDEGLVKALGVSNFNHFQI 167
Cdd:cd19136 79 RAACLGSLERLGTDYLDLYLIHWPgvQGLKP-------SDPRNAELRRES----WRALEDLYKEGKLRAIGVSNYTVRHL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 168 ERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedPSLLEDPKIKEIAAKHKKTTAQ 247
Cdd:cd19136 148 EELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD--------LRLLEDPTVLAIAKKYGRTPAQ 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1538612546 248 VLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILS 291
Cdd:cd19136 218 VLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-289 |
3.15e-95 |
|
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: 283.26 E-value: 3.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 14 PIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRKAF 93
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 94 EKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLLNK 173
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 174 pgLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKpedpSLLEDPKIKEIAAKHKKTTAQVLIRFH 253
Cdd:cd19128 162 --CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNL----TFLNDSELKALATKYNTTPPQVIIAWH 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 1538612546 254 IQR---NVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19128 236 LQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-297 |
1.13e-90 |
|
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: 271.19 E-value: 1.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 4 FVELSTKAKMPIVGLGTWRSLLGK-VKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIqekaVMREDLFIVSKVWPT 82
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESG----IPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 83 --FFERPLvrKAFEKTLKDLKLSYLDVYLIHWPqgfktgddffpkddkgnmisGKGTFLDAWEAMEELVDEGLVKALGVS 160
Cdd:cd19157 77 dqGYDSTL--KAFEASLERLGLDYLDLYLIHWP--------------------VKGKYKETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 161 NFNHFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAK 240
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEK 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1538612546 241 HKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWR 297
Cdd:cd19157 203 YNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLR 259
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-289 |
1.58e-90 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 269.91 E-value: 1.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 13 MPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFFERPLVRKA 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 93 FEKTLKDLKLSYLDVYLIHWPQgfktgddffPKDDKGNMIsgkgtfldawEAMEELVDEGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN---------PTVPLEETL----------GALKELKEAGKVKSIGVSNFTIELLEEALD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 173 KPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLgspdrpwAKPEdpsLLEDPKIKEIAAKHKKTTAQVLIRF 252
Cdd:cd19073 138 ISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-------ARGE---VLRDPVIQEIAEKYDKTPAQVALRW 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 1538612546 253 HIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19073 206 LVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
5-297 |
2.26e-90 |
|
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: 271.67 E-value: 2.26e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTff 84
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFK-TG---DDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVS 160
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKhTGvgtTGSALGEDGVLDIDVTISLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 161 NFNHFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLG--SPDRPWAKPEDPslLEDPKIKEIA 238
Cdd:cd19112 161 NYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWFGSVSP--LDDPVLKDLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1538612546 239 AKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWR 297
Cdd:cd19112 237 KKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-292 |
1.12e-89 |
|
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: 268.42 E-value: 1.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 4 FVELSTKAKMPIVGLGTWRSLlGKVKEAVKVAI-DAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPT 82
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSG-GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIKES----GVPREDLFLTTKLWPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 83 FFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDdffpkddkgnmiSGKGTFLDAWEAMEELVDEGLVKALGVSNF 162
Cdd:cd19135 79 DYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGK------------NVKETRAETWRALEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 163 NHFQIERLLNKPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrPWakpedpSLLEDPKIKEIAAKHK 242
Cdd:cd19135 147 LIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA----KG------KALEEPTVTELAKKYQ 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1538612546 243 KTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSF 292
Cdd:cd19135 215 KTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-289 |
1.20e-88 |
|
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: 265.39 E-value: 1.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFF 84
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRAS----GVPREELFITTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPQgfktgddffPKDDKgnmisgkgtFLDAWEAMEELVDEGLVKALGVSNFNH 164
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWPV---------PAQDK---------YVETWKALIELKKEGRVKSIGVSNFTI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 165 FQIERLLNKPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPdrpwakpedpSLLEDPKIKEIAAKHKKT 244
Cdd:cd19131 140 EHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQG----------GLLSDPVIGEIAEKHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1538612546 245 TAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19131 208 PAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAI 252
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-293 |
1.78e-88 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 265.21 E-value: 1.78e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTWR-SLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIqekaVMREDLFIVSKVWPTF 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSG----IPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGfktgddffpkDDKGnmisgkgtfldAWEAMEELVDEGLVKALGVSNFN 163
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG----------DVYG-----------AWRAMEELYKEGKIRAIGVSNFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 164 HFQIERLLnkPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSpdrpwakpEDPSLLEDPKIKEIAAKHKK 243
Cdd:cd19133 136 PDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE--------GRNNLFENPVLTEIAEKYGK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1538612546 244 TTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFN 293
Cdd:cd19133 206 SVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
2-286 |
6.90e-88 |
|
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: 264.39 E-value: 6.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 2 ATFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIqEKAVMREDLFIVSKVWP 81
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 82 TFFERPlvRKAFEKTLKDLKLSYLDVYLIHWPQGFKT--GDDFFPK--DDKGNMISGKgTFLDAWEAMEELVDEGLVKAL 157
Cdd:cd19121 80 TYHRRV--ELCLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTlpDGSRDLDWDW-NHVDTWKQMEKVLKTGKTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 158 GVSNFNHFQIERLLnkPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKEI 237
Cdd:cd19121 157 GVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1538612546 238 AAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFklSDEEM 286
Cdd:cd19121 227 AKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDM 273
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-293 |
5.22e-87 |
|
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: 261.22 E-value: 5.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTWRSLLG-KVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTF 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRES----GVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 FERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfktgddffpkddkgnmisGKGTFLDAWEAMEELVDEGLVKALGVSNFN 163
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWP--------------------GKDKFIDTWKALEKLYASGKVKAIGVSNFQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 164 HFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPdrpwakpedpSLLEDPKIKEIAAKHKK 243
Cdd:cd19126 137 EHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----------GLLSNPVLAAIGEKYGK 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1538612546 244 TTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFN 293
Cdd:cd19126 205 SAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-297 |
1.02e-86 |
|
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: 262.77 E-value: 1.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFF 84
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKtgddFFPKDDK--GNMISGKGT--------FLDAWEAMEELVDEGLV 154
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFK----FVPIEEKypPGFYCGDGDnfvyedvpILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 155 KALGVSNFNHFQIERLLNkpGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP-----DRPWAKpEDPSLL 229
Cdd:cd19113 159 KSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL-NTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538612546 230 EDPKIKEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWR 297
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-289 |
4.45e-85 |
|
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: 257.20 E-value: 4.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 11 AKMPIVGLGTWRSLLGK--VKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVM-REDLFIVSKVWPTFFERP 87
Cdd:cd19124 3 QTMPVIGMGTASDPPSPedIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAHPD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 88 LVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTG--------DDFFPKDDKGnmisgkgtfldAWEAMEELVDEGLVKALGV 159
Cdd:cd19124 83 LVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGkfsfpieeEDFLPFDIKG-----------VWEAMEECQRLGLTKAIGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 160 SNFNHFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAkpeDPSLLEDPKIKEIAA 239
Cdd:cd19124 152 SNFSCKKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWG---SNAVMESDVLKEIAA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1538612546 240 KHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19124 227 AKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKI 276
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-289 |
2.79e-84 |
|
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: 254.49 E-value: 2.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 11 AKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFFERPLVR 90
Cdd:cd19140 6 VRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAAS----GVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 91 KAFEKTLKDLKLSYLDVYLIHWPqgfktgddffpkddkgnmiSGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERL 170
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWP-------------------NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 171 LNKPGLKYkpVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrpwakpeDPSLLEDPKIKEIAAKHKKTTAQVLI 250
Cdd:cd19140 143 VELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA----------RGEVLKDPVLQEIGRKHGKTPAQVAL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1538612546 251 RFHIQR-NVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19140 211 RWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-297 |
3.67e-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: 3.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 1 MATFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVW 80
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 81 PTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDF--FP---KDDKGNMISGKGTFLDAWEAMEELVDEGLVK 155
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDPAvrYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 156 ALGVSNFNHFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGsP------DRPWAKpEDPSLL 229
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PqsflelDLPGAK-DTPPLF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538612546 230 EDPKIKEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWR 297
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
5-297 |
1.55e-83 |
|
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: 252.82 E-value: 1.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTWRSLLGKVKE-AVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPT- 82
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWNSd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 83 -FFERPLvrKAFEKTLKDLKLSYLDVYLIHWPqgfktgddffpkddkgnmisGKGTFLDAWEAMEELVDEGLVKALGVSN 161
Cdd:cd19156 77 qGYESTL--AAFEESLEKLGLDYVDLYLIHWP--------------------VKGKFKDTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 162 FNHFQIERLLNKpgLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAKH 241
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1538612546 242 KKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWR 297
Cdd:cd19156 203 GKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-294 |
2.03e-83 |
|
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: 253.57 E-value: 2.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTW--RSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPT 82
Cdd:cd19119 4 FKLNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 83 FFERplVRKAFEKTLKDLKLSYLDVYLIHWPQGFK-----TGDDFFPKDDKGN-MISGKGTFLDAWEAMEELVDEGLVKA 156
Cdd:cd19119 84 FYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKtRYAASGDHITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 157 LGVSNFNHFQIERLLNKpgLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPwakpedpsLLEDPKIKE 236
Cdd:cd19119 162 IGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLVKK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1538612546 237 IAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVfdFKLSDEEMATILSFNR 294
Cdd:cd19119 232 IAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-289 |
5.08e-82 |
|
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: 248.72 E-value: 5.08e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFFERPLVRK 91
Cdd:cd19132 6 QIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRS----GVPREELFVTTKLPGRHHGYEEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 92 AFEKTLKDLKLSYLDVYLIHWPQgfktgddffPKDDKgnmisgkgtFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLL 171
Cdd:cd19132 82 TIEESLYRLGLDYVDLYLIHWPN---------PSRDL---------YVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 172 NKPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRpwakpedpsLLEDPKIKEIAAKHKKTTAQVLIR 251
Cdd:cd19132 144 DETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPAQVVLR 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 1538612546 252 FHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19132 213 WHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAI 250
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-289 |
6.17e-80 |
|
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: 244.67 E-value: 6.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 13 MPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRKA 92
Cdd:cd19129 6 IPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERVKPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 93 FEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKG-TFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLL 171
Cdd:cd19129 86 FEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDGvTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 172 NKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRpwakpedPSLLEDPKIKEIAAKHKKTTAQVLIR 251
Cdd:cd19129 166 EAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME-------PKLLEDPVITAIARRVNKTPAQVLLA 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 1538612546 252 FHIQRNVTVIPKSMTPAHIVENiqvFDFK-LSDEEMATI 289
Cdd:cd19129 237 WAIQRGTALLTTSKTPSRIREN---FDIStLPEDAMREI 272
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-289 |
1.24e-79 |
|
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: 243.08 E-value: 1.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFF 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfkTGDDFfpkDDKgnmisgkgtfLDAWEAMEELVDEGLVKALGVSNFNH 164
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWP----VPNDF---DRT----------IQAYKALEKLLAEGRVRAIGVSNFTP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 165 FQIERLLNKPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAK--PEDPSLLEDPKIKEIAAKHK 242
Cdd:cd19127 140 EHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASgpTGPGDVLQDPTITGLAEKYG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1538612546 243 KTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19127 218 KTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-289 |
6.76e-78 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 238.67 E-value: 6.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGT---WRSLLG-----KVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTF 83
Cdd:cd19120 3 KIPAIAFGTgtaWYKSGDddiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKVSPGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 ferPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfktgddFFPKDdkgnmisGKGTFLDAWEAMEELVDEGLVKALGVSNFN 163
Cdd:cd19120 79 ---KDPREALRKSLAKLGVDYVDLYLIHSP--------FFAKE-------GGPTLAEAWAELEALKDAGLVRSIGVSNFR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 164 HFQIERLLNKPglKYKPVTNQVECHPYLT--QEKLIQYCHSKGITVTAYSPLGspdrPWAKPEDPSLleDPKIKEIAAKH 241
Cdd:cd19120 141 IEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLS----PLTRDAGGPL--DPVLEKIAEKY 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1538612546 242 KKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19120 213 GVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEI 260
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-297 |
1.24e-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: 236.69 E-value: 1.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRK 91
Cdd:cd19114 3 KMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHVRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 92 AFEKTLKDLKLSYLDVYLIHWPQGFKTGD---DFFPKDDKGNMISG---KGTFLDAWEAMEELVDEGLVKALGVSNFNHF 165
Cdd:cd19114 83 AFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaeNYPFLWKDKELKKFpleQSPMQECWREMEKLVDAGLVRNIGIANFNVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 166 QIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSP---DRPWAKPEDPSLLEDPKIKEIAAKHK 242
Cdd:cd19114 163 LILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1538612546 243 KTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWR 297
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-289 |
3.52e-71 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 221.48 E-value: 3.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 3 TFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPT 82
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA----SVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 83 FFERPlvRKAFEKTLKDLKLSYLDVYLIHWPqgfktgddfFPKDDkgnmisgkgTFLDAWEAMEELVDEGLVKALGVSNF 162
Cdd:PRK11565 81 DHKRP--REALEESLKKLQLDYVDLYLMHWP---------VPAID---------HYVEAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 163 NHFQIERLLNKPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRpwakpedpSLLEDPKIKEIAAKHK 242
Cdd:PRK11565 141 QIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK--------GVFDQKVIRDLADKYG 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1538612546 243 KTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:PRK11565 211 KTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEI 257
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
13-293 |
1.25e-68 |
|
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: 214.39 E-value: 1.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 13 MPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFFERPLVRKA 92
Cdd:cd19130 10 IPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAAS----GIPRDELFVTTKLWNDRHDGDEPAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 93 FEKTLKDLKLSYLDVYLIHWPqgfktgddffpkddkgnmISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19130 86 FAESLAKLGLDQVDLYLVHWP------------------TPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 173 KPGLKykPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPdrpwakpedpSLLEDPKIKEIAAKHKKTTAQVLIRF 252
Cdd:cd19130 148 ATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG----------KLLGDPPVGAIAAAHGKTPAQIVLRW 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1538612546 253 HIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFN 293
Cdd:cd19130 216 HLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-289 |
1.38e-68 |
|
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: 215.56 E-value: 1.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 7 LSTKAKMPIVGLGTWRS--LLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEK-AVMREDLFIVSKVWPTF 83
Cdd:cd19122 3 LNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPK-DDKGNMISGKGTFLD---AWEAMEELVDEGLVKALGV 159
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILKDLTENpepTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 160 SNFNHFQIERLLNKPglKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSllEDPKIKEIAA 239
Cdd:cd19122 163 SNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVS--ENPTLNEVAE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1538612546 240 KHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDfkLSDEEMATI 289
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAI 286
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-289 |
4.71e-67 |
|
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: 210.55 E-value: 4.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 10 KAKMPIVGLGTW------RSLLGKVKEAVKV---AIDAEYRHIDCAYFYENQH---EVGEAIqekiqeKAVMREDLFIVS 77
Cdd:cd19072 1 GEEVPVLGLGTWgigggmSKDYSDDKKAIEAlryAIELGINLIDTAEMYGGGHaeeLVGKAI------KGFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 78 KVWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPkddkgnmisgkgtFLDAWEAMEELVDEGLVKAL 157
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP------NPSIP-------------IEETLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 158 GVSNFNHFQIERLLNKPGlKYKPVTNQVECHpYLTQE---KLIQYCHSKGITVTAYSPLGSPDRPWAKPedpslleDPKI 234
Cdd:cd19072 136 GVSNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEKGKLSNAKG-------SPLL 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1538612546 235 KEIAAKHKKTTAQVLIRFHIQR-NVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 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 |
3.10e-65 |
|
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: 206.78 E-value: 3.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTWRslLG---------KVKEAVKVAIDAEYRHIDCAYFY---ENQHEVGEAIQEKiqekAVMREDLFIVSKV---- 79
Cdd:pfam00248 1 IGLGTWQ--LGggwgpiskeEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 --WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfktgddfFPKDDkgnmisgkgtFLDAWEAMEELVDEGLVKAL 157
Cdd:pfam00248 75 gpWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP---------DPDTP----------IEETWDALEELKKEGKIRAI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 158 GVSNFNHFQIERLLNKPglKYKPVTNQVECHPY--LTQEKLIQYCHSKGITVTAYSPLGS-----------------PDR 218
Cdd:pfam00248 136 GVSNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgeRRR 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538612546 219 PWAKPEDPSLLEDPKIKEIAAKHKKTTAQVLIRFHIQ--RNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:pfam00248 214 LLKKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-289 |
3.15e-65 |
|
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: 205.67 E-value: 3.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 13 MPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFFERPLVRKA 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 93 FEKTLKDLKLSYLDVYLIHWPqgfkTGDDFFPKDDkgnmisgkgtFLdawEAMEELVDEGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWP----SPNDEVPVEE----------YI---GALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 173 KPGlKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrpWAKpedpsLLEDPKIKEIAAKHKKTTAQVLIRF 252
Cdd:cd19139 140 VVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA-----YGK-----VLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 1538612546 253 HIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAI 245
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-289 |
6.76e-63 |
|
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: 200.17 E-value: 6.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTW-----RSLLGKVKEAVKVAIDAEYRHIDCAYFYEN---QHEVGEAIQEKiqekavmREDLFIV 76
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 77 SKVWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFfpkddkgnmisgkgtfldawEAMEELVDEGLVKA 156
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETV--------------------AAMEELKKEGKIRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 157 LGVSNFNHFQIERLLNKPGLKyKPVTNQVECHpyLTQE----KLIQYCHSKGITVTAYSPLGSPDRPwakpeDPSLLEDP 232
Cdd:cd19138 136 WGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLL-----RRGLLENP 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1538612546 233 KIKEIAAKHKKTTAQVLIRFHI-QRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19138 208 TLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-289 |
6.93e-62 |
|
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: 197.39 E-value: 6.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 5 VELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFF 84
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 85 ERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGfktgddffpkddkgnmisGKGTFLDAWEAMEELVDEGLVKALGVSNFNH 164
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWPAG------------------REGKYVDSWGGLMKLREEGLARSIGVSNFTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 165 FQIERLLNKPGlkYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPdrpwakpedpSLLEDPKIKEIAAKHKKT 244
Cdd:cd19134 141 EHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVG----------RLLDNPAVTAIAAAHGRT 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1538612546 245 TAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-297 |
1.97e-58 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 188.69 E-value: 1.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWRsLLGK-VKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKiqekAVMREDLFIVSKVWPTFFERPLVR 90
Cdd:PRK11172 2 SIPAFGLGTFR-LKDQvVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWIDNLAKDKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 91 KAFEKTLKDLKLSYLDVYLIHWPQgfktgddffPKDDkgnmisgkgtfLDAWEAMEELVD---EGLVKALGVSNFNHFQI 167
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHWPS---------PNDE-----------VSVEEFMQALLEakkQGLTREIGISNFTIALM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 168 ERLLNKPGlKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGspdrpWAKpedpsLLEDPKIKEIAAKHKKTTAQ 247
Cdd:PRK11172 137 KQAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA-----YGK-----VLKDPVIARIAAKHNATPAQ 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1538612546 248 VLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWR 297
Cdd:PRK11172 206 VILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-289 |
2.66e-56 |
|
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: 183.16 E-value: 2.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWR---------SLLGKVKEAVKVAIDAEYRHIDCAYFYENQHE---VGEAIqekiqeKAVMREDLFIVSKV 79
Cdd:cd19137 3 KIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGGGHTeelVGKAI------KDFPREDLFIVTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQgfktgddffPKddkgnmISGKGTFldawEAMEELVDEGLVKALGV 159
Cdd:cd19137 77 WPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPN---------PN------IPLEETL----SAMAEGVRQGLIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 160 SNFNHFQIERLLNKpgLKYKPVTNQVECHPY---LTQEKLIQYCHSKGITVTAYSPLgspDRPWAKPEDpslledpKIKE 236
Cdd:cd19137 138 SNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL---RRGLEKTNR-------TLEE 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1538612546 237 IAAKHKKTTAQVLIRFHIQR-NVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19137 206 IAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-287 |
4.17e-47 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 160.09 E-value: 4.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTW----RSLLGK-------VKEAVKVAIDAEYRHIDCAYFYENQHE---VGEAIQEKIQekavmREDLFIVS 77
Cdd:cd19093 1 EVSPLGLGTWqwgdRLWWGYgeygdedLQAAFDAALEAGVNLFDTAEVYGTGRSerlLGRFLKELGD-----RDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 78 KVWPTF--FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFpkddkgnmisgkgtfldaWEAMEELVDEGLVK 155
Cdd:cd19093 76 KFAPLPwrLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 156 ALGVSNFNHFQIER---LLNKPGlkYKPVTNQVE---CHPYLTQEKLIQYCHSKGITVTAYSPLG--------SPDRP-- 219
Cdd:cd19093 138 AVGVSNYSADQLRRahkALKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPpp 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538612546 220 ---------WAKPEDPSLLEdpKIKEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMA 287
Cdd:cd19093 216 ggrrrlfgrKNLEKVQPLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVA 290
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
16-289 |
1.67e-44 |
|
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: 154.18 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTWR--SLLGKV--KEAVKV---AIDAEYRHIDCAYFY---ENQHEVGEAIqekiqeKAVMREDLFIVSKVWPTFFE 85
Cdd:COG0667 16 LGLGTMTfgGPWGGVdeAEAIAIldaALDAGINFFDTADVYgpgRSEELLGEAL------KGRPRDDVVIATKVGRRMGP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 86 RPL--------VRKAFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPKDDkgnmisgkgtfldAWEAMEELVDEGLVKAL 157
Cdd:COG0667 90 GPNgrglsrehIRRAVEASLRRLGTDYIDLYQLHRP------DPDTPIEE-------------TLGALDELVREGKIRYI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 158 GVSNFNHFQIERLLNKPGLKYKPVTNQVEchpY--LTQ---EKLIQYCHSKGITVTAYSPLGS---------------PD 217
Cdd:COG0667 151 GVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAYSPLAGglltgkyrrgatfpeGD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 218 R-------PWAKPEDPSLLEdpKIKEIAAKHKKTTAQVLIRFHIQR--NVTVIPKSMTPAHIVENIQVFDFKLSDEEMAT 288
Cdd:COG0667 228 RaatnfvqGYLTERNLALVD--ALRAIAAEHGVTPAQLALAWLLAQpgVTSVIPGARSPEQLEENLAAADLELSAEDLAA 305
|
.
gi 1538612546 289 I 289
Cdd:COG0667 306 L 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-289 |
1.65e-41 |
|
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: 145.42 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 14 PIVGLGTW----RSLLGKVKE-----AVKVAIDAEYRHIDCAYFYENQHE---VGEAIQEKiqekavmREDLFIVSKVWP 81
Cdd:cd19085 2 SRLGLGCWqfggGYWWGDQDDeesiaTIHAALDAGINFFDTAEAYGDGHSeevLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 82 TFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfKTGDDFFPkddkgnmisgkgTFldawEAMEELVDEGLVKALGVSN 161
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP---SSDVPLEE------------TM----EALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 162 FNHFQIERLLnKPGlkyKPVTNQVECHPYLTQ-EK-LIQYCHSKGITVTAYSPL------GSPDRPWAKPED------PS 227
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQLPYNLLWRAiEYeILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlFR 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1538612546 228 LLEDP----------KIKEIAAKHKKTTAQVLIRFHIQRN--VTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19085 212 HFEPGaeeetfealeKLKEIADELGVTMAQLALAWVLQQPgvTSVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
12-289 |
1.22e-38 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 138.04 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWrSLLGK---------VKEAVKVAIDAEYRHIDCAYFYENQH---EVGEAIQEKiqekavmREDLFIVSKV 79
Cdd:cd19084 3 KVSRIGLGTW-AIGGTwwgevddqeSIEAIKAAIDLGINFFDTAPVYGFGHseeILGKALKGR-------RDDVVIATKC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 ---W--PTFFERPL----VRKAFEKTLKDLKLSYLDVYLIHWPQGfKTgddffPKDDkgnmisgkgtfldAWEAMEELVD 150
Cdd:cd19084 75 glrWdgGKGVTKDLspesIRKEVEQSLRRLQTDYIDLYQIHWPDP-NT-----PIEE-------------TAEALEKLKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 151 EGLVKALGVSNFNHFQIERLlnkpgLKY-KPVTNQVechPY--LTQ---EKLIQYCHSKGITVTAYSPLG---------- 214
Cdd:cd19084 136 EGKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAqglltgkykk 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 215 ----SPD---------RPWAKPEDPSLLEdpKIKEIAAKHKKTTAQVLIRFHIQRN--VTVIPKSMTPAHIVENIQVFDF 279
Cdd:cd19084 208 eptfPPDdrrsrfpffRGENFEKNLEIVD--KLKEIAEKYGKSLAQLAIAWTLAQPgvTSAIVGAKNPEQLEENAGALDW 285
|
330
....*....|
gi 1538612546 280 KLSDEEMATI 289
Cdd:cd19084 286 ELTEEELKEI 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-275 |
7.40e-33 |
|
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: 121.09 E-value: 7.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTWR-SLLGKVKEAVKV---AIDAEYRHIDCAYFY---ENQHEVGEAIQEKiqekaVMREDLFIVSKVWPTFFERPL 88
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAFALldaALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPGGDPS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 89 --------VRKAFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPKDdkgnmisgkgtflDAWEAMEELVDEGLVKALGVS 160
Cdd:cd06660 78 rsrlspehIRRDLEESLRRLGTDYIDLYYLHRD------DPSTPVE-------------ETLEALNELVREGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 161 NFNHFQIERLLN--KPGLKYKPVTNQVE---CHPYLTQEKLIQYCHSKGITVTAYSPLGS-Pdrpwakpedpslledpki 234
Cdd:cd06660 139 NWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARgP------------------ 200
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1538612546 235 keiaakhkkttAQVLIRFHIQR--NVTVIPKSMTPAHIVENIQ 275
Cdd:cd06660 201 -----------AQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
16-285 |
2.01e-30 |
|
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: 116.12 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTWRSL-----LGKVKEAVKVAIDAEYRHIDCAYFYENqHEVGEAIQEKIQEKAVMREDLFIVSK--VWPTFFERPL 88
Cdd:cd19092 9 LVLGCMRLAdwgesAEELLSLIEAALELGITTFDHADIYGG-GKCEELFGEALALNPGLREKIEIQTKcgIRLGDDPRPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 89 -----------VRKAFEKTLKDLKLSYLDVYLIHWPqgfktgddffpkdDkgnmisgkgTFLDAWE---AMEELVDEGLV 154
Cdd:cd19092 88 rikhydtskehILASVEGSLKRLGTDYLDLLLLHRP-------------D---------PLMDPEEvaeAFDELVKSGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 155 KALGVSNFNHFQIErLLNKpGLKYKPVTNQVEC---HPYLTQEKLIQYCHSKGITVTAYSPLG-----SPDRpwakPEDP 226
Cdd:cd19092 146 RYFGVSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGggrlfGGFD----ERFQ 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1538612546 227 SLLEdpKIKEIAAKHKKTTAQVLIRF---HIQRNVTVIpKSMTPAHIVENIQVFDFKLSDEE 285
Cdd:cd19092 220 RLRA--ALEELAEEYGVTIEAIALAWllrHPARIQPIL-GTTNPERIRSAVKALDIELTREE 278
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
14-285 |
3.19e-30 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 116.02 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 14 PIVgLGTWRsLLGK---VKEAVKV---AIDAEYRHIDCA--Y-FYENQHEVGEAIQEKiqekAVMREDLFIVSK-----V 79
Cdd:COG4989 15 RIV-LGCMR-LGEWdlsPAEAAALieaALELGITTFDHAdiYgGYTCEALFGEALKLS----PSLREKIELQTKcgirlP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 WPTFFERPL--------VRKAFEKTLKDLKLSYLDVYLIHWPqgfktgddffpkdDkgnmisgkgTFLDAWE---AMEEL 148
Cdd:COG4989 89 SEARDNRVKhydtskehIIASVEGSLRRLGTDYLDLLLLHRP-------------D---------PLMDPEEvaeAFDEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 149 VDEGLVKALGVSNFNHFQIErLLNKpGLKYKPVTNQVECHPYLTQ---EKLIQYCHSKGITVTAYSPLGSPDrpWAKPED 225
Cdd:COG4989 147 KASGKVRHFGVSNFTPSQFE-LLQS-ALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWSPLAGGR--LFGGFD 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1538612546 226 PSLLE-DPKIKEIAAKHKKTTAQVLIRFhIQR---NVTVIPKSMTPAHIVENIQVFDFKLSDEE 285
Cdd:COG4989 223 EQFPRlRAALDELAEKYGVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-289 |
4.24e-30 |
|
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: 115.85 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTW-----------------RSLlgkvkEAVKVAIDAEYRHIDCAYFYENQHE---VGEAIQEkiqekavMREDLFI 75
Cdd:cd19102 4 IGLGTWaiggggwgggwgpqddrDSI-----AAIRAALDLGINWIDTAAVYGLGHSeevVGRALKG-------LRDRPIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 76 VSKVWP---------TFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQgfktgddffPKDDkgnmisgkgtFLDAWEAME 146
Cdd:cd19102 72 ATKCGLlwdeegrirRSLKPASIRAECEASLRRLGVDVIDLYQIHWPD---------PDEP----------IEEAWGALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 147 ELVDEGLVKALGVSNFNHFQIERLlnkpgLKYKPVT-NQVechPY--LTQE---KLIQYCHSKGITVTAYSPLGS----- 215
Cdd:cd19102 133 ELKEEGKVRAIGVSNFSVDQMKRC-----QAIHPIAsLQP---PYslLRRGieaEILPFCAEHGIGVIVYSPMQSglltg 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 216 ---PDRPWAKPED-----------PSLLEDPKI----KEIAAKHKKTTAQVLIRFHIQR-NVT-VIPKSMTPAHIVENIQ 275
Cdd:cd19102 205 kmtPERVASLPADdwrrrspffqePNLARNLALvdalRPIAERHGRTVAQLAIAWVLRRpEVTsAIVGARRPDQIDETVG 284
|
330
....*....|....
gi 1538612546 276 VFDFKLSDEEMATI 289
Cdd:cd19102 285 AADLRLTPEELAEI 298
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-289 |
4.22e-27 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 108.75 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWRSLLGKVKEAVKV---AIDAEYRHIDCAYFYENQHE-VGEAIQEkiqekavMREDLFIVSKVWPTFFERP 87
Cdd:COG1453 12 EVSVLGFGGMRLPRKDEEEAEALirrAIDNGINYIDTARGYGDSEEfLGKALKG-------PRDKVILATKLPPWVRDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 88 LVRKAFEKTLKDLKLSYLDVYLIHwpqGFKTGDDFfpkddkGNMISGKGtfldAWEAMEELVDEGLVKALGVSNFNHFQ- 166
Cdd:COG1453 85 DMRKDLEESLKRLQTDYIDLYLIH---GLNTEEDL------EKVLKPGG----ALEALEKAKAEGKIRHIGFSTHGSLEv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 167 IERLLNkpglkykpvTNQVEC---------HPYLTQEKLIQYCHSKGITVTAYSPLGspdrpwakpeDPSLLEDP-KIKE 236
Cdd:COG1453 152 IKEAID---------TGDFDFvqlqynyldQDNQAGEEALEAAAEKGIGVIIMKPLK----------GGRLANPPeKLVE 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1538612546 237 IaAKHKKTTAQVLIRFHIQR-NVTVIPKSM-TPAHIVENIQVFD--FKLSDEEMATI 289
Cdd:COG1453 213 L-LCPPLSPAEWALRFLLSHpEVTTVLSGMsTPEQLDENLKTADnlEPLTEEELAIL 268
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-291 |
6.54e-27 |
|
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: 107.36 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTWR----SLLGKVKEAVKV-AIDAEYRH----IDCAYFYENQHE---VGEAIQEKiqekavmREDLFIVSK---VW 80
Cdd:cd19149 14 IGLGTWAigggPWWGGSDDNESIrTIHAALDLginlIDTAPAYGFGHSeeiVGKAIKGR-------RDKVVLATKcglRW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 81 PT-----FFERPLV-----------RKAFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPkddkgnmISgkgtflDAWEA 144
Cdd:cd19149 87 DReggsfFFVRDGVtvyknlspesiREEVEQSLKRLGTDYIDLYQTHWQ------DVETP-------IE------ETMEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 145 MEELVDEGLVKALGVSNFNHFQIERLLNKPGL-----KYKPVTNQVEchpyltqEKLIQYCHSKGITVTAYSPLGS---- 215
Cdd:cd19149 148 LEELKRQGKIRAIGASNVSVEQIKEYVKAGQLdiiqeKYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLEQgllt 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 216 ----PDR-----------PWAKPEDPS----LLEdpKIKEIAAKHKKTTAQVLIRFHIQR--NVTVIPKSMTPAHIVENI 274
Cdd:cd19149 221 gkitPDRefdagdarsgiPWFSPENREkvlaLLE--KWKPLCEKYGCTLAQLVIAWTLAQpgITSALCGARKPEQAEENA 298
|
330
....*....|....*..
gi 1538612546 275 QVFDFKLSDEEMATILS 291
Cdd:cd19149 299 KAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
29-291 |
1.22e-25 |
|
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: 103.65 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 29 KEAVKVAIDAEYRHIDCAYFYENQHE---VGEAIQEKIQEKAVM--------REDLFIVSKvwptffERPLVRKAFEKTL 97
Cdd:cd19083 36 KDLVREALDNGVNLLDTAFIYGLGRSeelVGEVLKEYNRNEVVIatkgahkfGGDGSVLNN------SPEFLRSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 98 KDLKLSYLDVYLIHWPqgfktgDDFFPKDdkgnmisgkgtflDAWEAMEELVDEGLVKALGVSNFNHFQIERlLNKPGLk 177
Cdd:cd19083 110 KRLNTDYIDLYYIHFP------DGETPKA-------------EAVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDGY- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 178 ykpvTNQVEcHPY-LTQ----EKLIQYCHSKGITVTAYSPLGS-------------PDRPWAKpeDPSLLEDP------- 232
Cdd:cd19083 169 ----VDVLQ-GEYnLLQreaeEDILPYCVENNISFIPYFPLASgllagkytkdtkfPDNDLRN--DKPLFKGErfsenld 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1538612546 233 ---KIKEIAAKHKKTTAQVLIRFHIQRNV--TVIPKSMTPAHIVENIQVFDFKLSDEEMATILS 291
Cdd:cd19083 242 kvdKLKSIADEKGVTVAHLALAWYLTRPAidVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-282 |
4.51e-25 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 101.14 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 13 MPIVGLGTW--RSLLGKVKEAVKVAIDAEYRHIDCAYFYenqhevGEAIQEKIQEKAV--MREDLFIVSKV--------- 79
Cdd:cd19088 9 MRLTGPGIWgpPADREEAIAVLRRALELGVNFIDTADSY------GPDVNERLIAEALhpYPDDVVIATKGglvrtgpgw 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPkddkgnmisgkgtFLDAWEAMEELVDEGLVKALGV 159
Cdd:cd19088 83 WGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI------DPKVP-------------FEEQLGALAELQDEGLIRHIGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 160 SNFNHFQIERLLNKPGLkykpVTNQVECHPYLTQ-EKLIQYCHSKGITVTAYSPLGSpdRPWAKPEdpslledPKIKEIA 238
Cdd:cd19088 144 SNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG--GDLAQPG-------GLLAEVA 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1538612546 239 AKHKKTTAQVLIRFHIQR--NVTVIPKSMTPAHIVENIQVFDFKLS 282
Cdd:cd19088 211 ARLGATPAQVALAWLLARspVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-276 |
1.51e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 99.58 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 9 TKAKMPIVGLGTWRsLLGKVKEAVKVAIDAEYRHIDCAYFYENQHE---VGEAIqekiqeKAVMREDLFIVSKVWPTFFE 85
Cdd:cd19105 9 TGLKVSRLGFGGGG-LPRESPELLRRALDLGINYFDTAEGYGNGNSeeiIGEAL------KGLRRDKVFLATKASPRLDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 86 RPL--VRKAFEKTLKDLKLSYLDVYLIHwpqgfktGDDfFPKDDKGNmisgkgtflDAW-EAMEELVDEGLVKALGVS-- 160
Cdd:cd19105 82 KDKaeLLKSVEESLKRLQTDYIDIYQLH-------GVD-TPEERLLN---------EELlEALEKLKKEGKVRFIGFSth 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 161 -NFNHFqIERLLNKPG-----LKYKPVtnqvecHPYLTQEKLIQYCHSKGITVTAYSPLGS-PDRPWAKPEDPSLledpk 233
Cdd:cd19105 145 dNMAEV-LQAAIESGWfdvimVAYNFL------NQPAELEEALAAAAEKGIGVVAMKTLAGgYLQPALLSVLKAK----- 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1538612546 234 ikeiaakhKKTTAQVLIRFHIQ-RNVTVIPKSM-TPAHIVENIQV 276
Cdd:cd19105 213 --------GFSLPQAALKWVLSnPRVDTVVPGMrNFAELEENLAA 249
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-276 |
2.41e-23 |
|
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: 96.01 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTWRslLG----------KVKEAVKVAIDAEYRHIDCAYFYENQH-E--VGEAIQEKiqekavmREDLFIVSKVWPT 82
Cdd:cd19086 6 IGFGTWG--LGgdwwgdvddaEAIRALRAALDLGINFFDTADVYGDGHsErlLGKALKGR-------RDKVVIATKFGNR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 83 FFERPL---------VRKAFEKTLKDLKLSYLDVYLIH-WPqgfktgDDFFPKDdkgnmisgkgtflDAWEAMEELVDEG 152
Cdd:cd19086 77 FDGGPErpqdfspeyIREAVEASLKRLGTDYIDLYQLHnPP------DEVLDND-------------ELFEALEKLKQEG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 153 LVKALGVSNFNHFQIERLLNKPGLK-----YkpvtNQVECHPYltqEKLIQYCHSKGITVTAYSPLGSpdrpwakpedpS 227
Cdd:cd19086 138 KIRAYGVSVGDPEEALAALRRGGIDvvqviY----NLLDQRPE---EELFPLAEEHGVGVIARVPLAS-----------G 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1538612546 228 LLEDpKIKEIAakhkkttaqvlIRFHIQRN--VTVIPKSMTPAHIVENIQV 276
Cdd:cd19086 200 LLTG-KLAQAA-----------LRFILSHPavSTVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-226 |
2.86e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 95.63 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 8 STKAKMPIVGLGTWRSLLGKVKEAVKV---AIDAEYRHIDCAYFYENQHE-VGEAIQEKiqekavmREDLFIVSKVWPTf 83
Cdd:cd19100 6 RTGLKVSRLGFGGGPLGRLSQEEAAAIirrALDLGINYFDTAPSYGDSEEkIGKALKGR-------RDKVFLATKTGAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 fERPLVRKAFEKTLKDLKLSYLDVYLIHwpqGFKTGDDFFPKDDKGNmisgkgtfldAWEAMEELVDEGLVKALGVSNFN 163
Cdd:cd19100 78 -DYEGAKRDLERSLKRLGTDYIDLYQLH---AVDTEEDLDQVFGPGG----------ALEALLEAKEEGKIRFIGISGHS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1538612546 164 HFQIERLLNKPglkykPV------TNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDP 226
Cdd:cd19100 144 PEVLLRALETG-----EFdvvlfpINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP 207
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
29-289 |
5.10e-23 |
|
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: 96.88 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 29 KEAVKVAIDAEYRHIDCAYFYEN---QHEVGEAIQEKIqekavMREDLFIVSKVWPTFFERP----LVRK----AFEKTL 97
Cdd:cd19079 38 RPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFPMGDGPngrgLSRKhimaEVDASL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 98 KDLKLSYLDVYLIHWPqgfktgDDFFPkddkgnmisgkgtFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLLN---KP 174
Cdd:cd19079 113 KRLGTDYIDLYQIHRW------DYETP-------------IEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHlaeKN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 175 GLKyKPVTNQvecHPY--LTQE---KLIQYCHSKGITVTAYSPL----------GSPDRPWAKPEDPSLLED-------- 231
Cdd:cd19079 174 GWT-KFVSMQ---NHYnlLYREeerEMIPLCEEEGIGVIPWSPLargrlarpwgDTTERRRSTTDTAKLKYDyfteadke 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1538612546 232 --PKIKEIAAKHKKTTAQVLIRFHIQRNVTVIP--KSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19079 250 ivDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
16-284 |
9.87e-20 |
|
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: 87.26 E-value: 9.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTWRSLLGKV-----KEAVKVAIDAEYRHIDCAYFYEN---QHEVGEAIQEkiqekaVMREDLFIVSKV-WPT---F 83
Cdd:cd19074 7 LSLGTWLTFGGQVddedaKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfWPTgpgP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 FERPLVRK----AFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPKDDkgnmisgkgTFldawEAMEELVDEGLVKALGV 159
Cdd:cd19074 81 NDRGLSRKhifeSIHASLKRLQLDYVDIYYCHRY------DPETPLEE---------TV----RAMDDLIRQGKILYWGT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 160 SNFNHFQIE---RLLNKPGLkYKPVTNQVECHpYLTQEK---LIQYCHSKGITVTAYSPLGS-------------PDRPW 220
Cdd:cd19074 142 SEWSAEQIAeahDLARQFGL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQglltgkyrdgippPSRSR 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538612546 221 AKPEDP-----SLLEDP------KIKEIAAKHKKTTAQVLIRFHIQR-NVT-VIPKSMTPAHIVENIQVFDFKLSDE 284
Cdd:cd19074 220 ATDEDNrdkkrRLLTDEnlekvkKLKPIADELGLTLAQLALAWCLRNpAVSsAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-276 |
1.18e-19 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 86.13 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 14 PIVGLGTWRSL-------LGKVKEAVKVAIDAEYRHIDCAYFYENQHEV-GEAIQEKIqekavmREDLFIVSKVWPTF-- 83
Cdd:cd19095 1 SVLGLGTSGIGrvwgvpsEAEAARLLNTALDLGINLIDTAPAYGRSEERlGRALAGLR------RDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 ------FERPLVRKAFEKTLKDLKLSYLDVYLIHWPQgfktgddffPKDDKGNMIsgkgtfldawEAMEELVDEGLVKAL 157
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGPS---------DDELTGEVL----------ETLEDLKAAGKVRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 158 GVSNFNHfQIERLLNKPGLKykpvTNQVechPY----LTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPK 233
Cdd:cd19095 136 GVSGDGE-ELEAAIASGVFD----VVQL---PYnvldREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYAR 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1538612546 234 IKEIAAKHK-KTTAQVLIRFHIQ--RNVTVIPKSMTPAHIVENIQV 276
Cdd:cd19095 208 RPEFAAEIGgATWAQAALRFVLShpGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-284 |
6.02e-19 |
|
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: 84.91 E-value: 6.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 14 PIVGLGTwrSLLGKVK---------EAVKVAIDAEYRHIDCAYFY-ENQHEVGEAIQEkiqekaVMREDLFIVSKV---- 79
Cdd:cd19090 1 SALGLGT--AGLGGVFggvdddeavATIRAALDLGINYIDTAPAYgDSEERLGLALAE------LPREPLVLSTKVgrlp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 -WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPkddkgnmisgKGTFldawEAMEELVDEGLVKALG 158
Cdd:cd19090 73 eDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP----------GGAL----EALLELKEEGLIKHIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 159 VSNFNHFQIERLLNkpglkykpvTNQVEC----HPY--LTQE---KLIQYCHSKGITVTAYSPLGS-------PDRPWAK 222
Cdd:cd19090 139 LGGGPPDLLRRAIE---------TGDFDVvltaNRYtlLDQSaadELLPAAARHGVGVINASPLGMgllagrpPERVRYT 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538612546 223 PEDPSLLEDP---KIKEIAAKHKKTTAQVLIRFHIQ--RNVTVIPKSMTPAHIVENIQVFDFKLSDE 284
Cdd:cd19090 210 YRWLSPELLDrakRLYELCDEHGVPLPALALRFLLRdpRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
27-278 |
6.09e-19 |
|
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: 84.54 E-value: 6.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 27 KVKEAVKVAIDAEYRHIDCAYFYENQH-E--VGEAIqekiqeKAVMREDLFIVSKVWPTFFERPL-VRKAFEKTLKDLKL 102
Cdd:cd19096 22 KAIEMIRYAIDAGINYFDTAYGYGGGKsEeiLGEAL------KEGPREKFYLATKLPPWSVKSAEdFRRILEESLKRLGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 103 SYLDVYLIHWPQgfktGDDFFPKDDKGnmisgkgtflDAWEAMEELVDEGLVKALGVSnfnhF-----QIERLLNkpglk 177
Cdd:cd19096 96 DYIDFYLLHGLN----SPEWLEKARKG----------GLLEFLEKAKKEGLIRHIGFS----FhdspeLLKEILD----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 178 ykpvTNQVEC----HPYLTQE-----KLIQYCHSKGITVTAYSPL--GspdrpwAKPEDPslledPKIKEIAAKHKKTTA 246
Cdd:cd19096 153 ----SYDFDFvqlqYNYLDQEnqagrPGIEYAAKKGMGVIIMEPLkgG------GLANNP-----PEALAILCGAPLSPA 217
|
250 260 270
....*....|....*....|....*....|....
gi 1538612546 247 QVLIRFHI-QRNVTVIPKSM-TPAHIVENIQVFD 278
Cdd:cd19096 218 EWALRFLLsHPEVTTVLSGMsTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-289 |
1.50e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 83.92 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWR-------------SLLGK--VKEAVKVAIDAEYRHIDCAYFYenqhevGEAIQEKIQE---KAVMREDL 73
Cdd:cd19103 3 KLPKIALGTWSwgsggaggdqvfgNHLDEdtLKAVFDKAMAAGLNLWDTAAVY------GMGASEKILGeflKRYPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 74 FIVSKVWPTF---FERPlVRKAFEKTLKDLKLSYLDVYLIHwpqgfktgddfFPKDDKGNMisgkgtfldawEAMEELVD 150
Cdd:cd19103 77 IISTKFTPQIagqSADP-VADMLEGSLARLGTDYIDIYWIH-----------NPADVERWT-----------PELIPLLK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 151 EGLVKALGVSNFNHFQIER---LLNKPGLKYKPVTNqvecH---PYLTQEK--LIQYCHSKGITVTAYSPL------GSP 216
Cdd:cd19103 134 SGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQN----HyslLYRSSEEagILDYCKENGITFFAYMVLeqgalsGKY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 217 DRPWAKPEDPSLLED-----PKI-------KEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDE 284
Cdd:cd19103 210 DTKHPLPEGSGRAETynpllPQLeeltavmAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDD 289
|
....*
gi 1538612546 285 EMATI 289
Cdd:cd19103 290 EIKEL 294
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-275 |
2.14e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 83.91 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTWRSLLGK-----VKEAVKVAIDAEYRHIDCAYFYENQH---EVGEAIQEKIQEKAVMREDLFIVSKV-------- 79
Cdd:cd19099 6 LGLGTYRGDSDDetdeeYREALKAALDSGINVIDTAINYRGGRserLIGKALRELIEKGGIKRDEVVIVTKAgyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 ----WPTFFERPLVRK---------------------AFEKTLKDLKLSYLDVYLIHWPQGfktgddFFPKDDKGNMISg 134
Cdd:cd19099 86 eplrPLKYLEEKLGRGlidvadsaglrhcispayledQIERSLKRLGLDTIDLYLLHNPEE------QLLELGEEEFYD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 135 kgTFLDAWEAMEELVDEGLVKALGVSNFN----------HFQIERLL--------NKPGLKYkpVtnQVECHPYLTQ--- 193
Cdd:cd19099 159 --RLEEAFEALEEAVAEGKIRYYGISTWDgfrappalpgHLSLEKLVaaaeevggDNHHFKV--I--QLPLNLLEPEalt 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 194 ---------EKLIQYCHSKGITVTAYSPL--GSPDRPWAKPEDPSLLEDpkikeiaakhkKTTAQVLIRF-HIQRNV-TV 260
Cdd:cd19099 233 ekntvkgeaLSLLEAAKELGLGVIASRPLnqGQLLGELRLADLLALPGG-----------ATLAQRALQFaRSTPGVdSA 301
|
330
....*....|....*
gi 1538612546 261 IPKSMTPAHIVENIQ 275
Cdd:cd19099 302 LVGMRRPEHVDENLA 316
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
35-289 |
2.75e-18 |
|
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: 83.42 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 35 AIDAEYRHIDCAYFY---ENQHEVGEAIQEKiqekavmREDLFIVSK---VWPTFFE------RP-LVRKAFEKTLKDLK 101
Cdd:cd19076 41 ALELGVTFLDTADMYgpgTNEELLGKALKDR-------RDEVVIATKfgiVRDPGSGfrgvdgRPeYVRAACEASLKRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 102 LSYLDVYLIHWPqgfktgDDFFPKDDkgnmisgkgtfldAWEAMEELVDEGLVKALGVSNFNHFQIERllnkpGLKYKPV 181
Cdd:cd19076 114 TDVIDLYYQHRV------DPNVPIEE-------------TVGAMAELVEEGKVRYIGLSEASADTIRR-----AHAVHPI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 182 TN-QVECHPYLT--QEKLIQYCHSKGITVTAYSPL------GSPDRPWAKPEDPSLLEDP---------------KIKEI 237
Cdd:cd19076 170 TAvQSEYSLWTRdiEDEVLPTCRELGIGFVAYSPLgrgfltGAIKSPEDLPEDDFRRNNPrfqgenfdknlklveKLEAI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1538612546 238 AAKHKKTTAQVLIRFHIQR--NVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19076 250 AAEKGCTPAQLALAWVLAQgdDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
16-289 |
2.81e-18 |
|
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: 83.51 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 16 VGLGTWR---SLLG--KVKEAVKV---AIDAEYRHIDCAYFY---ENQHEVGEAIQEKIQekavmREDLFIVSKVWPTFF 84
Cdd:cd19148 7 IALGTWAiggWMWGgtDEKEAIETihkALDLGINLIDTAPVYgfgLSEEIVGKALKEYGK-----RDRVVIATKVGLEWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 85 ERPLV---------RKAFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPkddkgnmisgkgtFLDAWEAMEELVDEGLVK 155
Cdd:cd19148 82 EGGEVvrnsspariRKEVEDSLRRLQTDYIDLYQVHWP------DPLVP-------------IEETAEALKELLDEGKIR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 156 ALGVSNFNHFQIERLlnkpgLKYKPV-TNQVechPY-----LTQEKLIQYCHSKGITVTAYSPL------GSPDRPWAKP 223
Cdd:cd19148 143 AIGVSNFSPEQMETF-----RKVAPLhTVQP---PYnlferEIEKDVLPYARKHNIVTLAYGALcrgllsGKMTKDTKFE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 224 EDPSLLEDPKIKE------IAA----------KHKKTTAQVLIRFHI-QRNVTVIP-KSMTPAHIVENIQVFDFKLSDEE 285
Cdd:cd19148 215 GDDLRRTDPKFQEprfsqyLAAveeldklaqeRYGKSVIHLAVRWLLdQPGVSIALwGARKPEQLDAVDEVFGWSLNDED 294
|
....
gi 1538612546 286 MATI 289
Cdd:cd19148 295 MKEI 298
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
70-275 |
2.39e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 80.45 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 70 REDLFIVSKV---------WPTFFE---RPLVRKAFEKTLKDLKLSYLDVYLIHwpqgfktgddffpKDDKGNMISgkgt 137
Cdd:cd19752 66 RDDVVIATKVgagprdpdgGPESPEglsAETIEQEIDKSLRRLGTDYIDLYYAH-------------VDDRDTPLE---- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 138 flDAWEAMEELVDEGLVKALGVSNFNHFQIER---LLNKPGL-KYKPVTNQvecHPYL--------------TQEkLIQY 199
Cdd:cd19752 129 --ETLEAFNELVKAGKVRAIGASNFAAWRLERarqIARQQGWaEFSAIQQR---HSYLrprpgadfgvqrivTDE-LLDY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 200 CHSKG-ITVTAYSPL--GSPDRPWAKPEDPSLLEDP-----KIKEIAAKHKKTTAQVLIRFHIQRNVTVIP--KSMTPAH 269
Cdd:cd19752 203 ASSRPdLTLLAYSPLlsGAYTRPDRPLPEQYDGPDSdarlaVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQ 282
|
....*.
gi 1538612546 270 IVENIQ 275
Cdd:cd19752 283 LEENLA 288
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-289 |
2.79e-17 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 80.74 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGT--------WRSLLGKV--KEA---VKVAIDAEYRHIDCAYFYEN-QHEV--GEAIQEKiqekavmREDLFI 75
Cdd:cd19091 12 KVSELALGTmtfgggggFFGAWGGVdqEEAdrlVDIALDAGINFFDTADVYSEgESEEilGKALKGR-------RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 76 VSKVwptFF-------ERPLVR----KAFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPkddkgnmisgkgtFLDAWEA 144
Cdd:cd19091 85 ATKV---RGrmgegpnDVGLSRhhiiRAVEASLKRLGTDYIDLYQLHGF------DALTP-------------LEETLRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 145 MEELVDEGLVKALGVSNFNHFQIERLL---NKPGLKyKPVTNQVechpYLT------QEKLIQYCHSKGITVTAYSPLG- 214
Cdd:cd19091 143 LDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPLAg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 215 -------SPDRPWAK------------PEDPSLLED--PKIKEIAAKHKKTTAQVLIRFHIQRNV--TVIPKSMTPAHIV 271
Cdd:cd19091 218 gllsgkyRRGQPAPEgsrlrrtgfdfpPVDRERGYDvvDALREIAKETGATPAQVALAWLLSRPTvsSVIIGARNEEQLE 297
|
330
....*....|....*...
gi 1538612546 272 ENIQVFDFKLSDEEMATI 289
Cdd:cd19091 298 DNLGAAGLSLTPEEIARL 315
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
34-289 |
4.39e-17 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 80.30 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 34 VAIDAEYRHIDCAYFY------ENQHEVGEAIQEKIQEKAVmREDLFIVSKV--------WP----TFFERPLVRKAFEK 95
Cdd:cd19094 26 YAFDEGVNFIDTAEMYpvppspETQGRTEEIIGSWLKKKGN-RDKVVLATKVagpgegitWPrgggTRLDRENIREAVEG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 96 TLKDLKLSYLDVYLIHWPQ----GFKTGDDFFPKDDKGNMisgkgTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLL 171
Cdd:cd19094 105 SLKRLGTDYIDLYQLHWPDrytpLFGGGYYTEPSEEEDSV-----SFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 172 N---KPGLKyKPVTNQvecHPY--LTQ---EKLIQYCHSKGITVTAYSPLG----------SPDRP-------------- 219
Cdd:cd19094 180 ElaeQLGLP-RIVSIQ---NPYslLNRnfeEGLAEACHRENVGLLAYSPLAggvltgkyldGAARPeggrlnlfpgymar 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1538612546 220 WAKPEDPSLLEdpKIKEIAAKHKKTTAQVLIRFHIQR--NVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19094 256 YRSPQALEAVA--EYVKLARKHGLSPAQLALAWVRSRpfVTSTIIGATTLEQLKENIDAFDVPLSDELLAEI 325
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-289 |
1.36e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 78.79 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 13 MPIVGLGTW--------RSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHE-VGEAIqEKIQEKAVMREDLFIVSKVWPTF 83
Cdd:cd19101 2 ISRVINGMWqlsgghggIRDEDAAVRAMAAYVDAGLTTFDCADIYGPAEElIGEFR-KRLRRERDAADDVQIHTKWVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 FE----RPLVRKAFEKTLKDLKLSYLDVYLIHWpqgfktgDDFfpkDDKGnmisgkgtFLDAWEAMEELVDEGLVKALGV 159
Cdd:cd19101 81 GEltmtRAYVEAAIDRSLKRLGVDRLDLVQFHW-------WDY---SDPG--------YLDAAKHLAELQEEGKIRHLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 160 SNFNHFQIERLLNKPglkYKPVTNQVEC-----HPyltQEKLIQYCHSKGITVTAYSP----------LGSPDRPWAKPE 224
Cdd:cd19101 143 TNFDTERLREILDAG---VPIVSNQVQYslldrRP---ENGMAALCEDHGIKLLAYGTlaggllsekyLGVPEPTGPALE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 225 DPSLLEDPKI-----------------KEIAAKHKKTTAQVLIRFHIQRNVT--VIPKSMTPAHIVENIQVFDFKLSDEE 285
Cdd:cd19101 217 TRSLQKYKLMidewggwdlfqellrtlKAIADKHGVSIANVAVRWVLDQPGVagVIVGARNSEHIDDNVRAFSFRLDDED 296
|
....
gi 1538612546 286 MATI 289
Cdd:cd19101 297 RAAI 300
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
70-289 |
1.54e-16 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 78.41 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 70 REDLFIVSKV-WPTFFERP-----LVRKAFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPKDDkgnmisgkgTFldawE 143
Cdd:cd19081 75 RDRVVIATKVgFPMGPNGPglsrkHIRRAVEASLRRLQTDYIDLYQAHWD------DPATPLEE---------TL----G 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 144 AMEELVDEGLVKALGVSNFNHFQIERLLN---KPGLKyKPVTNQVEchpY------LTQEKLIQYCHSKGITVTAYSPLG 214
Cdd:cd19081 136 ALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGLP-RYVSLQPE---YnlvdreSFEGELLPLCREEGIGVIPYSPLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 215 S--------PDRPWAK----PEDPSLLEDPK-------IKEIAAKHKKTTAQVLIRFHIQRN-VT-VIPKSMTPAHIVEN 273
Cdd:cd19081 212 GgfltgkyrSEADLPGstrrGEAAKRYLNERglrildaLDEVAAEHGATPAQVALAWLLARPgVTaPIAGARTVEQLEDL 291
|
250
....*....|....*.
gi 1538612546 274 IQVFDFKLSDEEMATI 289
Cdd:cd19081 292 LAAAGLRLTDEEVARL 307
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-252 |
2.27e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 77.57 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 26 GKV--KEAVKV---AIDAEYRHIDCAYFYENQHEV-GEAIQEKiqekavmrEDLFIVSKV----WPTFFERPLVRKAFEK 95
Cdd:cd19097 21 GKPseKEAKKIleyALKAGINTLDTAPAYGDSEKVlGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 96 TLKDLKLSYLDVYLIHWPqgfktgDDFFPKDDKgnmisgkgtfldAWEAMEELVDEGLVKALGVSNFNHFQIERLLNKPG 175
Cdd:cd19097 93 SLKRLKVDSLDGLLLHNP------DDLLKHGGK------------LVEALLELKKEGLIRKIGVSVYSPEELEKALESFK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 176 LKYkpVtnQVECHPY---LTQEKLIQYCHSKGITVTAYSP------LGSPDRPWAKPED-PSLLEdpKIKEIAAKHKKTT 245
Cdd:cd19097 155 IDI--I--QLPFNILdqrFLKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLPAKFAPaKPLLK--KLHELAKKLGLSP 228
|
....*..
gi 1538612546 246 AQVLIRF 252
Cdd:cd19097 229 LELALGF 235
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-289 |
8.10e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 76.54 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 31 AVKVAIDAEYRHIDCAYFY-ENQHEV--GEAIQEKiqekavmREDLFIVSKVWPTFFERP----LVRKAFEKTLKDLKLS 103
Cdd:cd19104 37 AVRRALDLGINFFDTAPSYgDGKSEEnlGRALKGL-------PAGPYITTKVRLDPDDLGdiggQIERSVEKSLKRLKRD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 104 YLDVYLIH---WPQGFKTGDDFFPKDDkgnmISGKGtflDAWEAMEELVDEGLVKALGVSNFNHFQ-IERLL--NKPG-- 175
Cdd:cd19104 110 SVDLLQLHnriGDERDKPVGGTLSTTD----VLGLG---GVADAFERLRSEGKIRFIGITGLGNPPaIRELLdsGKFDav 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 176 ------LKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPL------GSPDRPwakPEDPSLLEDP---------KI 234
Cdd:cd19104 183 qvyynlLNPSAAEARPRGWSAQDYGGIIDAAAEHGVGVMGIRVLaagaltTSLDRG---REAPPTSDSDvaidfrraaAF 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1538612546 235 KEIAAKHKKTTAQVLIRFHI-QRNV-TVIPKSMTPAHIVENIQVFDF-KLSDEEMATI 289
Cdd:cd19104 260 RALAREWGETLAQLAHRFALsNPGVsTVLVGVKNREELEEAVAAEAAgPLPAENLARL 317
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
70-289 |
1.37e-15 |
|
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: 75.94 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 70 REDLFIVSKV----------WPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHwpqgfktgddffpkddkgnMISGKGTFL 139
Cdd:cd19144 75 REKIFLATKFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH-------------------RVDGKTPIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 140 DAWEAMEELVDEGLVKALGVSNFNHFQIERllnkpGLKYKPVTN-QVECHPYLT-----QEKLIQYCHSKGITVTAYSPL 213
Cdd:cd19144 136 KTVAAMAELVQEGKIKHIGLSECSAETLRR-----AHAVHPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 214 G---------SPD----------RPWAKPED-PSLLE--DpKIKEIAAKHKKTTAQVLIRFHIQR--NVTVIPKSMTPAH 269
Cdd:cd19144 211 GrgfltgairSPDdfeegdfrrmAPRFQAENfPKNLElvD-KIKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKR 289
|
250 260
....*....|....*....|
gi 1538612546 270 IVENIQVFDFKLSDEEMATI 289
Cdd:cd19144 290 LEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
29-289 |
8.05e-14 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 70.72 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 29 KEAVKV---AIDAEYRHIDCAYFY---ENQHEVGEAIqekiqekAVMREDLFIVSK----------VWPTFFERP-LVRK 91
Cdd:cd19078 25 EEMIELirkAVELGITFFDTAEVYgpyTNEELVGEAL-------KPFRDQVVIATKfgfkidggkpGPLGLDSRPeHIRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 92 AFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPKDDKGnmisgkgtfldawEAMEELVDEGLVKALGVSNFNHFQIERll 171
Cdd:cd19078 98 AVEGSLKRLQTDYIDLYYQHRV------DPNVPIEEVA-------------GTMKELIKEGKIRHWGLSEAGVETIRR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 172 nkpGLKYKPVTN-QVECH-----PyltQEKLIQYCHSKGITVTAYSPLGS--------PDRPWAKPEDPSLLedPK---- 233
Cdd:cd19078 157 ---AHAVCPVTAvQSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGKgfltgkidENTKFDEGDDRASL--PRftpe 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1538612546 234 -----------IKEIAAKHKKTTAQVLIRF--HIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19078 229 aleanqalvdlLKEFAEEKGATPAQIALAWllAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
28-289 |
3.89e-13 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 68.46 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 28 VKEAVKVAIDaeyrHIDCAYFYeNQHEVGEAIQEKIQEkavMREDLFIVSKV---------WPTFFERPLVRKAFEKTLK 98
Cdd:PRK10376 46 LREAVALGVN----HIDTSDFY-GPHVTNQLIREALHP---YPDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 99 DLKLSYLDVYLIHwpqgfKTGDDFFPKDdkgnmisgkGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERllnkpGLKY 178
Cdd:PRK10376 118 NLGLDVLDVVNLR-----LMGDGHGPAE---------GSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAE-----ARKI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 179 KPVTNqVECHPYLTQ---EKLIQYCHSKGITVTAYSPLG--SPdrpwakpedpslLEDPKIKEIAAKHKKTTAQVLIRFH 253
Cdd:PRK10376 179 AEIVC-VQNHYNLAHradDALIDALARDGIAYVPFFPLGgfTP------------LQSSTLSDVAASLGATPMQVALAWL 245
|
250 260 270
....*....|....*....|....*....|....*...
gi 1538612546 254 IQR--NVTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:PRK10376 246 LQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLAEL 283
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
143-289 |
5.02e-13 |
|
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: 68.42 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 143 EAMEELVDEGLVKALGVSNFNHFQIERllnkpGLKYKPVT-NQVECHPyLTQEKL----IQYCHSKGITVTAYSPL---- 213
Cdd:cd19077 132 KALKELVKEGKIRGIGLSEVSAETIRR-----AHAVHPIAaVEVEYSL-FSREIEengvLETCAELGIPIIAYSPLgrgl 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 214 --GSPDRPWAKPEDPSLLEDP---------------KIKEIAAKHKKTTAQVLIRFHIQRNVTVI---PKSMTPAHIVEN 273
Cdd:cd19077 206 ltGRIKSLADIPEGDFRRHLDrfngenfeknlklvdALQELAEKKGCTPAQLALAWILAQSGPKIipiPGSTTLERVEEN 285
|
170
....*....|....*.
gi 1538612546 274 IQVFDFKLSDEEMATI 289
Cdd:cd19077 286 LKAANVELTDEELKEI 301
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
35-214 |
5.49e-13 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 68.37 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 35 AIDAEYRHIDCAYFYENQHE---VGEAIQEKiqekavmREDLFIVSKVwptFFE-----------RPLVRKAFEKTLKDL 100
Cdd:cd19087 39 ALDAGINFFDTADVYGGGRSeeiIGRWIAGR-------RDDIVLATKV---FGPmgddpndrglsRRHIRRAVEASLRRL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 101 KLSYLDVYLIHWPqgfktgDDFFPKDDKgnmisgkgtfldaWEAMEELVDEGLVKALGVSNFNHFQIERLLN---KPGL- 176
Cdd:cd19087 109 QTDYIDLYQMHHF------DRDTPLEET-------------LRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaaRRGLl 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1538612546 177 -------KYKPVTNQVECHpyltqekLIQYCHSKGITVTAYSPLG 214
Cdd:cd19087 170 rfvseqpMYNLLKRQAELE-------ILPAARAYGLGVIPYSPLA 207
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
12-287 |
9.62e-12 |
|
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: 64.59 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWR-----SLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKI--QEKAVMREDLFIVSKV----W 80
Cdd:cd19089 10 HLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRIlkRDLRPYRDELVISTKAgygmW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 81 P----TFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfktgDDFFPKDDkgnmisgkgtfldAWEAMEELVDEGlvKA 156
Cdd:cd19089 90 PgpygDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRY------DPDTPLEE-------------TMTALADAVRSG--KA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 157 L--GVSNFNHFQIER---LLNKpgLKYKPVTNQVechPY--LTQ---EKLIQYCHSKGITVTAYSPL-----------GS 215
Cdd:cd19089 149 LyvGISNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIGFIAFSPLaqglltdkylnGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 216 PDRPWAKPEDPSLLED-------PKIK---EIAAKHKKTTAQVLIRFHIQR-NVT-VIPKSMTPAHIVENIQVFD-FKLS 282
Cdd:cd19089 224 PPDSRRAAESKFLTEEaltpeklEQLRklnKIAAKRGQSLAQLALSWVLRDpRVTsVLIGASSPSQLEDNVAALKnLDFS 303
|
....*
gi 1538612546 283 DEEMA 287
Cdd:cd19089 304 EEELA 308
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-253 |
1.99e-11 |
|
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: 63.73 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 15 IVGLGTWRSLLG-----KVKEAVKVAIDAEYRHIDCAYFYEN-QHE--VGEAIQEKiqekavmrEDLFIVSKVWPTF--- 83
Cdd:cd19075 4 ILGTMTFGSQGRfttaeAAAELLDAFLERGHTEIDTARVYPDgTSEelLGELGLGE--------RGFKIDTKANPGVggg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 FERPLVRKAFEKTLKDLKLSYLDVYLIHWPqgfktgddffpkdDKGNMISgkgtflDAWEAMEELVDEGLVKALGVSNFN 163
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAP-------------DRSTPLE------ETLAAIDELYKEGKFKEFGLSNYS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 164 HFQIERLLN--------KP----GLkYKPVTNQVEchpyltqEKLIQYCHSKGITVTAYSPLG----------------- 214
Cdd:cd19075 137 AWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLAggfltgkykysedkagg 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1538612546 215 ---SPDRPWA--------KPEDPSLLEdpKIKEIAAKHKKTTAQVLIR---FH 253
Cdd:cd19075 209 grfDPNNALGklyrdrywKPSYFEALE--KVEEAAEKEGISLAEAALRwlyHH 259
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
12-287 |
7.34e-10 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 58.72 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTwrSLLGKV------KEAVKV---AIDAEYRHIDCAYFYenqhevGEAIQEKIQEKA---VMREDLFIVSKV 79
Cdd:cd19163 12 KVSKLGFGA--SPLGGVfgpvdeEEAIRTvheALDSGINYIDTAPWY------GQGRSETVLGKAlkgIPRDSYYLATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 ------WPTFF----ERplVRKAFEKTLKDLKLSYLDVYLIHwpqgfktgD-DFFPKDDkgnMIsgkgtFLDAWEAMEEL 148
Cdd:cd19163 84 grygldPDKMFdfsaER--ITKSVEESLKRLGLDYIDIIQVH--------DiEFAPSLD---QI-----LNETLPALQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 149 VDEGLVKALGVSNFNHFQIERLLNKpglkykpVTNQVE-----CHPYL---TQEKLIQYCHSKGITVTAYSPLG------ 214
Cdd:cd19163 146 KEEGKVRFIGITGYPLDVLKEVLER-------SPVKIDtvlsyCHYTLndtSLLELLPFFKEKGVGVINASPLSmgllte 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 215 SPDRPW--AKPEdpslledpkIKEI---AAKHKKT----TAQVLIRFHIQR---NVTVIpkSMT-PAHIVENIQVFDFKL 281
Cdd:cd19163 219 RGPPDWhpASPE---------IKEAcakAAAYCKSrgvdISKLALQFALSNpdiATTLV--GTAsPENLRKNLEAAEEPL 287
|
....*.
gi 1538612546 282 SDEEMA 287
Cdd:cd19163 288 DAHLLA 293
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
43-289 |
8.52e-10 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 58.77 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 43 IDCAYFYEN-QHE--VGEAIQEkiqekavMREDLFIVSKVwpTFFERP------------LVRkAFEKTLKDLKLSYLDV 107
Cdd:cd19080 48 IDTANNYTNgTSErlLGEFIAG-------NRDRIVLATKY--TMNRRPgdpnaggnhrknLRR-SVEASLRRLQTDYIDL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 108 YLIHWPQGFKTGDDFfpkddkgnMisgkgtfldawEAMEELVDEGLVKALGVSNFNHFQIER---LLNKPGLKyKPVTNQ 184
Cdd:cd19080 118 LYVHAWDFTTPVEEV--------M-----------RALDDLVRAGKVLYVGISDTPAWVVARantLAELRGWS-PFVALQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 185 VECHpyLTQ----EKLIQYCHSKGITVTAYSPLGS---------PDRPWAKPEDPSLLEDPKI-----------KEIAAK 240
Cdd:cd19080 178 IEYS--LLErtpeRELLPMARALGLGVTPWSPLGGglltgkyqrGEEGRAGEAKGVTVGFGKLternwaivdvvAAVAEE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1538612546 241 HKKTTAQVLIRFHIQRNVTVIP--KSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19080 256 LGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
32-289 |
3.41e-09 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 57.06 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 32 VKVAIDAEYRHIDCAYFY---ENQHEVGEAIQEKIQEKAVM--REDLFIVSKVWPTFFERP-LVRKAFEKTLKDLKLSYL 105
Cdd:cd19145 39 IHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGPREKVQLatKFGIHEIGGSGVEVRGDPaYVRAACEASLKRLDVDYI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 106 DVYLIHwpqgfktgddffpkddkgnMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERllnkpGLKYKPVTN-Q 184
Cdd:cd19145 119 DLYYQH-------------------RIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRR-----AHAVHPITAvQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 185 VECHPYL--TQEKLIQYCHSKGITVTAYSPLGspdRP--WAKPEDPSLLEDP----------------------KIKEIA 238
Cdd:cd19145 175 LEWSLWTrdIEEEIIPTCRELGIGIVPYSPLG---RGffAGKAKLEELLENSdvrkshprfqgenleknkvlyeRVEALA 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1538612546 239 AKHKKTTAQV-LIRFHIQRN-VTVIPKSMTPAHIVENIQVFDFKLSDEEMATI 289
Cdd:cd19145 252 KKKGCTPAQLaLAWVLHQGEdVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
70-214 |
6.94e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 56.40 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 70 REDLFIVSKV-WPT-----------FFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQgfkTGDDFFPK------DDKGNM 131
Cdd:PRK10625 79 REKLIIASKVsGPSrnndkgirpnqALDRKNIREALHDSLKRLQTDYLDLYQVHWPQ---RPTNCFGKlgyswtDSAPAV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 132 isgkgTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLL---NKPGLKyKPVTNQvecHPYLTQEK-----LIQYCHSK 203
Cdd:PRK10625 156 -----SLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLhlaEKHDLP-RIVTIQ---NPYSLLNRsfevgLAEVSQYE 226
|
170
....*....|.
gi 1538612546 204 GITVTAYSPLG 214
Cdd:PRK10625 227 GVELLAYSCLA 237
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-284 |
2.28e-08 |
|
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: 54.54 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 14 PIVGLGTwrSLLG---------KVKEAVKVAIDAEYRHIDCAYFYEN---QHEVGEAIQEKIQEKAVM-------REDLF 74
Cdd:cd19152 1 PKLGFGT--APLGnlyeavsdeEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRELGREDYVIstkvgrlLVPLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 75 IVSKVWPTFFERPL------------VRKAFEKTLKDLKLSYLDVYLIHWPQGfktgDDFFPKDDKGNMISGKGTFLdaw 142
Cdd:cd19152 79 EVEPTFEPGFWNPLpfdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPDE----DLAGAESDEHFAQAIKGAFR--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 143 eAMEELVDEGLVKALGV--------------SNFNHFQIER---LLNKPGLKykpvtnqvechpyltqeKLIQYCHSKGI 205
Cdd:cd19152 152 -ALEELREEGVIKAIGLgvndwevilrileeADLDWVMLAGrytLLDHSAAR-----------------ELLPECEKRGV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 206 TVTAYSPLGS--------PDRPWAKPEDPSLLE--DpKIKEIAAKHKKTTAQVLIRFHIQRNV--TVIPKSMTPAHIVEN 273
Cdd:cd19152 214 KVVNAGPFNSgflaggdnFDYYEYGPAPPELIArrD-RIEALCEQHGVSLAAAALQFALAPPAvaSVAPGASSPERVEEN 292
|
330
....*....|.
gi 1538612546 274 IQVFDFKLSDE 284
Cdd:cd19152 293 VALLATEIPAA 303
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-273 |
2.38e-08 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 54.29 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 14 PIVGLGTwrSLLGKVKE--------AVKVAIDAEYRHIDCAYFY---ENQHEVGEAIQEKiqekavMREDLFIVSKV--- 79
Cdd:cd19162 1 PRLGLGA--ASLGNLARagedeaaaTLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 80 -------WPTFFERPL------VRKAFEKTLKDLKLSYLDVYLIHWPQgfktgddffPKDDKGnmisgkgtFLDAWEAME 146
Cdd:cd19162 73 lepgaagRPAGADRRFdfsadgIRRSIEASLERLGLDRLDLVFLHDPD---------RHLLQA--------LTDAFPALE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 147 ELVDEGLVKALGVSNFNHFQIERLLNKPGLKYKPVTNQvecHPYLTQE---KLIQYCHSKGITVTAYSPLGS-------- 215
Cdd:cd19162 136 ELRAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAGR---YTLLDRRaatELLPLCAAKGVAVVAAGVFNSgilatddp 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1538612546 216 -PDRPWAKPEDPSLLEDP-KIKEIAAKHKKTTAQVLIRFHIQ--RNVTVIPKSMTPAHIVEN 273
Cdd:cd19162 213 aGDRYDYRPATPEVLARArRLAAVCRRYGVPLPAAALQFPLRhpAVASVVVGAASPAELRDN 274
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-289 |
8.99e-07 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 49.52 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 18 LGTWRSLLGKV-----KEAVKVAIDAEYRHIDCAYFYEN-QHEV--GEAIQEKiqekAVMREDLFIVSKVwptFF----- 84
Cdd:cd19143 18 FGSWVTFGNQVdvdeaKECMKAAYDAGVNFFDNAEVYANgQSEEimGQAIKEL----GWPRSDYVVSTKI---FWggggp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 85 ---ERPLVRK----AFEKTLKDLKLSYLDVYLIHWPqgfktgddffpkDDKGNMisgkgtfLDAWEAMEELVDEGLVKAL 157
Cdd:cd19143 91 ppnDRGLSRKhiveGTKASLKRLQLDYVDLVFCHRP------------DPATPI-------EETVRAMNDLIDQGKAFYW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 158 GVSNFNHFQIE---RLLNKPGLkYKPVTNQVECHpYLTQEKL-IQY---CHSKGITVTAYSPLGS--------------- 215
Cdd:cd19143 152 GTSEWSAQQIEeahEIADRLGL-IPPVMEQPQYN-LFHRERVeVEYaplYEKYGLGTTTWSPLASglltgkynngipegs 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 216 ----PDRPWAKPEDPSLLED-----PKIKEIAAKHKKTTAQVLIRFHIQR-NV-TVIPKSMTPAHIVENIQVFDF--KLS 282
Cdd:cd19143 230 rlalPGYEWLKDRKEELGQEkiekvRKLKPIAEELGCSLAQLAIAWCLKNpNVsTVITGATKVEQLEENLKALEVlpKLT 309
|
....*..
gi 1538612546 283 DEEMATI 289
Cdd:cd19143 310 PEVMEKI 316
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
12-213 |
1.49e-06 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 49.00 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 12 KMPIVGLGTWRSLLGKVKEA-----VKVAIDAEYRHIDCAYFYENQHevGEAIQEKIQEKAVMREDLFIVS-KV-WPTF- 83
Cdd:cd19142 12 RVSNVGLGTWSTFSTAISEEqaeeiVTLAYENGINYFDTSDAFTSGQ--AETELGRILKKKGWKRSSYIVStKIyWSYGs 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 84 FERPLVRK----AFEKTLKDLKLSYLDVYLIHWpqgfktgddffpkddkgnmisgkgtfLDAWEAMEE-------LVDEG 152
Cdd:cd19142 90 EERGLSRKhiieSVRASLRRLQLDYIDIVIIHK--------------------------ADPMCPMEEvvramsyLIDNG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1538612546 153 LVKALGVSNFNH------FQIERLLNKPglkyKPVTNQVECHPyLTQEKLIQYC----HSKGITVTAYSPL 213
Cdd:cd19142 144 LIMYWGTSRWSPveimeaFSIARQFNCP----TPICEQSEYHM-FCREKMELYMpelyNKVGVGLITWSPL 209
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
30-167 |
3.96e-06 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 47.71 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 30 EAVKVAIDAEYRHIDCAYFYEN---QHEVGEAIQEKIQEKAVM----------REDLFIVSKVW---PTFFERPL----- 88
Cdd:cd19161 24 ATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREKPRDEFVLstkvgrllkpAREGSVPDPNGfvdPLPFEIVYdysyd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 89 -VRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGkgtfldaWEAMEELVDEGLVKA--LGVsnfNHF 165
Cdd:cd19161 104 gIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKERHHFAQLMSGG-------FKALEELKKAGVIKAfgLGV---NEV 173
|
..
gi 1538612546 166 QI 167
Cdd:cd19161 174 QI 175
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
30-160 |
5.06e-06 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 47.27 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 30 EAVKVAIDAEYRHIDCAYFYENQHEV-GEAIqeKIQEKAVMREDLFIVSKV----WPTF-FERPLVRKAFEKTLKDLKLS 103
Cdd:cd19164 38 DIVRRALELGIRAFDTSPYYGPSEIIlGRAL--KALRDEFPRDTYFIITKVgrygPDDFdYSPEWIRASVERSLRRLHTD 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 104 YLDVYLIHwpqgfktgDDFFPKDDkgnmisgkgtflDAWEAMEELV---DEGLVKALGVS 160
Cdd:cd19164 116 YLDLVYLH--------DVEFVADE------------EVLEALKELFklkDEGKIRNVGIS 155
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
9-278 |
7.01e-05 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 43.68 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 9 TKAKMPIVGLGTwrSLLGKV----------KEAVKVAIDAEYRHIDCAYFYenqhevGEAIQEKIQEKA-----VMREDL 73
Cdd:cd19153 8 ALGNVSPVGLGT--AALGGVygdgleqdeaVAIVAEAFAAGINHFDTSPYY------GAESSEAVLGKAlaalqVPRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 74 FIVSKVW----PTF-FERPLVRKAFEKTLKDLKLSYLDVYLIHwpqgfktgDDFFPKDDKgnmisgkgTFLDAWEAMEEL 148
Cdd:cd19153 80 TVATKVGryrdSEFdYSAERVRASVATSLERLHTTYLDVVYLH--------DIEFVDYDT--------LVDEALPALRTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538612546 149 VDEGLVKALGVSNFNHFQIERLLNKPGLKYKPVTnQVECH------------PYLTQEKLIQYCHSKGITVTAYSPLGSP 216
Cdd:cd19153 144 KDEGVIKRIGIAGYPLDTLTRATRRCSPGSLDAV-LSYCHltlqdarlesdaPGLVRGAGPHVINASPLSMGLLTSQGPP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1538612546 217 drPWaKPEDPSLLEDPKikeIAAKHKKTTAQVLIRFHIQRNV-------TVIPKSMTPAHIVENIQVFD 278
Cdd:cd19153 223 --PW-HPASGELRHYAA---AADAVCASVEASLPDLALQYSLaahagvgTVLLGPSSLAQLRSMLAAVD 285
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