|
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: 617.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 10 KAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFFEKSLV 89
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 90 KKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGISNFNHFQIER 169
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 170 LLNKPGLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKPEDPVVMEIPKIKEIAAKHKKTVAQVL 249
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160415215 250 IRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWRACDLLDARTEEDYPFHEEY 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 |
1.51e-153 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 432.19 E-value: 1.51e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 7 LSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKEN-AVKREDLFIVSKLWATFFE 85
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGkAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 86 KSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGISNFNHF 165
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 166 QIERLLNKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKPEDPVVMEIPKIKEIAAKHKKTV 245
Cdd:cd19106 161 QIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 160415215 246 AQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWRAC 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 |
1.34e-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: 427.07 E-value: 1.34e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFFEKSLVKK 91
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 92 AFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGISNFNHFQIERLL 171
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 172 NKPGLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKPEDPVvmeipkIKEIAAKHKKTVAQVLIR 251
Cdd:cd19110 163 NKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVDLIDDPV------IQRIAKKHGKSPAQILIR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160415215 252 FHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWRACDLLDARTEEDYPFHEEY 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) ... |
3-297 |
1.91e-126 |
|
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: 363.47 E-value: 1.91e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 3 TFVELSTKAKMPLVGLGTWKSS---PGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKL 79
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEevpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 80 WATFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGI 159
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 160 SNFNHFQIERLLNKPGLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSP-DRPYAKPEDPVVMEIPKIKEIA 238
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 160415215 239 AKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-289 |
1.02e-122 |
|
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: 351.78 E-value: 1.02e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 13 MPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIkenaVKREDLFIVSKLWATFFEKSLVKKA 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 93 FQNTLSDLKLDYLDLYLVHWPQGFQAGNallpkdnkgkvllSKSTFLDAWEAMEELVDQGLVKALGISNFNHFQIERLLN 172
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEGG-------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 173 KPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPyakpedpvVMEIPKIKEIAAKHKKTVAQVLIRF 252
Cdd:cd19071 144 AA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP--------LLDDPVLKEIAKKYGKTPAQVLLRW 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 160415215 253 HVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 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 |
1.05e-120 |
|
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: 349.10 E-value: 1.05e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 13 MPLVGLGTW----KSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFFEKSL 88
Cdd:cd19109 4 IPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHPPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 89 VKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGISNFNHFQIE 168
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRRQLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 169 RLLNKPGLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSP-DRPYAKPEDPVVMEIPKIKEIAAKHKKTVAQ 247
Cdd:cd19109 164 LILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNKTAAQ 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160415215 248 VLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWRACDLLDARTEEDYPF 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 |
1.04e-119 |
|
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: 345.81 E-value: 1.04e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTWKS-SPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFFEKSLVK 90
Cdd:cd19116 10 EIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHEREQVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 91 KAFQNTLSDLKLDYLDLYLVHWPQGFQAGNallPKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGISNFNHFQIERL 170
Cdd:cd19116 90 PALRESLKRLGLDYVDLYLIHWPVAFKENN---DSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 171 LNkpGLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKPEdPVVMEIPKIKEIAAKHKKTVAQVLI 250
Cdd:cd19116 167 LS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNP-PPRLDDPTLVAIAKKYGKTTAQIVL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 160415215 251 RFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWRAC 299
Cdd:cd19116 244 RYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-297 |
1.19e-116 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 338.23 E-value: 1.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 1 MATFvELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLW 80
Cdd:cd19123 1 MKTL-PLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 81 ATFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGnALLPKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGIS 160
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 161 NFNHFQIERLLNKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYA-KPED-PVVMEIPKIKEIA 238
Cdd:cd19123 159 NFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAmKAEGePVLLEDPVINKIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 160415215 239 AKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19123 237 EKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-297 |
1.68e-114 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 331.25 E-value: 1.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 11 AKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWATFFEKSLVK 90
Cdd:COG0656 3 VEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAI----AASGVPREELFVTTKVWNDNHGYDDTL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 91 KAFQNTlsdlkldyldlylVHWPqgfqagnallpkdNKGKvllskstFLDAWEAMEELVDQGLVKALGISNFNHFQIERL 170
Cdd:COG0656 79 AAFEESlerlgldyldlylIHWP-------------GPGP-------YVETWRALEELYEEGLIRAIGVSNFDPEHLEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 171 LNKPGlkHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDrpyakpedpvVMEIPKIKEIAAKHKKTVAQVLI 250
Cdd:COG0656 139 LAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQVVL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 160415215 251 RFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:COG0656 207 RWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGER 253
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-299 |
2.04e-106 |
|
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: 312.42 E-value: 2.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 2 ATFVELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWA 81
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 82 TFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGISN 161
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 162 FNHFQIERLLNKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKPED-----PVVMEIPKIKE 236
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspaPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160415215 237 IAAKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWRAC 299
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
3-289 |
5.25e-103 |
|
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: 303.11 E-value: 5.25e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 3 TFVELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWAT 82
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 83 FFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNallPKDNKGKVLlsKSTFLDAWEAMEELVDQGLVKALGISNF 162
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 163 NHFQIERLLNKPGLkhKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKPEdpvVMEIPKIKEIAAKHK 242
Cdd:cd19125 156 SVKKLEDLLAVARV--PPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKLG 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 160415215 243 KTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19125 231 KTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKF 277
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-300 |
1.41e-93 |
|
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: 280.18 E-value: 1.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 4 FVELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATF 83
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 FEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQA-GNALLPKDNKGKVLLSKST-FLDAWEAMEELVDQGLVKALGISN 161
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSkEDDSGKLDPTGEHKQDYTTdLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 162 FNHFQIERLLNKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKP-------EDPVVMEIPKI 234
Cdd:cd19155 163 FNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160415215 235 KEIAAKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWRACD 300
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGRT 306
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-289 |
3.19e-92 |
|
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: 275.83 E-value: 3.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 7 LSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKEN-AVKREDLFIVSKLWATFFE 85
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEpGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 86 KSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPK----DNKGKVLLSKSTFL-DAWEAMEELVDQGLVKALGIS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavpTNGGEVDLDLSVSLvDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 161 NFNHFQIERLLNKPGLkhKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSpdrpyAKPEDPVVMEIPKIKEIAAK 240
Cdd:cd19118 161 NFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-----NLAGLPLLVQHPEVKAIAAK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 160415215 241 HKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDfqLSEEDMAAI 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 |
1.49e-90 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 271.29 E-value: 1.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 7 LSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWATFFEK 86
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFITTKLWCTWHRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 87 slVKKAFQNTLSDLKLDYLDLYLVHWPQGF-QAGNALLPKDNKG-KVLLSKSTFLDAWEAMEELVDQGLVKALGISNFNH 164
Cdd:cd19117 84 --VEEALDQSLKKLGLDYVDLYLMHWPVPLdPDGNDFLFKKDDGtKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 165 FQIERLLNKPGLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPyakpedpvVMEIPKIKEIAAKHKKT 244
Cdd:cd19117 162 KNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGKT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 160415215 245 VAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVfdFQLSEEDMAAI 289
Cdd:cd19117 234 PAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEI 276
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-297 |
5.95e-90 |
|
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: 270.14 E-value: 5.95e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFFEKSLVKK 91
Cdd:cd19111 3 PMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDTEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 92 AFQNTLSDLKLDYLDLYLVHWPQGFQAgnallpKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGISNFNHFQIERLL 171
Cdd:cd19111 83 SLEKSLENLKLPYVDLYLIHHPCGFVN------KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 172 NKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRP--YAKPEDPVVMEIPKIKEIAAKHKKTVAQVL 249
Cdd:cd19111 157 AYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPAQVL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 160415215 250 IRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19111 235 LRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-289 |
1.05e-89 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 269.01 E-value: 1.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 14 PLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFFEKSLVKKAF 93
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 94 QNTLSDLKLDYLDLYLVHWPQGFQAGNALLPKDNKGKVLLSKSTFLDAWEAMEELVDQGLVKALGISNFNHFQIERLLNK 173
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 174 pgLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSpdrPYAKPEDpVVMEIPKIKEIAAKHKKTVAQVLIRFH 253
Cdd:cd19128 162 --CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGG---SYGDGNL-TFLNDSELKALATKYNTTPPQVIIAWH 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 160415215 254 VQR---NVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19128 236 LQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
5-297 |
8.38e-87 |
|
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: 262.81 E-value: 8.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATff 84
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 85 EKSLVKKAFQNTLSDLKLDYLDLYLVHWP-----QGFQAGNALLPKDNKGKVLLSKStFLDAWEAMEELVDQGLVKALGI 159
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHFPvatkhTGVGTTGSALGEDGVLDIDVTIS-LETTWHAMEKLVSAGLVRSIGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 160 SNFNHFQIERLLNKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRP-----YAKP-EDPVVmeipk 233
Cdd:cd19112 160 SNYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANaewfgSVSPlDDPVL----- 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160415215 234 iKEIAAKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19112 233 -KDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-289 |
1.32e-86 |
|
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: 260.38 E-value: 1.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLW--AT 82
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLWnsDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 83 FFEKSLvkKAFQNTLSDLKLDYLDLYLVHWPQgfqagnallPKDNKgkvllskstFLDAWEAMEELVDQGLVKALGISNF 162
Cdd:cd19131 78 GYDSTL--RAFDESLRKLGLDYVDLYLIHWPV---------PAQDK---------YVETWKALIELKKEGRVKSIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 163 NHFQIERLLNKPGLKhkPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDrpyakpedpvVMEIPKIKEIAAKHK 242
Cdd:cd19131 138 TIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG----------LLSDPVIGEIAEKHG 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 160415215 243 KTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19131 206 KTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAI 252
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-297 |
2.25e-86 |
|
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: 261.59 E-value: 2.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 1 MATFVELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLW 80
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 81 ATFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQ--AGNALLP---KDNKGKVLLSKSTFLDAWEAMEELVDQGLVK 155
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvDPAVRYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 156 ALGISNFNHFQIERLLNKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGsP------DRPYAKpEDPVVM 229
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PqsflelDLPGAK-DTPPLF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160415215 230 EIPKIKEIAAKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
2-292 |
2.12e-83 |
|
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: 253.22 E-value: 2.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 2 ATFVELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIkENAVKREDLFIVSKLWA 81
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 82 TFFEKslVKKAFQNTLSDLKLDYLDLYLVHWPQGFQA-GN-ALLPKDNKGK-VLLSKSTFLDAWEAMEELVDQGLVKALG 158
Cdd:cd19121 80 TYHRR--VELCLDRSLKSLGLDYVDLYLVHWPVLLNPnGNhDLFPTLPDGSrDLDWDWNHVDTWKQMEKVLKTGKTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 159 ISNFNHFQIERLLnkPGLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKpEDPVVmeipkikEIA 238
Cdd:cd19121 158 VSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLIS-DEPVV-------EIA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 160415215 239 AKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFqlSEEDMAAILSF 292
Cdd:cd19121 228 KKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-291 |
2.99e-83 |
|
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: 252.17 E-value: 2.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 13 MPLVGLGTWK-SSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFFEKSLVKK 91
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 92 AFQNTLSDLKLDYLDLYLVHWPqgfqaGNALLPKDNKGKVLLSKSTfldaWEAMEELVDQGLVKALGISNFNHFQIERLL 171
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWP-----GVQGLKPSDPRNAELRRES----WRALEDLYKEGKLRAIGVSNYTVRHLEELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 172 NKPGLkhKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPdrpyakpeDPVVMEIPKIKEIAAKHKKTVAQVLIR 251
Cdd:cd19136 152 KYCEV--PPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG--------DLRLLEDPTVLAIAKKYGRTPAQVLLR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 160415215 252 FHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILS 291
Cdd:cd19136 222 WALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-297 |
5.56e-83 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 253.14 E-value: 5.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFF 84
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 85 EKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQagnaLLPKDNK----------GKVLLSKSTFLDAWEAMEELVDQGLV 154
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFK----FVPIEEKyppgfycgdgDNFVYEDVPILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 155 KALGISNFNHFQIERLLNkpGLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSP-----DRPYAKpEDPVVM 229
Cdd:cd19113 159 KSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL-NTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160415215 230 EIPKIKEIAAKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-293 |
4.47e-82 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 248.89 E-value: 4.47e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTWKSSPG-QVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWATF 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAI----RESGVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 FEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagnallpkdnkgkvllSKSTFLDAWEAMEELVDQGLVKALGISNFN 163
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWP--------------------GKDKFIDTWKALEKLYASGKVKAIGVSNFQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 164 HFQIERLLnkpglKH---KPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPdrpyakpedpVVMEIPKIKEIAAK 240
Cdd:cd19126 137 EHHLEELL-----AHadvVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----------GLLSNPVLAAIGEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 160415215 241 HKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFN 293
Cdd:cd19126 202 YGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-297 |
6.82e-82 |
|
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: 248.85 E-value: 6.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 4 FVELSTKAKMPLVGLGTWKSSPGQ-VKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWAT 82
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGI----KESGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 83 --FFEKSLvkKAFQNTLSDLKLDYLDLYLVHWPqgfqagnallpKDNKGKvllskstflDAWEAMEELVDQGLVKALGIS 160
Cdd:cd19157 77 dqGYDSTL--KAFEASLERLGLDYLDLYLIHWP-----------VKGKYK---------ETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 161 NFNHFQIERLLNKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDrpyakpedpvVMEIPKIKEIAAK 240
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEK 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 160415215 241 HKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 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 |
3.74e-79 |
|
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: 241.02 E-value: 3.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 13 MPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWATFFEKSLVKKA 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 93 FQNTLSDLKLDYLDLYLVHWPQgfqagnallPKDNKGKVLlskstfldawEAMEELVDQGLVKALGISNFNHFQIERLLN 172
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN---------PTVPLEETL----------GALKELKEAGKVKSIGVSNFTIELLEEALD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 173 KPGLKhkPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLgspdrpyAKPEdpvVMEIPKIKEIAAKHKKTVAQVLIRF 252
Cdd:cd19073 138 ISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-------ARGE---VLRDPVIQEIAEKYDKTPAQVALRW 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 160415215 253 HVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19073 206 LVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-292 |
5.23e-79 |
|
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: 241.46 E-value: 5.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 4 FVELSTKAKMPLVGLGTWKSSpGQVKEAVKAAI-DAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWAT 82
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSG-GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAI----KESGVPREDLFLTTKLWPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 83 FFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQgfqagnALLPKDNKgkvllsKSTFLDAWEAMEELVDQGLVKALGISNF 162
Cdd:cd19135 79 DYGYESTKQAFEASLKRLGVDYLDLYLLHWPD------CPSSGKNV------KETRAETWRALEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 163 NHFQIERLLNKPGLKhkPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLgspdrpyAKPEdpvVMEIPKIKEIAAKHK 242
Cdd:cd19135 147 LIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-------AKGK---ALEEPTVTELAKKYQ 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 160415215 243 KTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSF 292
Cdd:cd19135 215 KTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
5-297 |
1.23e-77 |
|
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: 237.80 E-value: 1.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTWKSSPGQVKE-AVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWAT- 82
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGI----RESGVPREEVFVTTKLWNSd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 83 -FFEKSLvkKAFQNTLSDLKLDYLDLYLVHWPQgfqagnallpkdnKGKvllskstFLDAWEAMEELVDQGLVKALGISN 161
Cdd:cd19156 77 qGYESTL--AAFEESLEKLGLDYVDLYLIHWPV-------------KGK-------FKDTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 162 FNHFQIERLLNKpgLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDrpyakpedpvVMEIPKIKEIAAKH 241
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 160415215 242 KKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:cd19156 203 GKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-289 |
1.78e-77 |
|
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: 237.17 E-value: 1.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWATFFEKSLVKK 91
Cdd:cd19132 6 QIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAV----RRSGVPREELFVTTKLPGRHHGYEEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 92 AFQNTLSDLKLDYLDLYLVHWPqgfqagnalLPKDNKgkvllskstFLDAWEAMEELVDQGLVKALGISNFNHFQIERLL 171
Cdd:cd19132 82 TIEESLYRLGLDYVDLYLIHWP---------NPSRDL---------YVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 172 NKPGLKhkPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRpyakpedpvVMEIPKIKEIAAKHKKTVAQVLIR 251
Cdd:cd19132 144 DETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPAQVVLR 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 160415215 252 FHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19132 213 WHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAI 250
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-293 |
2.50e-77 |
|
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: 236.70 E-value: 2.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTWK-SSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWATF 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAI----KKSGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 FEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGfqagnallpkDNKGkvllskstfldAWEAMEELVDQGLVKALGISNFN 163
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG----------DVYG-----------AWRAMEELYKEGKIRAIGVSNFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 164 HFQIERLLnkPGLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSpdrpyakpEDPVVMEIPKIKEIAAKHKK 243
Cdd:cd19133 136 PDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE--------GRNNLFENPVLTEIAEKYGK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 160415215 244 TVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFN 293
Cdd:cd19133 206 SVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-289 |
4.96e-77 |
|
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: 236.78 E-value: 4.96e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 11 AKMPLVGLGTWKSSPG--QVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVK-REDLFIVSKLWATFFEKS 87
Cdd:cd19124 3 QTMPVIGMGTASDPPSpeDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAHPD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 88 LVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNA--------LLPKDNKGkvllskstfldAWEAMEELVDQGLVKALGI 159
Cdd:cd19124 83 LVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFsfpieeedFLPFDIKG-----------VWEAMEECQRLGLTKAIGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 160 SNFNHFQIERLL---NKPglkhkPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAkpeDPVVMEIPKIKE 236
Cdd:cd19124 152 SNFSCKKLQELLsfaTIP-----PAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWG---SNAVMESDVLKE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 160415215 237 IAAKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19124 224 IAAAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKI 276
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-302 |
2.64e-75 |
|
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: 233.22 E-value: 2.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFFEKSLVKK 91
Cdd:cd19114 3 KMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHVRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 92 AFQNTLSDLKLDYLDLYLVHWP--QGFQAGNALLPKDNKGKVL----LSKSTFLDAWEAMEELVDQGLVKALGISNFNHF 165
Cdd:cd19114 83 AFDRQLKDYGLDYIDLYLIHFPipAAYVDPAENYPFLWKDKELkkfpLEQSPMQECWREMEKLVDAGLVRNIGIANFNVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 166 QIERLLNKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSP---DRPYAKPEDPVVMEIPKIKEIAAKHK 242
Cdd:cd19114 163 LILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 243 KTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWRACDLL 302
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPV 300
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-289 |
3.04e-75 |
|
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: 231.91 E-value: 3.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWATFF 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGI----RRSGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 85 EKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagnalLPKDNKGKVllskstflDAWEAMEELVDQGLVKALGISNFNH 164
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWP---------VPNDFDRTI--------QAYKALEKLLAEGRVRAIGVSNFTP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 165 FQIERLLNKPGLKhkPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSP--DRPYAKPEDPVVMEIPKIKEIAAKHK 242
Cdd:cd19127 140 EHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVmrYGASGPTGPGDVLQDPTITGLAEKYG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 160415215 243 KTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19127 218 KTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-289 |
9.90e-75 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 229.84 E-value: 9.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 11 AKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAiqekIKENAVKREDLFIVSKLWATFFEKSLVK 90
Cdd:cd19140 6 VRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEA----IAASGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 91 KAFQNTLSDLKLDYLDLYLVHWPqgfqagNALLPkdnkgkvllskstFLDAWEAMEELVDQGLVKALGISNFNHFQIERL 170
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWP------NKDVP-------------LAETLGALNEAQEAGLARHIGVSNFTVALLREA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 171 LNKPGLkhKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGspdrpyakpeDPVVMEIPKIKEIAAKHKKTVAQVLI 250
Cdd:cd19140 143 VELSEA--PLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA----------RGEVLKDPVLQEIGRKHGKTPAQVAL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 160415215 251 RFHVQR-NVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19140 211 RWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-294 |
1.25e-74 |
|
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: 231.23 E-value: 1.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTWksSP----GQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLW 80
Cdd:cd19119 4 FKLNTGASIPALGLGTA--SPhedrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 81 ATFFEKslVKKAFQNTLSDLKLDYLDLYLVHWPQGFQA-----GNALLPKDNKGKVLLSKST-FLDAWEAMEELVDQGLV 154
Cdd:cd19119 82 PTFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEKdsddsGKPFTPVNDDGKTRYAASGdHITTYKQLEKIYLDGRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 155 KALGISNFNHFQIERLLNKpgLKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPyakpedpvVMEIPKI 234
Cdd:cd19119 160 KAIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 235 KEIAAKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVfdFQLSEEDMAAILSFNR 294
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-289 |
1.38e-72 |
|
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: 225.80 E-value: 1.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 13 MPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKENAVKREDLFIVSKLWATFFEKSLVKKA 92
Cdd:cd19129 6 IPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERVKPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 93 FQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPKDNKGKVLLSKS-TFLDAWEAMEELVDQGLVKALGISNFNHFQIERLL 171
Cdd:cd19129 86 FEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDGvTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 172 NKPGLkhKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPyaKP-EDPVvmeipkIKEIAAKHKKTVAQVLI 250
Cdd:cd19129 166 EAARI--KPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEP--KLlEDPV------ITAIARRVNKTPAQVLL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 160415215 251 RFHVQRNVVVIPKSVTPSRIQENlqvFDFQ-LSEEDMAAI 289
Cdd:cd19129 236 AWAIQRGTALLTTSKTPSRIREN---FDIStLPEDAMREI 272
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-289 |
9.67e-71 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 220.18 E-value: 9.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGT---WKSSPG-----QVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWatf 83
Cdd:cd19120 3 KIPAIAFGTgtaWYKSGDddiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEAL----KESGVPREDLFITTKVS--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 feKSL--VKKAFQNTLSDLKLDYLDLYLVHWPqgFQAGNallpkdnkgkvllSKSTFLDAWEAMEELVDQGLVKALGISN 161
Cdd:cd19120 76 --PGIkdPREALRKSLAKLGVDYVDLYLIHSP--FFAKE-------------GGPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 162 FNHFQIERLLNKPglKHKPVTNQIESHPYLT--QEKLIQYCQSKGIAVTAYSPLGSPDRPYAKPEDPVVmeipkiKEIAA 239
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPLTRDAGGPLDPVL------EKIAE 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 160415215 240 KHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19120 211 KYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEI 260
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-289 |
8.11e-70 |
|
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: 218.65 E-value: 8.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 7 LSTKAKMPLVGLGTWKS--SPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEKIKEN-AVKREDLFIVSKLWATF 83
Cdd:cd19122 3 LNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 FEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPKDN-KGKVLLSKSTFLD---AWEAMEELVDQGLVKALGI 159
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKLGpDGKYVILKDLTENpepTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 160 SNFNHFQIERLLNKPglKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKPEDpvVMEIPKIKEIAA 239
Cdd:cd19122 163 SNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGER--VSENPTLNEVAE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 160415215 240 KHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDfqLSEEDMAAI 289
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAI 286
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-289 |
1.13e-68 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 215.32 E-value: 1.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 3 TFVELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEkikeNAVKREDLFIVSKLWAT 82
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 83 ffEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagnalLPkdnkgkvllSKSTFLDAWEAMEELVDQGLVKALGISNF 162
Cdd:PRK11565 81 --DHKRPREALEESLKKLQLDYVDLYLMHWP---------VP---------AIDHYVEAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 163 NHFQIERLLNKPGLKhkPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPyakpedpvVMEIPKIKEIAAKHK 242
Cdd:PRK11565 141 QIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG--------VFDQKVIRDLADKYG 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 160415215 243 KTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 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 |
9.98e-66 |
|
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: 207.07 E-value: 9.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 13 MPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWATFFEKSLVKKA 92
Cdd:cd19130 10 IPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDRHDGDEPAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 93 FQNTLSDLKLDYLDLYLVHWPqgfqagnalLPkdnkgkvllSKSTFLDAWEAMEELVDQGLVKALGISNFNHFQIERLLN 172
Cdd:cd19130 86 FAESLAKLGLDQVDLYLVHWP---------TP---------AAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 173 KPGLKhkPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDrpyakpedpvVMEIPKIKEIAAKHKKTVAQVLIRF 252
Cdd:cd19130 148 ATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK----------LLGDPPVGAIAAAHGKTPAQIVLRW 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 160415215 253 HVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFN 293
Cdd:cd19130 216 HLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-289 |
4.42e-62 |
|
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: 197.58 E-value: 4.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 13 MPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEkikeNAVKREDLFIVSKLWATFFEKSLVKKA 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 93 FQNTLSDLKLDYLDLYLVHWPQgfqagnallPKDNkgkvlLSKSTFLdawEAMEELVDQGLVKALGISNFNHFQIERLLN 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPS---------PNDE-----VPVEEYI---GALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 173 KPGlKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGspdrpYAKpedpvVMEIPKIKEIAAKHKKTVAQVLIRF 252
Cdd:cd19139 140 VVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA-----YGK-----VLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 160415215 253 HVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAI 245
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-289 |
3.33e-56 |
|
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: 183.67 E-value: 3.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTW-------KSSPGQVKEAVKAAIDAGYRHIDCAYVYH---NENEVGEAIQEKikenAVKREDLFIVSKL------ 79
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 80 WATFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagNALLPkdnkgkvllskstFLDAWEAMEELVDQGLVKALGI 159
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP------DPDTP-------------IEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 160 SNFNHFQIERLLNKPglKHKPVTNQIESHPY--LTQEKLIQYCQSKGIAVTAYSPLGS--------PDRPYAKPEDPVVM 229
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytRDPDKGPGERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160415215 230 ---------EIPKIKEIAAKHKKTVAQVLIRFHVQ--RNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:pfam00248 216 kkgtplnleALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-289 |
6.72e-56 |
|
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: 182.04 E-value: 6.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 10 KAKMPLVGLGTWKSSPGQVK---------EAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEkikenaVKREDLFIVS 77
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKdysddkkaiEALRYAIELGINLIDTAEMYgggHAEELVGKAIKG------FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 78 KLWATFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagNALLPkdnkgkvllskstFLDAWEAMEELVDQGLVKAL 157
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP------NPSIP-------------IEETLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 158 GISNFNHFQIERLLNKPGlKHKPVTNQIESHpYLTQE---KLIQYCQSKGIAVTAYSPLGSPDRPYAKPedpvvmeIPKI 234
Cdd:cd19072 136 GVSNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEKGKLSNAKG-------SPLL 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 160415215 235 KEIAAKHKKTVAQVLIRFHVQR-NVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19072 207 DEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-297 |
1.65e-55 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 180.99 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIQEkikeNAVKREDLFIVSKLWATFFEKSLVKK 91
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 92 AFQNTLSDLKLDYLDLYLVHWPQgfqagnallPKDnkgKVLLSkstfldawEAMEELVD---QGLVKALGISNFNHFQIE 168
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWPS---------PND---EVSVE--------EFMQALLEakkQGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 169 RLLNKPGlKHKPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGspdrpYAKpedpvVMEIPKIKEIAAKHKKTVAQV 248
Cdd:PRK11172 138 QAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA-----YGK-----VLKDPVIARIAAKHNATPAQV 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 160415215 249 LIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNRNWR 297
Cdd:PRK11172 207 ILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-289 |
2.48e-55 |
|
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: 180.82 E-value: 2.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHNENEVGEAIqekiKENAVKREDLFIVSKLWATFF 84
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 85 EKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGfqagnallpkdnkgkvllSKSTFLDAWEAMEELVDQGLVKALGISNFNH 164
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWPAG------------------REGKYVDSWGGLMKLREEGLARSIGVSNFTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 165 FQIERLLNKPGLKhkPVTNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDrpyakpedpvVMEIPKIKEIAAKHKKT 244
Cdd:cd19134 141 EHLENLIDLTFFT--PAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR----------LLDNPAVTAIAAAHGRT 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 160415215 245 VAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-289 |
1.22e-50 |
|
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: 168.58 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 5 VELSTKAKMPLVGLGTW-----KSSPGQVKEAVKAAIDAGYRHIDCAYVYHN---ENEVGEAIQEKikenavkREDLFIV 76
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 77 SKLWATFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagnallpkdnkGKVLLSKsTFldawEAMEELVDQGLVKA 156
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR---------------GGVPLAE-TV----AAMEELKKEGKIRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 157 LGISNFNHFQIERLLNKPGlKHKPVTNQIESHpyLTQE----KLIQYCQSKGIAVTAYSPLGSPDRPyakpeDPVVMEIP 232
Cdd:cd19138 136 WGVSNFDTDDMEELWAVPG-GGNCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLL-----RRGLLENP 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 160415215 233 KIKEIAAKHKKTVAQVLIRFHV-QRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19138 208 TLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-289 |
2.31e-49 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 165.05 E-value: 2.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTWK---------SSPGQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEkikenaVKREDLFIVSKL 79
Cdd:cd19137 3 KIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 80 WATFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagNALLPkdnkgkvllskstFLDAWEAMEELVDQGLVKALGI 159
Cdd:cd19137 77 WPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP------NPNIP-------------LEETLSAMAEGVRQGLIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 160 SNFNHFQIERLLNKpgLKHKPVTNQIESHPY---LTQEKLIQYCQSKGIAVTAYSPLgspDRPYAKPEDPVvmeipkiKE 236
Cdd:cd19137 138 SNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL---RRGLEKTNRTL-------EE 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 160415215 237 IAAKHKKTVAQVLIRFHVQR-NVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19137 206 IAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
16-289 |
1.27e-40 |
|
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: 143.14 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTWK-----------SSPGQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenaVKREDLFIVSKLWA 81
Cdd:cd19093 5 LGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKEL-----GDRDEVVIATKFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 82 TF--FEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLpkdnkgkvllskstfldaWEAMEELVDQGLVKALGI 159
Cdd:cd19093 80 LPwrLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLVRAVGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 160 SNFNHFQIER---LLNKPGlkHKPVTNQIE---SHPYLTQEKLIQYCQSKGIAVTAYSPLG--------SPDRP------ 219
Cdd:cd19093 142 SNYSADQLRRahkALKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPppggrr 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160415215 220 -----YAKPEDPVVMEipKIKEIAAKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19093 220 rlfgrKNLEKVQPLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
16-289 |
2.48e-35 |
|
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: 129.91 E-value: 2.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTW-------KSSPGQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenavKREDLFIVSKLWATFFE 85
Cdd:COG0667 16 LGLGTMtfggpwgGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIATKVGRRMGP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 86 KSL--------VKKA---------------FQntlsdlkldyldlylVHWPqgfqagNALLPKDnkgkvllskstflDAW 142
Cdd:COG0667 90 GPNgrglsrehIRRAveaslrrlgtdyidlYQ---------------LHRP------DPDTPIE-------------ETL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 143 EAMEELVDQGLVKALGISNFNHFQIERLLNKPGLKHKPVTNQIEshpY--LTQ---EKLIQYCQSKGIAVTAYSPLGS-- 215
Cdd:COG0667 136 GALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAYSPLAGgl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 216 ----PDRPYAKPED---------PVVME-----IPKIKEIAAKHKKTVAQVLIRFHVQR--NVVVIPKSVTPSRIQENLQ 275
Cdd:COG0667 213 ltgkYRRGATFPEGdraatnfvqGYLTErnlalVDALRAIAAEHGVTPAQLALAWLLAQpgVTSVIPGARSPEQLEENLA 292
|
330
....*....|....
gi 160415215 276 VFDFQLSEEDMAAI 289
Cdd:COG0667 293 AADLELSAEDLAAL 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-289 |
4.71e-34 |
|
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: 126.16 E-value: 4.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTW---------KSSPGQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenavkREDLFIVSKLWATF 83
Cdd:cd19085 4 LGLGCWqfgggywwgDQDDEESIATIHAALDAGINFFDTAEAYgdgHSEEVLGKALKGR-------RDDVVIATKVSPDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 FEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagnallpkdnkgkvlLSKSTFLDAWEAMEELVDQGLVKALGISNFN 163
Cdd:cd19085 77 LTPEDVRKSCERSLKRLGTDYIDLYQIHWP-------------------SSDVPLEETMEALEKLKEEGKIRAIGVSNFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 164 HFQIERLLnKPGlkhKPVTNQIeshPY-LTQ---EK-LIQYCQSKGIAVTAYSPL------GSPDRPYAKPED------P 226
Cdd:cd19085 138 PAQLEEAL-DAG---RIDSNQL---PYnLLWraiEYeILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlF 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160415215 227 VVME----------IPKIKEIAAKHKKTVAQVLIRFHVQRNVV--VIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19085 211 RHFEpgaeeetfeaLEKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
16-289 |
1.10e-32 |
|
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: 122.63 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTW--------KSSPGQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenavkREDLFIVSK---LW- 80
Cdd:cd19084 7 IGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYgfgHSEEILGKALKGR-------RDDVVIATKcglRWd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 81 -ATFFEKSL----VKKAFQNTLSDLKLDYLDLYLVHWPQGfqagnallpkdnkgkvllsKSTFLDAWEAMEELVDQGLVK 155
Cdd:cd19084 80 gGKGVTKDLspesIRKEVEQSLRRLQTDYIDLYQIHWPDP-------------------NTPIEETAEALEKLKKEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 156 ALGISNFNHFQIERLLNkpglKHKPVTNQIeshPY--LTQ---EKLIQYCQSKGIAVTAYSPLG---------------- 214
Cdd:cd19084 141 YIGVSNFSVEQLEEARK----YGPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAqglltgkykkeptfpp 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 215 ----SPDRPYAKPEDPVVMEI-PKIKEIAAKHKKTVAQVLIRFHVQRN--VVVIPKSVTPSRIQENLQVFDFQLSEEDMA 287
Cdd:cd19084 214 ddrrSRFPFFRGENFEKNLEIvDKLKEIAEKYGKSLAQLAIAWTLAQPgvTSAIVGAKNPEQLEENAGALDWELTEEELK 293
|
..
gi 160415215 288 AI 289
Cdd:cd19084 294 EI 295
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-289 |
1.29e-26 |
|
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: 106.22 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTWKSSPGQ------------VKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenavkREDLFIVSK-- 78
Cdd:cd19102 4 IGLGTWAIGGGGwgggwgpqddrdSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 79 -LWA------TFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagnalLPKDNkgkvllskstFLDAWEAMEELVDQ 151
Cdd:cd19102 77 lLWDeegrirRSLKPASIRAECEASLRRLGVDVIDLYQIHWP---------DPDEP----------IEEAWGALAELKEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 152 GLVKALGISNFNHFQIERLlnkpgLKHKPVT-NQIeshPY--LTQE---KLIQYCQSKGIAVTAYSPLGS--------PD 217
Cdd:cd19102 138 GKVRAIGVSNFSVDQMKRC-----QAIHPIAsLQP---PYslLRRGieaEILPFCAEHGIGVIVYSPMQSglltgkmtPE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 218 RPYAKPED------PVVME---------IPKIKEIAAKHKKTVAQVLIRFHVQRNVV--VIPKSVTPSRIQENLQVFDFQ 280
Cdd:cd19102 210 RVASLPADdwrrrsPFFQEpnlarnlalVDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLR 289
|
....*....
gi 160415215 281 LSEEDMAAI 289
Cdd:cd19102 290 LTPEELAEI 298
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
17-285 |
1.28e-25 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 103.69 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 17 GLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHN---ENEVGEAIqekiKENAVKREDLFIVSKLwatffekslvkkaf 93
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYGGytcEALFGEAL----KLSPSLREKIELQTKC-------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 94 qntlsdlkldyldlylvhwpqGFQAGNAllPKDNKGK--------------------------VLL--SKSTFLDAWE-- 143
Cdd:COG4989 84 ---------------------GIRLPSE--ARDNRVKhydtskehiiasvegslrrlgtdyldLLLlhRPDPLMDPEEva 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 144 -AMEELVDQGLVKALGISNFNHFQIErLLNKpGLKHKPVTNQIE---SHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDrp 219
Cdd:COG4989 141 eAFDELKASGKVRHFGVSNFTPSQFE-LLQS-ALDQPLVTNQIElslLHTDAFDDGTLDYCQLNGITPMAWSPLAGGR-- 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 220 YAKPEDPVVMEI-PKIKEIAAKHKKTVAQVLIRF---HVQRNVVVIpKSVTPSRIQENLQVFDFQLSEED 285
Cdd:COG4989 217 LFGGFDEQFPRLrAALDELAEKYGVSPEAIALAWllrHPAGIQPVI-GTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
17-285 |
2.20e-23 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 97.24 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 17 GLGTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHN---ENEVGEAIqekiKENAVKREDLFIVSKlwatffekSLVKKAF 93
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEAL----ALNPGLREKIEIQTK--------CGIRLGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 94 QNTLsdlkldyldlylvHWPQGF--------QAGNALLPKDNKGKV---LLSK-STFLDAWE---AMEELVDQGLVKALG 158
Cdd:cd19092 83 DPRP-------------GRIKHYdtskehilASVEGSLKRLGTDYLdllLLHRpDPLMDPEEvaeAFDELVKSGKVRYFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 159 ISNFNHFQIErLLNKpGLKHKPVTNQIE---SHPYLTQEKLIQYCQSKGIAVTAYSPLGSpDRpYAKPEDPVVMEIPK-I 234
Cdd:cd19092 150 VSNFTPSQIE-LLQS-YLDQPLVTNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLGG-GR-LFGGFDERFQRLRAaL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 160415215 235 KEIAAKHKKTVAQVLIRF---HVQRNVVVIpKSVTPSRIQENLQVFDFQLSEED 285
Cdd:cd19092 226 EELAEEYGVTIEAIALAWllrHPARIQPIL-GTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-275 |
1.14e-21 |
|
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: 91.43 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTWK-SSPGQVKEA---VKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenaVKREDLFIVSKLWATF----- 83
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAfalLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPggdps 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 ------------FEKSLvkKA--------FqntlsdlkldyldlyLVHWPqgfqagNALLPKDnkgkvllskstflDAWE 143
Cdd:cd06660 78 rsrlspehirrdLEESL--RRlgtdyidlY---------------YLHRD------DPSTPVE-------------ETLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 144 AMEELVDQGLVKALGISNFNHFQIERLLNKPGLKHK--PVTNQIE-S--HPYLTQEKLIQYCQSKGIAVTAYSPLGSpdr 218
Cdd:cd06660 122 ALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLpgFAAVQPQySllDRSPMEEELLDWAEENGLPLLAYSPLAR--- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 160415215 219 pyakpedpvvmeipkikeiaakhkkTVAQVLIRFHVQR--NVVVIPKSVTPSRIQENLQ 275
Cdd:cd06660 199 -------------------------GPAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
29-291 |
1.75e-20 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 89.79 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 29 KEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenavKREDLFIVSKLWATFFEKSLV--------KKAFQNTL 97
Cdd:cd19083 36 KDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKFGGDGSVlnnspeflRSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 98 SDLKLDYLDLYLVHWPQGFqagnalLPKDnkgkvllskstflDAWEAMEELVDQGLVKALGISNFNHFQIERlLNKPGLk 177
Cdd:cd19083 110 KRLNTDYIDLYYIHFPDGE------TPKA-------------EAVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDGY- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 178 hkpvTNQIESHPYLTQ----EKLIQYCQSKGIAVTAYSPL------GSPDRPYAKPEDPVVMEIP--------------- 232
Cdd:cd19083 169 ----VDVLQGEYNLLQreaeEDILPYCVENNISFIPYFPLasgllaGKYTKDTKFPDNDLRNDKPlfkgerfsenldkvd 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160415215 233 KIKEIAAKHKKTVAQVLIRFHVQRNVV--VIPKSVTPSRIQENLQVFDFQLSEEDMAAILS 291
Cdd:cd19083 245 KLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-282 |
1.43e-17 |
|
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: 80.72 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 13 MPLVGLGTWKSSP--GQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIqekikenAVKREDLFIVSKL-------- 79
Cdd:cd19088 9 MRLTGPGIWGPPAdrEEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEAL-------HPYPDDVVIATKGglvrtgpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 80 -WATFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagnallpkDNKGkvllsksTFLDAWEAMEELVDQGLVKALG 158
Cdd:cd19088 82 wWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI------------DPKV-------PFEEQLGALAELQDEGLIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 159 ISNFNHFQIERLLNKPGLkhkpVTNQIESHPYLTQ-EKLIQYCQSKGIAVTAYSPLGSpdRPYAKPEDPVvmeipkiKEI 237
Cdd:cd19088 143 LSNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG--GDLAQPGGLL-------AEV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 160415215 238 AAKHKKTVAQVLIRFHVQR--NVVVIPKSVTPSRIQENLQVFDFQLS 282
Cdd:cd19088 210 AARLGATPAQVALAWLLARspVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
19-289 |
4.42e-17 |
|
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: 79.94 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 19 GTWKSSPGQVKEAVKAAIDAGYRHIDCAYVYHN---ENEVGEAIqekiKENAvKREDLFIVSKLwatFFEKSlvkkafqn 95
Cdd:cd19079 28 RPWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRAL----KEFA-PRDEVVIATKV---YFPMG-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 96 tlsdlkldyldlylvhwPQGFQAGnallpkdnkgkvlLSKSTFLDA--------------------W----------EAM 145
Cdd:cd19079 92 -----------------DGPNGRG-------------LSRKHIMAEvdaslkrlgtdyidlyqihrWdyetpieetlEAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 146 EELVDQGLVKALGISNFNHFQIERLLN---KPGLkHKPVTNQiESHPYLTQE---KLIQYCQSKGIAVTAYSPLGS---- 215
Cdd:cd19079 142 HDVVKSGKVRYIGASSMYAWQFAKALHlaeKNGW-TKFVSMQ-NHYNLLYREeerEMIPLCEEEGIGVIPWSPLARgrla 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 216 -------------PDRPYAK-----PEDPVVMEipKIKEIAAKHKKTVAQVLIRFHVQRNVVVIP--KSVTPSRIQENLQ 275
Cdd:cd19079 220 rpwgdtterrrstTDTAKLKydyftEADKEIVD--RVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVA 297
|
330
....*....|....
gi 160415215 276 VFDFQLSEEDMAAI 289
Cdd:cd19079 298 ALDIKLSEEEIKYL 311
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-289 |
5.79e-15 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 74.47 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTW---KSSPGQVKEAVKAAIDAGYRHIDCAYVYHN-ENEVGEAIQEKikenavkREDLFIVSKL-------- 79
Cdd:COG1453 12 EVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKGP-------RDKVILATKLppwvrdpe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 80 -WATFFEKSLvkKAFQ----NtlsdlkldyldLYLVHwpqgfqagnALLPKDNKGKVLLSkstfLDAWEAMEELVDQGLV 154
Cdd:COG1453 85 dMRKDLEESL--KRLQtdyiD-----------LYLIH---------GLNTEEDLEKVLKP----GGALEALEKAKAEGKI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 155 KALGISnfNHFQIERLLnkpglkhkpvtNQIESHP---------YLTQ-----EKLIQYCQSKGIAVTAYSPL--GspdR 218
Cdd:COG1453 139 RHIGFS--THGSLEVIK-----------EAIDTGDfdfvqlqynYLDQdnqagEEALEAAAEKGIGVIIMKPLkgG---R 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160415215 219 PYAKPEDpvVMEIpkikeiaAKHKKTVAQVLIRFhVQ---RNVVVIPKSVTPSRIQENLQVFD--FQLSEEDMAAI 289
Cdd:COG1453 203 LANPPEK--LVEL-------LCPPLSPAEWALRF-LLshpEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAIL 268
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
143-289 |
9.05e-15 |
|
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: 73.43 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 143 EAMEELVDQGLVKALGISNFNHFQIERLLNKpglkHKPVTNQIESHPyLTQEKL----IQYCQSKGIAVTAYSPLG---- 214
Cdd:cd19077 132 KALKELVKEGKIRGIGLSEVSAETIRRAHAV----HPIAAVEVEYSL-FSREIEengvLETCAELGIPIIAYSPLGrgll 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 215 -----SPD-------RPYAKPEDPVVME-----IPKIKEIAAKHKKTVAQVLIRFHVQRN---VVVIPKSVTPSRIQENL 274
Cdd:cd19077 207 tgrikSLAdipegdfRRHLDRFNGENFEknlklVDALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENL 286
|
170
....*....|....*
gi 160415215 275 QVFDFQLSEEDMAAI 289
Cdd:cd19077 287 KAANVELTDEELKEI 301
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-291 |
9.15e-15 |
|
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: 73.46 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTWK----SSPGQVKE-----AVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenavkREDLFIVSK---LW 80
Cdd:cd19149 14 IGLGTWAigggPWWGGSDDnesirTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKGR-------RDKVVLATKcglRW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 81 AT----FFEKSLVKKAFQNTLSDLKLDYLDLY------------LVHWPqgfqagnallpkdnkgkvllSKSTFL-DAWE 143
Cdd:cd19149 87 DReggsFFFVRDGVTVYKNLSPESIREEVEQSlkrlgtdyidlyQTHWQ--------------------DVETPIeETME 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 144 AMEELVDQGLVKALGISNFNHFQIERLLNKPGL-----KHKPVTNQIEshpyltqEKLIQYCQSKGIAVTAYSPLGS--- 215
Cdd:cd19149 147 ALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLdiiqeKYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLEQgll 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 216 -----PDR-----------PYAKPED--PVVMEIPKIKEIAAKHKKTVAQVLIR--FHVQRNVVVIPKSVTPSRIQENLQ 275
Cdd:cd19149 220 tgkitPDRefdagdarsgiPWFSPENreKVLALLEKWKPLCEKYGCTLAQLVIAwtLAQPGITSALCGARKPEQAEENAK 299
|
330
....*....|....*.
gi 160415215 276 VFDFQLSEEDMAAILS 291
Cdd:cd19149 300 AGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
16-289 |
1.44e-14 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 72.72 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTWK--------SSPGQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIqekikENAVKREDLFIVSKL---W- 80
Cdd:cd19148 7 IALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKAL-----KEYGKRDRVVIATKVgleWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 81 --------ATffeKSLVKKAFQNTLSDLKLDYLDLYLVHWPQgfqagnallpkdnkgkvllSKSTFLDAWEAMEELVDQG 152
Cdd:cd19148 82 eggevvrnSS---PARIRKEVEDSLRRLQTDYIDLYQVHWPD-------------------PLVPIEETAEALKELLDEG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 153 LVKALGISNFNHFQIERLLNKPGLkH--KPVTNQIESHpylTQEKLIQYCQSKGIAVTAYSPL------GSPDRPYAKPE 224
Cdd:cd19148 140 KIRAIGVSNFSPEQMETFRKVAPL-HtvQPPYNLFERE---IEKDVLPYARKHNIVTLAYGALcrgllsGKMTKDTKFEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 225 DPVVMEIPKIKE------IAA----------KHKKTVAQVLIRFHVQRNVVVIP--KSVTPSRIQENLQVFDFQLSEEDM 286
Cdd:cd19148 216 DDLRRTDPKFQEprfsqyLAAveeldklaqeRYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDM 295
|
...
gi 160415215 287 AAI 289
Cdd:cd19148 296 KEI 298
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
144-289 |
3.91e-14 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 71.71 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 144 AMEELVDQGLVKALGISNFNHFQIERllnkpglKHK--PVTN-QIESHPYLT-----QEKLIQYCQSKGIAVTAYSPLG- 214
Cdd:cd19144 140 AMAELVQEGKIKHIGLSECSAETLRR-------AHAvhPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGr 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 215 --------SPD-------RPYA---KPED-PVVME-IPKIKEIAAKHKKTVAQVLIRFHVQR--NVVVIPKSVTPSRIQE 272
Cdd:cd19144 213 gfltgairSPDdfeegdfRRMAprfQAENfPKNLElVDKIKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRLEE 292
|
170
....*....|....*..
gi 160415215 273 NLQVFDFQLSEEDMAAI 289
Cdd:cd19144 293 NLGALKVKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
138-289 |
9.98e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 70.32 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 138 FLDAWEAMEELVDQGLVKALGISNFNHFQIERLLNKPGlkhKPVTNQ-----IESHPyltQEKLIQYCQSKGIAVTAYSP 212
Cdd:cd19101 121 YLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAGV---PIVSNQvqyslLDRRP---ENGMAALCEDHGIKLLAYGT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 213 LGS---PDRPYAKPEdPVVMEIP-------------------------KIKEIAAKHKKTVAQVLIRFHVQRNVV--VIP 262
Cdd:cd19101 195 LAGgllSEKYLGVPE-PTGPALEtrslqkyklmidewggwdlfqellrTLKAIADKHGVSIANVAVRWVLDQPGVagVIV 273
|
170 180
....*....|....*....|....*..
gi 160415215 263 KSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19101 274 GARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-289 |
1.33e-13 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 69.95 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGT--------WKSSPGQV--KEA---VKAAIDAGYRHIDCAYVYHN---ENEVGEAIQEKikenavkREDLFI 75
Cdd:cd19091 12 KVSELALGTmtfgggggFFGAWGGVdqEEAdrlVDIALDAGINFFDTADVYSEgesEEILGKALKGR-------RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 76 VSKLwatffekslvkkafqntlsdlkldyldlylvhwpqGFQAGNALlpkDNKGkvlLSKSTFLDA-------------- 141
Cdd:cd19091 85 ATKV-----------------------------------RGRMGEGP---NDVG---LSRHHIIRAveaslkrlgtdyid 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 142 ------W----------EAMEELVDQGLVKALGISNFNHFQIERLL---NKPGLKhKPVTNQIeshpYLT------QEKL 196
Cdd:cd19091 124 lyqlhgFdaltpleetlRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHEL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 197 IQYCQSKGIAVTAYSPLG--------SPDRPyaKPED----------PVVME------IPKIKEIAAKHKKTVAQVLIRF 252
Cdd:cd19091 199 MPLALDQGVGLLVWSPLAggllsgkyRRGQP--APEGsrlrrtgfdfPPVDRergydvVDALREIAKETGATPAQVALAW 276
|
330 340 350
....*....|....*....|....*....|....*....
gi 160415215 253 HVQRNVV--VIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19091 277 LLSRPTVssVIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
140-289 |
7.37e-13 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 67.63 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 140 DAWEAMEELVDQGLVKALGISNFNHFQIERllnkpglKHK--PVTN-QIESHPYLT--QEKLIQYCQSKGIAVTAYSPL- 213
Cdd:cd19076 133 ETVGAMAELVEEGKVRYIGLSEASADTIRR-------AHAvhPITAvQSEYSLWTRdiEDEVLPTCRELGIGFVAYSPLg 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 214 -----GSPDRPYAKPEDPVVMEIP---------------KIKEIAAKHKKTVAQ-----VLirfHVQRNVVVIPKSVTPS 268
Cdd:cd19076 206 rgfltGAIKSPEDLPEDDFRRNNPrfqgenfdknlklveKLEAIAAEKGCTPAQlalawVL---AQGDDIVPIPGTKRIK 282
|
170 180
....*....|....*....|.
gi 160415215 269 RIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19076 283 YLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-276 |
8.84e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 66.84 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 9 TKAKMPLVGLGTwKSSPGQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEkikenaVKREDLFIVSKlwatffe 85
Cdd:cd19105 9 TGLKVSRLGFGG-GGLPRESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALKG------LRRDKVFLATK------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 86 kslvkkafqntlsdlkldyldlylVHWPQGFQAGNALLPK--------------------DNKGKVLLSKSTFLdawEAM 145
Cdd:cd19105 75 ------------------------ASPRLDKKDKAELLKSveeslkrlqtdyidiyqlhgVDTPEERLLNEELL---EAL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 146 EELVDQGLVKALGISnfNHFQIERLLNKpglkhkpvtnQIESHPY---------LTQ----EKLIQYCQSKGIAVTAYSP 212
Cdd:cd19105 128 EKLKKEGKVRFIGFS--THDNMAEVLQA----------AIESGWFdvimvaynfLNQpaelEEALAAAAEKGIGVVAMKT 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160415215 213 LGSpdrpyAKPEDPVVMEIPKIKEiaakhkkTVAQVLIRFHVQ-RNV-VVIPKSVTPSRIQENLQV 276
Cdd:cd19105 196 LAG-----GYLQPALLSVLKAKGF-------SLPQAALKWVLSnPRVdTVVPGMRNFAELEENLAA 249
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-278 |
1.24e-11 |
|
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: 63.73 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 14 PLVGLGT------WKSS--PGQVKEAVKAAIDAGYRHIDCAYVYHN---ENEVGEAIQEkikenaVKREDLFIVSKL--W 80
Cdd:cd19096 1 SVLGFGTmrlpesDDDSidEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLppW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 81 AT--------FFEKSLvKK---------AFQNTLSDLkldyldlylvhWPQGFQAGnallpkdnkgkvllskstflDAWE 143
Cdd:cd19096 75 SVksaedfrrILEESL-KRlgvdyidfyLLHGLNSPE-----------WLEKARKG--------------------GLLE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 144 AMEELVDQGLVKALGISnFnHFQIErLLNKpglkhkpvtnQIESHP---------YLTQE-----KLIQYCQSKGIAVTA 209
Cdd:cd19096 123 FLEKAKKEGLIRHIGFS-F-HDSPE-LLKE----------ILDSYDfdfvqlqynYLDQEnqagrPGIEYAAKKGMGVII 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160415215 210 YSPLGSPDRPYAkpedpvvmeIPKIKEIAAKHKKTVAQVLIRFHV-QRNV-VVIPKSVTPSRIQENLQVFD 278
Cdd:cd19096 190 MEPLKGGGLANN---------PPEALAILCGAPLSPAEWALRFLLsHPEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
27-289 |
1.35e-11 |
|
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: 64.18 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 27 QVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIqekikenAVKREDLFIVSKLWATFFEKSLVKKAFQNTlsdlkld 103
Cdd:cd19078 26 EMIELIRKAVELGITFFDTAEVYgpyTNEELVGEAL-------KPFRDQVVIATKFGFKIDGGKPGPLGLDSR------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 104 yldlylvhwPQGF-QAGNALLpkdnkgKVLlsKSTFLDAW---------------EAMEELVDQGLVKALGISNFNHFQI 167
Cdd:cd19078 92 ---------PEHIrKAVEGSL------KRL--QTDYIDLYyqhrvdpnvpieevaGTMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 168 ERllnkpglKHK--PVTnQIES-------HPyltQEKLIQYCQSKGIAVTAYSPLGS--------PDRPYAKPEDPVVMe 230
Cdd:cd19078 155 RR-------AHAvcPVT-AVQSeysmmwrEP---EKEVLPTLEELGIGFVPFSPLGKgfltgkidENTKFDEGDDRASL- 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160415215 231 iPK---------------IKEIAAKHKKTVAQVLIRF--HVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19078 223 -PRftpealeanqalvdlLKEFAEEKGATPAQIALAWllAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
16-284 |
1.39e-11 |
|
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: 64.15 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTWKSSPGQV-----KEAVKAAIDAGYRHIDCAYVYHN---ENEVGEAIQEkikenaVKREDLFIVSKlwatffeks 87
Cdd:cd19074 7 LSLGTWLTFGGQVddedaKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 88 lvkkafqntlsdlkldyldlylVHWPQGfqagnallPKDN-KGkvlLSK---------------STFLDAW--------- 142
Cdd:cd19074 72 ----------------------VFWPTG--------PGPNdRG---LSRkhifesihaslkrlqLDYVDIYychrydpet 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 143 ------EAMEELVDQGLVKALGISNFNHFQIE---RLLNKPGLkHKPVTNQIESHpYLTQEK---LIQYCQSKGIAVTAY 210
Cdd:cd19074 119 pleetvRAMDDLIRQGKILYWGTSEWSAEQIAeahDLARQFGL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVW 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 211 SPLGS-------------PDRPYAKPE-----------DPVVMEIPKIKEIAAKHKKTVAQVLIRFHVQRNVV--VIPKS 264
Cdd:cd19074 197 SPLAQglltgkyrdgippPSRSRATDEdnrdkkrrlltDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVssAIIGA 276
|
330 340
....*....|....*....|
gi 160415215 265 VTPSRIQENLQVFDFQLSEE 284
Cdd:cd19074 277 SRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
143-289 |
1.47e-11 |
|
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: 64.16 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 143 EAMEELVDQGLVKALGISNFNHFQIERLLN---KPGLKhKPVTNQIESHPY---LTQEKLIQYCQSKGIAVTAYSPLGS- 215
Cdd:cd19081 135 GALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGLP-RYVSLQPEYNLVdreSFEGELLPLCREEGIGVIPYSPLAGg 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 216 -------PDRP-------------YAKPEDPVVMEipKIKEIAAKHKKTVAQVLIRFHVQRNVV--VIPKSVTPSRIQEN 273
Cdd:cd19081 214 fltgkyrSEADlpgstrrgeaakrYLNERGLRILD--ALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDL 291
|
170
....*....|....*.
gi 160415215 274 LQVFDFQLSEEDMAAI 289
Cdd:cd19081 292 LAAAGLRLTDEEVARL 307
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-215 |
2.87e-11 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 62.49 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTW--------KSSPGQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenavkREDLFIVSKL----- 79
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVVIATKFgnrfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 80 ----WATFFEKSLVKKA---------------FQntlsdlkldyldlylVH-WPQgfqagnALLPKDnkgkvllskstfl 139
Cdd:cd19086 79 ggpeRPQDFSPEYIREAveaslkrlgtdyidlYQ---------------LHnPPD------EVLDND------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 140 DAWEAMEELVDQGLVKALGISnfnhfqIERLLN-KPGLKHKPVT------NQIESHPYltqEKLIQYCQSKGIAVTAYSP 212
Cdd:cd19086 125 ELFEALEKLKQEGKIRAYGVS------VGDPEEaLAALRRGGIDvvqviyNLLDQRPE---EELFPLAEEHGVGVIARVP 195
|
...
gi 160415215 213 LGS 215
Cdd:cd19086 196 LAS 198
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
110-289 |
3.57e-11 |
|
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: 62.97 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 110 VHWPQ----GFQAGNALLPKDNKGKVllsksTFLDAWEAMEELVDQGLVKALGISNFNHFQIERLLN---KPGLKhKPVT 182
Cdd:cd19094 119 LHWPDrytpLFGGGYYTEPSEEEDSV-----SFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLElaeQLGLP-RIVS 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 183 NQiesHPY--LTQ---EKLIQYCQSKGIAVTAYSPLG----------SPDRP--------------YAKPedPVVMEIPK 233
Cdd:cd19094 193 IQ---NPYslLNRnfeEGLAEACHRENVGLLAYSPLAggvltgkyldGAARPeggrlnlfpgymarYRSP--QALEAVAE 267
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 160415215 234 IKEIAAKHKKTVAQVLIRFHVQRNVV--VIPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19094 268 YVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELLAEI 325
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
16-284 |
4.16e-11 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 62.57 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGT------WKS-SPGQVKEAVKAAIDAGYRHIDCAYVYHN-ENEVGEAIQEkikenaVKREDLFIVSKL-----WAT 82
Cdd:cd19090 3 LGLGTaglggvFGGvDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 83 FFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPkdnkGKVLlskstfldawEAMEELVDQGLVKALGISNF 162
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP----GGAL----------EALLELKEEGLIKHIGLGGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 163 NHFQIERLLNkpglkhkpvTNQIE---SHPYLT------QEKLIQYCQSKGIAVTAYSPLGS-------PDRPYAKPEDP 226
Cdd:cd19090 143 PPDLLRRAIE---------TGDFDvvlTANRYTlldqsaADELLPAAARHGVGVINASPLGMgllagrpPERVRYTYRWL 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160415215 227 VVMEIP---KIKEIAAKHKKTVAQVLIRFhVQRN-----VVVIPKSvtPSRIQENLQVFDFQLSEE 284
Cdd:cd19090 214 SPELLDrakRLYELCDEHGVPLPALALRF-LLRDpristVLVGASS--PEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-226 |
6.07e-11 |
|
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: 61.34 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 8 STKAKMPLVGLGT---WKSSPGQVKEAVKAAIDAGYRHIDCAYVYHN-ENEVGEAIQEKikenavkREDLFIVSKLWATF 83
Cdd:cd19100 6 RTGLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGARD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 FEKslVKKAFQNTLSDLKLDYLDLYLVHwpqgfqagnALLPKDNKGKVLLSKStfldAWEAMEELVDQGLVKALGISNFN 163
Cdd:cd19100 79 YEG--AKRDLERSLKRLGTDYIDLYQLH---------AVDTEEDLDQVFGPGG----ALEALLEAKEEGKIRFIGISGHS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160415215 164 HFQIERLLNKPGLK--HKPVtNQIESHPYLTQEKLIQYCQSKGIAVTAYSPLGSPDRPYAKPEDP 226
Cdd:cd19100 144 PEVLLRALETGEFDvvLFPI-NPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP 207
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-252 |
3.81e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 60.02 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTWKSSPG-----QVKEAVKAAIDAGYRHIDCAYVYHN---ENEVGEAIQEKIKENAVKREDLFIVSKlwATF---- 83
Cdd:cd19099 6 LGLGTYRGDSDdetdeEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTK--AGYipgd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 FEKSLVKKAFQNTLSDLKLDYLDLYLVHW----PQGFQAgnAL-----------------------LPKDNKGKVLlskS 136
Cdd:cd19099 84 GDEPLRPLKYLEEKLGRGLIDVADSAGLRhcisPAYLED--QIerslkrlgldtidlyllhnpeeqLLELGEEEFY---D 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 137 TFLDAWEAMEELVDQGLVKALGISNFN----------HFQIERLL--------NKPGLKH--KPVtNQIES----HPYLT 192
Cdd:cd19099 159 RLEEAFEALEEAVAEGKIRYYGISTWDgfrappalpgHLSLEKLVaaaeevggDNHHFKViqLPL-NLLEPealtEKNTV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160415215 193 QEK---LIQYCQSKGIAVTAYSPLGSPDrpyakpedpVVMEIPKIKEIAAKHKKTVAQVLIRF 252
Cdd:cd19099 238 KGEalsLLEAAKELGLGVIASRPLNQGQ---------LLGELRLADLLALPGGATLAQRALQF 291
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-289 |
5.96e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 59.27 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTW---------------KSSPGQVKEAVKAAIDAGYRHIDCAYVYhnenevGEAIQEKIKENAVK---REDL 73
Cdd:cd19103 3 KLPKIALGTWswgsggaggdqvfgnHLDEDTLKAVFDKAMAAGLNLWDTAAVY------GMGASEKILGEFLKrypREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 74 FIVSKLWATFFEKSL--VKKAFQNTLSDLKLDYLDLYLVHWPqgfqagnALLPKDNKGKVLLSKStfldaweameelvdq 151
Cdd:cd19103 77 IISTKFTPQIAGQSAdpVADMLEGSLARLGTDYIDIYWIHNP-------ADVERWTPELIPLLKS--------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 152 GLVKALGISNFNHFQIER---LLNKPGLKHKPVTNQIeSHPYLTQEK--LIQYCQSKGIAVTAYSPL------GSPDRPY 220
Cdd:cd19103 135 GKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQNHY-SLLYRSSEEagILDYCKENGITFFAYMVLeqgalsGKYDTKH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 221 AKPED--------PVVMEI----PKIKEIAAKHKKTVAQVLIRFHVQRNVVVIPKSVTPSRIQENLQVFDFQLSEEDMAA 288
Cdd:cd19103 214 PLPEGsgraetynPLLPQLeeltAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKE 293
|
.
gi 160415215 289 I 289
Cdd:cd19103 294 L 294
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
16-276 |
1.75e-09 |
|
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: 57.24 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 16 VGLGTWK-------SSPGQVKEAVKAAIDAGYRHIDCAYVYHN-ENEVGEAIQEkikenaVKREDLFIVSKLWATF---- 83
Cdd:cd19095 3 LGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGTHGeggr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 84 -------------FEKSLVK------KAFQntlsdlkldyldlylVHWPQgfqagnallPKDNKGKVLlskstfldawEA 144
Cdd:cd19095 77 drkdfspaairasIERSLRRlgtdyiDLLQ---------------LHGPS---------DDELTGEVL----------ET 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 145 MEELVDQGLVKALGISNFNHfQIERLLNKPGLKhkpvTNQIESHPYLTQEK-LIQYCQSKGIAVTAYSPLGSPDRPYAKP 223
Cdd:cd19095 123 LEDLKAAGKVRYIGVSGDGE-ELEAAIASGVFD----VVQLPYNVLDREEEeLLPLAAEAGLGVIVNRPLANGRLRRRVR 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 160415215 224 EDPVVMEIPKIKEIAAKHK-KTVAQVLIRFHVQRNVV--VIPKSVTPSRIQENLQV 276
Cdd:cd19095 198 RRPLYADYARRPEFAAEIGgATWAQAALRFVLSHPGVssAIVGTTNPEHLEENLAA 253
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-289 |
2.54e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 51.50 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 19 GTW-KSSPGQVKEAVKAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenavkREDLFIVSKL---------WATFFE 85
Cdd:cd19104 24 GLMgRTTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVrldpddlgdIGGQIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 86 KSlVKKAFQNTLSDLKLDyldlylvhwpqgFQAGNALLPKDNKGK-VLLSKSTFL---DAWEAMEELVDQGLVKALGISN 161
Cdd:cd19104 97 RS-VEKSLKRLKRDSVDL------------LQLHNRIGDERDKPVgGTLSTTDVLglgGVADAFERLRSEGKIRFIGITG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 162 FNHFQ-----IER-----------LLNKP-GLKHKPvtnqieSHPYLTQEKLIQYCQSKGIAVTAYSPL------GSPDR 218
Cdd:cd19104 164 LGNPPairelLDSgkfdavqvyynLLNPSaAEARPR------GWSAQDYGGIIDAAAEHGVGVMGIRVLaagaltTSLDR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 219 PyakPEDPVVMEIP---------KIKEIAAKHKKTVAQVLIRFHVQRNVV--VIPKSVTPSRIQENLQVFDF-QLSEEDM 286
Cdd:cd19104 238 G---REAPPTSDSDvaidfrraaAFRALAREWGETLAQLAHRFALSNPGVstVLVGVKNREELEEAVAAEAAgPLPAENL 314
|
...
gi 160415215 287 AAI 289
Cdd:cd19104 315 ARL 317
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
144-289 |
2.65e-07 |
|
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: 51.07 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 144 AMEELVDQGLVKALGISNFNHFQIERLLNKPGLKHK--PVTNQIESHpyLTQ----EKLIQYCQSKGIAVTAYSPLGS-- 215
Cdd:cd19080 135 ALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWspFVALQIEYS--LLErtpeRELLPMARALGLGVTPWSPLGGgl 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 216 -----------------PDRPYAKPEDPVVMEI-PKIKEIAAKHKKTVAQVLIRFHVQRNVVVIP--KSVTPSRIQENLQ 275
Cdd:cd19080 213 ltgkyqrgeegrageakGVTVGFGKLTERNWAIvDVVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLG 292
|
170
....*....|....
gi 160415215 276 VFDFQLSEEDMAAI 289
Cdd:cd19080 293 ALDLTLSPEQLARL 306
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-275 |
3.20e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 50.79 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 36 IDAGYRHIDCA--YVYHNENEVG---EA-IQEKIKENAVkREDLFIVSKL---------WATFFE---KSLVKKAFQNTL 97
Cdd:cd19752 27 VAAGGNFLDTAnnYAFWTEGGVGgesERlIGRWLKDRGN-RDDVVIATKVgagprdpdgGPESPEglsAETIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 98 SDLKLDYLDLYLVHwpqgfqagnallpKDNKGKVLlskSTFLdawEAMEELVDQGLVKALGISNFNHFQIER---LLNKP 174
Cdd:cd19752 106 RRLGTDYIDLYYAH-------------VDDRDTPL---EETL---EAFNELVKAGKVRAIGASNFAAWRLERarqIARQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 175 GLkHKPVTNQiESHPYL--------------TQEkLIQYCQSKG-IAVTAYSPL-----GSPDRP----YAKPEDPVVME 230
Cdd:cd19752 167 GW-AEFSAIQ-QRHSYLrprpgadfgvqrivTDE-LLDYASSRPdLTLLAYSPLlsgayTRPDRPlpeqYDGPDSDARLA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 160415215 231 ipKIKEIAAKHKKTVAQVLIRFHVQRNVVVIP--KSVTPSRIQENLQ 275
Cdd:cd19752 244 --VLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-252 |
1.14e-06 |
|
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: 49.06 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 17 GLGTW-------------KSSPGQVKEAVKAAIDAGYRHIDCAYVYhnenevGEAiQEKIKENAVKREDLFIVSKL---- 79
Cdd:cd19097 4 ALGTAqfgldygianksgKPSEKEAKKILEYALKAGINTLDTAPAY------GDS-EKVLGKFLKRLDKFKIITKLpplk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 80 WATFFEKSLVKKAFQNTLSDLKLDYLDLYLVHWPqgfqagnALLPKDNKgkvllskstflDAWEAMEELVDQGLVKALGI 159
Cdd:cd19097 77 EDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNP-------DDLLKHGG-----------KLVEALLELKKEGLIRKIGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 160 SNFNHFQIERLLNKPGLKHkpVtnQIeshPY------LTQEKLIQYCQSKGIAVTAYSP------LGSPDRP--YAKPED 225
Cdd:cd19097 139 SVYSPEELEKALESFKIDI--I--QL---PFnildqrFLKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLpaKFAPAK 211
|
250 260
....*....|....*....|....*..
gi 160415215 226 PVVMeipKIKEIAAKHKKTVAQVLIRF 252
Cdd:cd19097 212 PLLK---KLHELAKKLGLSPLELALGF 235
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
33-289 |
2.72e-06 |
|
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: 47.95 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 33 KAAIDAGYRHIDCAYVY---HNENEVGEAIQEKikenavkREDLFIVSKlwatFFEK----------SL--VKKAFQNTL 97
Cdd:cd19087 37 DRALDAGINFFDTADVYgggRSEEIIGRWIAGR-------RDDIVLATK----VFGPmgddpndrglSRrhIRRAVEASL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 98 SDLKLDYLDLYLVHWPqgfqagnallpkdnkgkvlLSKSTFLDAWEAMEELVDQGLVKALGISNFNHFQIERLLN---KP 174
Cdd:cd19087 106 RRLQTDYIDLYQMHHF-------------------DRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaaRR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 175 GLKH----KPVTN----QIESHpyltqekLIQYCQSKGIAVTAYSPLG--------------------SPDRPYAKPEDP 226
Cdd:cd19087 167 GLLRfvseQPMYNllkrQAELE-------ILPAARAYGLGVIPYSPLAgglltgkygkgkrpesgrlvERARYQARYGLE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160415215 227 VVME-IPKIKEIAAKHKKTVAQVLIRFhVQRNVVV---IPKSVTPSRIQENLQVFDFQLSEEDMAAI 289
Cdd:cd19087 240 EYRDiAERFEALAAEAGLTPASLALAW-VLSHPAVtspIIGPRTLEQLEDSLAALEITLTPELLAEI 305
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
144-289 |
4.32e-06 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 47.43 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 144 AMEELVDQGLVKALGISNFNHFQIERllnkpglKH--KPVTN-QIESHPYL--TQEKLIQYCQSKGIAVTAYSPLGspdR 218
Cdd:cd19145 138 ELKKLVEEGKIKYIGLSEASADTIRR-------AHavHPITAvQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLG---R 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 219 PY--AKP-------EDPVVMEIP---------------KIKEIAAKHKKTVAQV-LIRFHVQRN-VVVIPKSVTPSRIQE 272
Cdd:cd19145 208 GFfaGKAkleelleNSDVRKSHPrfqgenleknkvlyeRVEALAKKKGCTPAQLaLAWVLHQGEdVVPIPGTTKIKNLNQ 287
|
170
....*....|....*..
gi 160415215 273 NLQVFDFQLSEEDMAAI 289
Cdd:cd19145 288 NIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-279 |
5.15e-06 |
|
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: 47.22 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 14 PLVGLGT-------WKSSPGQVKEAVKAAIDAGYRHIDCAYVYHN---ENEVGEAIQEKIKENAV-------KREDLFIV 76
Cdd:cd19152 1 PKLGFGTaplgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRELGREDYVistkvgrLLVPLQEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 77 SKLWATFFEKSL------------VKKAFQNTLSDLKLDYLDLYLVHWPQGFQAGNALLPK-DNKGKvllskstflDAWE 143
Cdd:cd19152 81 EPTFEPGFWNPLpfdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHfAQAIK---------GAFR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 144 AMEELVDQGLVKALGI--------------SNFNHFQIER---LLNKPGLKhkpvtnqieshpyltqeKLIQYCQSKGIA 206
Cdd:cd19152 152 ALEELREEGVIKAIGLgvndwevilrileeADLDWVMLAGrytLLDHSAAR-----------------ELLPECEKRGVK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 207 VTAYSPLGS---------PDRPYAKPEDPVVMEIPKIKEIAAKHKKTVAQVLIRFHVQRNVV--VIPKSVTPSRIQENLQ 275
Cdd:cd19152 215 VVNAGPFNSgflaggdnfDYYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVA 294
|
....
gi 160415215 276 VFDF 279
Cdd:cd19152 295 LLAT 298
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
140-274 |
2.41e-05 |
|
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: 45.04 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 140 DAWEAMEELVDQGLVKALGISNFNHFQIERLLNKPGLKHKPVTNqieSHPYLTQE---KLIQYCQSKGIAVTAYSPLGS- 215
Cdd:cd19162 129 DAFPALEELRAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAG---RYTLLDRRaatELLPLCAAKGVAVVAAGVFNSg 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160415215 216 --------PDR-PYAKPEDPVVMEIPKIKEIAAKHKKTVAQVLIRFHVQ----RNVVVIPKSvtPSRIQENL 274
Cdd:cd19162 206 ilatddpaGDRyDYRPATPEVLARARRLAAVCRRYGVPLPAAALQFPLRhpavASVVVGAAS--PAELRDNL 275
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
143-287 |
6.90e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 43.80 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 143 EAMEELVDQGLVKALGISNFNHFQIER---------LLNKPGLKHKpvtnqieshpylTQEKLIQYCQSKGIAVTAYSPL 213
Cdd:PRK10376 148 TVLAELQRQGLVRHIGLSNVTPTQVAEarkiaeivcVQNHYNLAHR------------ADDALIDALARDGIAYVPFFPL 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160415215 214 G--SPdrpyakpedpvvMEIPKIKEIAAKHKKTVAQVLIRFHVQR--NVVVIPKSVTPSRIQENLQVFDFQLSEEDMA 287
Cdd:PRK10376 216 GgfTP------------LQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLA 281
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
12-287 |
1.59e-04 |
|
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: 42.63 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 12 KMPLVGLGTWK-----SSPGQVKEAVKAAIDAGYRHIDCAYVY-----HNENEVGEAIQEKIKEnavKREDLFIVSKlwa 81
Cdd:cd19089 10 HLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDLRP---YRDELVISTK--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 82 tffekslvkkafqntlsdlkldyldlylvhwpqgfqAGNALLPKDNKG----KVLLS------KSTFLD----------- 140
Cdd:cd19089 84 ------------------------------------AGYGMWPGPYGDggsrKYLLAsldqslKRMGLDyvdifyhhryd 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 141 -------AWEAMEELVDQGlvKAL--GISNFNHFQIER---LLNKpgLKHKPVTNQIeSHPYLTQ---EKLIQYCQSKGI 205
Cdd:cd19089 128 pdtpleeTMTALADAVRSG--KALyvGISNYPGAKARRaiaLLRE--LGVPLIIHQP-RYSLLDRwaeDGLLEVLEEAGI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 206 AVTAYSPL-----------GSPDRPYAKPED----------PVVMEIPKIKEIAAKHKKTVAQVLIRFHVQRNVV--VIP 262
Cdd:cd19089 203 GFIAFSPLaqglltdkylnGIPPDSRRAAESkflteealtpEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVtsVLI 282
|
330 340
....*....|....*....|....*.
gi 160415215 263 KSVTPSRIQENLQVFD-FQLSEEDMA 287
Cdd:cd19089 283 GASSPSQLEDNVAALKnLDFSEEELA 308
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
109-294 |
5.45e-04 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 41.38 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 109 LVHWPQgfqagnalLPKDNKGKVLLSKS------TFLDAWEAMEELVDQGLVKALGISNFNHFQIERLLNKPGlKH---K 179
Cdd:PRK10625 130 QVHWPQ--------RPTNCFGKLGYSWTdsapavSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAE-KHdlpR 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160415215 180 PVTNQiesHPYLTQEK-----LIQYCQSKGIAVTAYSPL--GSPDRPY---AKPEDP---------------VVMEIPKI 234
Cdd:PRK10625 201 IVTIQ---NPYSLLNRsfevgLAEVSQYEGVELLAYSCLafGTLTGKYlngAKPAGArntlfsrftrysgeqTQKAVAAY 277
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160415215 235 KEIAAKHKKTVAQVLIRFHVQRNVV--VIPKSVTPSRIQENLQVFDFQLSEEDMAAILSFNR 294
Cdd:PRK10625 278 VDIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAVHQ 339
|
|
| |
