|
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: 652.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 10 GAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLV 89
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 90 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEM 169
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 170 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVL 249
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2PDK_A 250 IRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALMSCTSHKDYPFHEEF 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 |
1.66e-163 |
|
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: 457.23 E-value: 1.66e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLRE-QVVKREELFIVSKLWCTYHE 85
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPgKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 86 KGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHL 165
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 166 QVEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTT 245
Cdd:cd19106 161 QIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
2PDK_A 246 AQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVC 299
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-316 |
3.44e-160 |
|
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: 448.64 E-value: 3.44e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 12 KMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKG 91
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 92 ACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMIL 171
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 172 NKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpwAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIR 251
Cdd:cd19110 163 NKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG------GSCEGVDLIDDPVIQRIAKKHGKSPAQILIR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
2PDK_A 252 FPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALMSCTSHKDYPFHEEF 316
Cdd:cd19110 237 FQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
4-297 |
8.43e-141 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 399.68 E-value: 8.43e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 4 RILLNNGAKMPILGLGTWKS---PPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLW 80
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPeevPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 81 CTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGIS 160
Cdd:cd19108 82 CTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 161 NFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP-DRPWAKPEDPSLLEDPRIKAIAA 239
Cdd:cd19108 162 NFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALAK 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
2PDK_A 240 KHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWR 297
Cdd:cd19108 242 KHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
4-299 |
2.75e-130 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 372.77 E-value: 2.75e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 4 RILLNNGAKMPILGLGTWKS-PPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCT 82
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 83 YHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEffpLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNF 162
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENND---SESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 163 NHLQVEMILNkpGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSlLEDPRIKAIAAKHN 242
Cdd:cd19116 159 NSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPR-LDDPTLVAIAKKYG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
2PDK_A 243 KTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVC 299
Cdd:cd19116 236 KTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
10-312 |
9.03e-129 |
|
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: 369.51 E-value: 9.03e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 10 GAKMPILGLGTW----KSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHE 85
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 86 KGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHL 165
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 166 QVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP-DRPWAKPEDPSLLEDPRIKAIAAKHNKT 244
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2PDK_A 245 TAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALMSCTSHKDYPF 312
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
7-297 |
8.54e-127 |
|
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: 364.04 E-value: 8.54e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEK 86
Cdd:cd19123 6 LSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNSHAP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 87 GLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGkefFPLDESGNVVPSDTNI--LDTWAAMEELVDEGLVKAIGISNFNH 164
Cdd:cd19123 86 EDVLPALEKTLADLQLDYLDLYLMHWPVALKKG---VGFPESGEDLLSLSPIplEDTWRAMEELVDKGLCRHIGVSNFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 165 LQVEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWA-KPED-PSLLEDPRIKAIAAKHN 242
Cdd:cd19123 163 KKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAmKAEGePVLLEDPVINKIAEKHG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
2PDK_A 243 KTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWR 297
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-289 |
4.71e-124 |
|
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: 355.25 E-value: 4.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 13 MPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLreqvVKREELFIVSKLWCTYHEKGLVKGA 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 93 CQKTLSDLKLDYLDLYLIHWPTGFKPGkeffpldesgnvvPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILN 172
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEG-------------GSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 173 KPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKAIAAKHNKTTAQVLIRF 252
Cdd:cd19071 144 AA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP--------LLDDPVLKEIAKKYGKTPAQVLLRW 213
|
250 260 270
....*....|....*....|....*....|....*..
2PDK_A 253 PMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19071 214 ALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-299 |
2.63e-117 |
|
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: 340.16 E-value: 2.63e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 2 ASRILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWC 81
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 82 TYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISN 161
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 162 FNHLQVEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPED-----PSLLEDPRIKA 236
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspaPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
2PDK_A 237 IAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVC 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 ... |
7-289 |
1.43e-116 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 337.78 E-value: 1.43e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEK 86
Cdd:cd19125 5 LNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 87 GLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKeffPLDESGNVVPSDtnILDTWAAMEELVDEGLVKAIGISNFNHLQ 166
Cdd:cd19125 85 EDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVLPPD--IPSTWKAMEKLVDSGKVRAIGVSNFSVKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 167 VEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEdpsLLEDPRIKAIAAKHNKTTA 246
Cdd:cd19125 160 LEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKLGKTPA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
2PDK_A 247 QVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19125 235 QVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKF 277
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-298 |
1.57e-113 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 328.94 E-value: 1.57e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 9 NGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTYHEKGL 88
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAI----AASGVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 89 VKGACQKTlsdlkldyldlylIHWPtgfkpgkeffpldesgnvvpSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVE 168
Cdd:COG0656 77 TLAAFEESlerlgldyldlylIHWP--------------------GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 169 MILNKPGlkYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDrpwakpedpsLLEDPRIKAIAAKHNKTTAQV 248
Cdd:COG0656 137 ELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQV 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
2PDK_A 249 LIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRV 298
Cdd:COG0656 205 VLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-297 |
2.05e-100 |
|
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: 296.72 E-value: 2.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 10 GAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLV 89
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 90 KGACQKTLSDLKLDYLDLYLIHWPTGF--KPGKEFFPLDESgnvvpsdtNILDTWAAMEELVDEGLVKAIGISNFNHLQV 167
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFvnKKDKGERELASS--------DVTSVWRAMEALVSEGKVKSIGLSNFNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 168 EMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRP--WAKPEDPSLLEDPRIKAIAAKHNKTT 245
Cdd:cd19111 153 NKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTP 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
2PDK_A 246 AQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWR 297
Cdd:cd19111 231 AQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-299 |
2.40e-99 |
|
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: 294.82 E-value: 2.40e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 5 ILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYH 84
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 85 EKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKpGKEF--FPLDESGNV-VPSDTNILDTWAAMEELVDEGLVKAIGISN 161
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSL-SKEDdsGKLDPTGEHkQDYTTDLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 162 FNHLQVEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKP-------EDPSLLEDPRI 234
Cdd:cd19155 163 FNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
2PDK_A 235 KAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVC 299
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-285 |
4.16e-99 |
|
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: 293.16 E-value: 4.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQ-VVKREELFIVSKLWCTYHE 85
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEpGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 86 KGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKE---FFPLDESGNVVPSDTN--ILDTWAAMEELVDEGLVKAIGIS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDlnpLTAVPTNGGEVDLDLSvsLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 161 NFNHLQVEMILNKPGLkyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwAKPEDPSLLEDPRIKAIAAK 240
Cdd:cd19118 161 NFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-----NLAGLPLLVQHPEVKAIAAK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
2PDK_A 241 HNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKvfDFELSSQD 285
Cdd:cd19118 234 LGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDE 276
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
3-297 |
5.22e-96 |
|
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: 286.30 E-value: 5.22e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 3 SRILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCT 82
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 83 YHekGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKP---GKEFFPLDESGNV-VPSDTNILDTWAAMEELVDEGLVKAIG 158
Cdd:cd19112 81 DH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLdIDVTISLETTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 159 ISNFnhlqvEMILNKPGLKY---KPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLG--SPDRPWAKPEDPslLEDPR 233
Cdd:cd19112 159 ISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWFGSVSP--LDDPV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
2PDK_A 234 IKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWR 297
Cdd:cd19112 232 LKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-289 |
6.84e-96 |
|
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: 285.16 E-value: 6.84e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTYHEK 86
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFITTKLWCTWHRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 87 glVKGACQKTLSDLKLDYLDLYLIHWPTGFKP-GKEFFPLDESG-NVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNH 164
Cdd:cd19117 84 --VEEALDQSLKKLGLDYVDLYLMHWPVPLDPdGNDFLFKKDDGtKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 165 LQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKAIAAKHNKT 244
Cdd:cd19117 162 KNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGKT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
2PDK_A 245 TAQVLIRFPMQRNLVVIPKSVTPERIAENFKVfdFELSSQDMTTL 289
Cdd:cd19117 234 PAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEI 276
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-292 |
1.67e-94 |
|
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: 280.67 E-value: 1.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 13 MPILGLGTWK-SPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKG 91
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 92 ACQKTLSDLKLDYLDLYLIHWptgfkPGKEFFPLDESGNVvpsdTNILDTWAAMEELVDEGLVKAIGISNFN--HLQvEM 169
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHW-----PGVQGLKPSDPRNA----ELRRESWRALEDLYKEGKLRAIGVSNYTvrHLE-EL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 170 ilnkpgLKY---KPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpeDPSLLEDPRIKAIAAKHNKTTA 246
Cdd:cd19136 151 ------LKYcevPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG--------DLRLLEDPTVLAIAKKYGRTPA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
2PDK_A 247 QVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSY 292
Cdd:cd19136 217 QVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-297 |
4.87e-93 |
|
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: 278.56 E-value: 4.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 5 ILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYH 84
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 85 EKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKpgkeFFPLDES----------GNVVPSDTNILDTWAAMEELVDEGLV 154
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFK----FVPIEEKyppgfycgdgDNFVYEDVPILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 155 KAIGISNFNHLQVEMILNkpGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP-----DRPWAKpEDPSLL 229
Cdd:cd19113 159 KSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL-NTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2PDK_A 230 EDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWR 297
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-297 |
3.44e-92 |
|
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: 276.61 E-value: 3.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 1 MASRILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLW 80
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 81 CTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFK---PGKEFFP--LDESGNVVPSDTNILDTWAAMEELVDEGLVK 155
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 156 AIGISNFNHlQVEMILnkpgLKY---KPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGsP------DRPWAKpEDP 226
Cdd:cd19115 161 SIGVSNFSA-QLLMDL----LRYariRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PqsflelDLPGAK-DTP 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2PDK_A 227 SLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWR 297
Cdd:cd19115 234 PLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-286 |
3.00e-89 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 266.93 E-value: 3.00e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 5 ILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTYH 84
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 85 EKGLVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeffpldesgnvVPSDTNILDTWAAMEELVDEGLVKAIGISNFNH 164
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWP------------------VPAQDKYVETWKALIELKKEGRVKSIGVSNFTI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 165 LQVEMILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKAIAAKHNKT 244
Cdd:cd19131 140 EHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQG----------GLLSDPVIGEIAEKHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|..
2PDK_A 245 TAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDM 286
Cdd:cd19131 208 PAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDM 249
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
7-292 |
6.15e-87 |
|
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: 262.08 E-value: 6.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLrEQVVKREELFIVSKLWCTYHEK 86
Cdd:cd19121 6 LNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTYHRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 87 glVKGACQKTLSDLKLDYLDLYLIHWPTGFKP--GKEFFPL--DESGNVVPsDTNILDTWAAMEELVDEGLVKAIGISNF 162
Cdd:cd19121 85 --VELCLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTlpDGSRDLDW-DWNHVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 163 NHLQVEMILnkPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKAIAAKHN 242
Cdd:cd19121 162 SIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEIAKKHN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
2PDK_A 243 KTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFElsSQDMTTLLSY 292
Cdd:cd19121 232 VGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-286 |
1.27e-86 |
|
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: 261.43 E-value: 1.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 9 NGAKMPILGLGTWKSPPG--QVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVK-REELFIVSKLWCTYHE 85
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSpeDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 86 KGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDEsGNVVPSDtnILDTWAAMEELVDEGLVKAIGISNFNHL 165
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEE-EDFLPFD--IKGVWEAMEECQRLGLTKAIGVSNFSCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 166 QVEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAkpeDPSLLEDPRIKAIAAKHNKTT 245
Cdd:cd19124 158 KLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWG---SNAVMESDVLKEIAAAKGKTV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
2PDK_A 246 AQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDM 286
Cdd:cd19124 233 AQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDL 273
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-293 |
2.39e-86 |
|
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: 259.81 E-value: 2.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 5 ILLNNGAKMPILGLGTWKSPPGQVTE-AVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTY 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAI----KKSGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 84 HEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGfkpgkeffpldesgnvvpsdtNILDTWAAMEELVDEGLVKAIGISNFN 163
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVSNFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 164 HLQ-VEMILNKpglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwakpEDPSLLEDPRIKAIAAKHN 242
Cdd:cd19133 136 PDRlVDLILHN---EVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE--------GRNNLFENPVLTEIAEKYG 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
2PDK_A 243 KTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYN 293
Cdd:cd19133 205 KSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-289 |
3.39e-86 |
|
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: 259.29 E-value: 3.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 5 ILLNNGAKMPILGLGTWKSPPGQVTE-AVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTY 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDETErAVQTALENGYRSIDTAAIYKNEEGVGEAI----RESGVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 84 HEKGLVKGACQKTLSDLKLDYLDLYLIHWPTgfkPGKeffpldesgnvvpsdtnILDTWAAMEELVDEGLVKAIGISNFN 163
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWPG---KDK-----------------FIDTWKALEKLYASGKVKAIGVSNFQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 164 HLQVEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKAIAAKHNK 243
Cdd:cd19126 137 EHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----------GLLSNPVLAAIGEKYGK 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
2PDK_A 244 TTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19126 205 SAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAI 250
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-286 |
6.62e-86 |
|
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: 259.38 E-value: 6.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 14 PILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGAC 93
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 94 QKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNK 173
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 174 pgLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKpedpSLLEDPRIKAIAAKHNKTTAQVLIRFP 253
Cdd:cd19128 162 --CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNL----TFLNDSELKALATKYNTTPPQVIIAWH 235
|
250 260 270
....*....|....*....|....*....|....*.
2PDK_A 254 MQR---NLVVIPKSVTPERIAENFKVFDFELSSQDM 286
Cdd:cd19128 236 LQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDM 271
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-298 |
6.00e-85 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 256.55 E-value: 6.00e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPPGQ-VTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLreqvVKREELFIVSKLWCTYH- 84
Cdd:cd19157 4 LNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESG----IPREELFITSKVWNADQg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 85 -EKGLvkGACQKTLSDLKLDYLDLYLIHWPtgfKPGKEffpldesgnvvpsdtniLDTWAAMEELVDEGLVKAIGISNFN 163
Cdd:cd19157 80 yDSTL--KAFEASLERLGLDYLDLYLIHWP---VKGKY-----------------KETWKALEKLYKDGRVRAIGVSNFQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 164 HLQVEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDrpwakpedpsLLEDPRIKAIAAKHNK 243
Cdd:cd19157 138 VHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEKYNK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
2PDK_A 244 TTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRV 298
Cdd:cd19157 206 SVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-289 |
8.52e-83 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 250.27 E-value: 8.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 13 MPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEklreQVVKREELFIVSKLWCTYHEKGLVKGA 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAE----SGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 93 CQKTLSDLKLDYLDLYLIHWPTgfkpgkeffpldesgnvvpSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILN 172
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN-------------------PTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 173 KPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLgspdrpwAKPEdpsLLEDPRIKAIAAKHNKTTAQVLIRF 252
Cdd:cd19073 138 ISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-------ARGE---VLRDPVIQEIAEKYDKTPAQVALRW 205
|
250 260 270
....*....|....*....|....*....|....*..
2PDK_A 253 PMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19073 206 LVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-289 |
2.75e-81 |
|
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: 247.24 E-value: 2.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPpGQVTEAVKVAI-DVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCT--Y 83
Cdd:cd19135 7 LSNGVEMPILGLGTSHSG-GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAI----KESGVPREDLFLTTKLWPSdyG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 84 HEKglVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEffpldesgnvvpSDTNILDTWAAMEELVDEGLVKAIGISNFN 163
Cdd:cd19135 82 YES--TKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN------------VKETRAETWRALEELYDEGLCRAIGVSNFL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 164 HLQVEMILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrPWakpedpSLLEDPRIKAIAAKHNK 243
Cdd:cd19135 148 IEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA----KG------KALEEPTVTELAKKYQK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
2PDK_A 244 TTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19135 216 TPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATL 261
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-276 |
2.89e-81 |
|
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: 248.14 E-value: 2.89e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 8 NNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKG 87
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 88 LVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSD-TNILDTWAAMEELVDEGLVKAIGISNFNHLQ 166
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 167 VEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRpwakpedPSLLEDPRIKAIAAKHNKTTA 246
Cdd:cd19129 161 LREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME-------PKLLEDPVITAIARRVNKTPA 231
|
250 260 270
....*....|....*....|....*....|
2PDK_A 247 QVLIRFPMQRNLVVIPKSVTPERIAENFKV 276
Cdd:cd19129 232 QVLLAWAIQRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
7-297 |
1.24e-79 |
|
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: 242.81 E-value: 1.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPPGQVTE-AVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTY-- 83
Cdd:cd19156 3 LANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGI----RESGVPREEVFVTTKLWNSDqg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 84 HEKGLvkGACQKTLSDLKLDYLDLYLIHWPTGFKpgkeffpldesgnvvpsdtnILDTWAAMEELVDEGLVKAIGISNFN 163
Cdd:cd19156 79 YESTL--AAFEESLEKLGLDYVDLYLIHWPVKGK--------------------FKDTWKAFEKLYKEKKVRAIGVSNFH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 164 HLQVEMILNKpgLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDrpwakpedpsLLEDPRIKAIAAKHNK 243
Cdd:cd19156 137 EHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKYGK 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
2PDK_A 244 TTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWR 297
Cdd:cd19156 205 SAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-297 |
6.55e-79 |
|
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: 242.46 E-value: 6.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 10 GAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLV 89
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 90 KGACQKTLSDLKLDYLDLYLIHWPTGFK---PGKEFFPLDESGNVVP---SDTNILDTWAAMEELVDEGLVKAIGISNFN 163
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWKDKELKKfplEQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 164 hlqVEMILNKpgLKY---KPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP---DRPWAKPEDPSLLEDPRIKAI 237
Cdd:cd19114 161 ---VQLILDL--LTYakiKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTNLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 238 AAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWR 297
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
9-289 |
3.73e-76 |
|
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: 233.69 E-value: 3.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 9 NGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTYHEKGL 88
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 89 VKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeffpldesgnvvPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVE 168
Cdd:cd19140 80 FLASVEESLRKLRTDYVDLLLLHWP-------------------NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 169 MILNKPGLKYkpAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpwakpeDPSLLEDPRIKAIAAKHNKTTAQV 248
Cdd:cd19140 141 EAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA----------RGEVLKDPVLQEIGRKHGKTPAQV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|..
2PDK_A 249 LIRFPMQR-NLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19140 209 ALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-286 |
6.38e-76 |
|
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: 233.45 E-value: 6.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 5 ILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGvaiqEKLREQVVKREELFIVSKLWCTYH 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVG----EGIRRSGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 85 EKGLVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeffpldesgnvVPSD-TNILDTWAAMEELVDEGLVKAIGISNFN 163
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWP------------------VPNDfDRTIQAYKALEKLLAEGRVRAIGVSNFT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 164 HLQVEMILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAK--PEDPSLLEDPRIKAIAAKH 241
Cdd:cd19127 139 PEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASgpTGPGDVLQDPTITGLAEKY 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
2PDK_A 242 NKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDM 286
Cdd:cd19127 217 GKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDM 261
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
7-286 |
5.75e-74 |
|
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: 227.92 E-value: 5.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTYHEK 86
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAV----RRSGVPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 87 GLVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeffpldesgnvVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQ 166
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWP------------------NPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 167 VEMILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRpwakpedpsLLEDPRIKAIAAKHNKTTA 246
Cdd:cd19132 139 LDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|
2PDK_A 247 QVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDM 286
Cdd:cd19132 208 QVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDM 247
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
7-276 |
1.01e-73 |
|
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: 228.92 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWkSPP---GQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTY 83
Cdd:cd19119 6 LNTGASIPALGLGTA-SPHedrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 84 HEKglVKGACQKTLSDLKLDYLDLYLIHWPTGFK-----PGKEFFPLDESGNVVPSDT-NILDTWAAMEELVDEGLVKAI 157
Cdd:cd19119 85 YDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAASgDHITTYKQLEKIYLDGRAKAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 158 GISNFNHLQVEMILNKpgLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKAI 237
Cdd:cd19119 163 GVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLVKKI 232
|
250 260 270
....*....|....*....|....*....|....*....
2PDK_A 238 AAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKV 276
Cdd:cd19119 233 AEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI 271
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-286 |
2.74e-72 |
|
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: 224.42 E-value: 2.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 10 GAKMPILGLGT----WKSPPG----QVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLreqvVKREELFIVSKLWC 81
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDdiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESG----VPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 82 TyheKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGkeffpldesgnvvpsDTNILDTWAAMEELVDEGLVKAIGISN 161
Cdd:cd19120 77 G---IKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 162 FNHLQVEMILNKPglKYKPAVNQIECHPYLT--QEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLledpriKAIAA 239
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPLTRDAGGPLDPVL------EKIAE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
2PDK_A 240 KHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDM 286
Cdd:cd19120 211 KYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEV 257
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
4-289 |
2.85e-70 |
|
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: 218.63 E-value: 2.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 4 RILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEklreQVVKREELFIVSKLWCTY 83
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAA----SGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 84 HEKGLVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkeffpldesgnvvPSDTNILDTWAAMEELVDEGLVKAIGISNFN 163
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPT------------------PAAGNYVHTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 164 HLQVEMILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKAIAAKHNK 243
Cdd:cd19130 139 PPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG----------KLLGDPPVGAIAAAHGK 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
2PDK_A 244 TTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19130 207 TPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAI 252
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-285 |
2.22e-66 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 209.79 E-value: 2.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 7 LNNGAKMPILGLGTWKS--PPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQ-VVKREELFIVSKLWCTY 83
Cdd:cd19122 3 LNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 84 HEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGF-KPGKEFFPLDESGNVVPSDT---NILDTWAAMEELVDEGLVKAIGI 159
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAeKNDQRSPKLGPDGKYVILKDlteNPEPTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 160 SNFNHLQVEMILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSllEDPRIKAIAA 239
Cdd:cd19122 163 SNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVS--ENPTLNEVAE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
2PDK_A 240 KHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVfdFELSSQD 285
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDED 282
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
5-289 |
1.91e-65 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 206.85 E-value: 1.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 5 ILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKlreqVVKREELFIVSKLWCTYH 84
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA----SVAREELFITTKLWNDDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 85 EKglVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeffpldesgnvVPSDTNILDTWAAMEELVDEGLVKAIGISNFN- 163
Cdd:PRK11565 83 KR--PREALEESLKKLQLDYVDLYLMHWP------------------VPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQi 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 164 -HLQveMILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRpwakpedpSLLEDPRIKAIAAKHN 242
Cdd:PRK11565 143 hHLQ--RLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK--------GVFDQKVIRDLADKYG 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
2PDK_A 243 KTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:PRK11565 211 KTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEI 257
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-298 |
4.04e-64 |
|
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: 203.16 E-value: 4.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 5 ILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTYH 84
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 85 EKGLVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeffpldesgnvVPSDTNILDTWAAMEELVDEGLVKAIGISNFNH 164
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWP------------------AGREGKYVDSWGGLMKLREEGLARSIGVSNFTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 165 LQVEMILNKPGlkYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKAIAAKHNKT 244
Cdd:cd19134 141 EHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVG----------RLLDNPAVTAIAAAHGRT 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
2PDK_A 245 TAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRV 298
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-287 |
8.73e-63 |
|
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: 199.12 E-value: 8.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 13 MPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIqeklREQVVKREELFIVSKLWCTYHEKGLVKGA 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 93 CQKTLSDLKLDYLDLYLIHWPTgfkpgkeffpldeSGNVVPSDtnilDTWAAMEELVDEGLVKAIGISNFNHLQVEMILN 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPS-------------PNDEVPVE----EYIGALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 173 KPGlKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpWAKpedpsLLEDPRIKAIAAKHNKTTAQVLIRF 252
Cdd:cd19139 140 VVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA-----YGK-----VLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270
....*....|....*....|....*....|....*
2PDK_A 253 PMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMT 287
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMA 243
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-297 |
2.50e-55 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 180.60 E-value: 2.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 12 KMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEklreQVVKREELFIVSKLWCTYHEKGLVKG 91
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 92 ACQKTLSDLKLDYLDLYLIHWPTgfkPGKEFfPLDEsgnvvpsdtnildtwaAMEELVD---EGLVKAIGISNFNHLQVE 168
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWPS---PNDEV-SVEE----------------FMQALLEakkQGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 169 MILNKPGlKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpWAKpedpsLLEDPRIKAIAAKHNKTTAQV 248
Cdd:PRK11172 138 QAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA-----YGK-----VLKDPVIARIAAKHNATPAQV 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
2PDK_A 249 LIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWR 297
Cdd:PRK11172 207 ILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-289 |
1.33e-54 |
|
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: 179.43 E-value: 1.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 16 LGLGTW-------KSPPGQVTEAVKVAIDVGYRHIDCAHVY---QNENEVGVAIQEKlreqVVKREELFIVSKL------ 79
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 80 WCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGfkpgkeffpldesgnvvpsDTNILDTWAAMEELVDEGLVKAIGI 159
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-------------------DTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 160 SNFNHLQVEMILNKPglKYKPAVNQIECHPY--LTQEKLIQYCQSKGIVVTAYSPLGS-----------------PDRPW 220
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgeRRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2PDK_A 221 AKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQ--RNLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-289 |
3.37e-51 |
|
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: 169.72 E-value: 3.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 10 GAKMPILGLGTWK---------SPPGQVTEAVKVAIDVGYRHIDCAHVYQN---ENEVGVAIQEklreqvVKREELFIVS 77
Cdd:cd19072 1 GEEVPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 78 KLW---CTYHEkglVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEffpldesgnvvpsdtnildTWAAMEELVDEGLV 154
Cdd:cd19072 75 KVSpdhLKYDD---VIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEE-------------------TLRAMEELVEEGKI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 155 KAIGISNFNHLQVEMILNKPGlKYKPAVNQIECHpYLTQE---KLIQYCQSKGIVVTAYSPLGSPDRPwAKPEDPSLLEd 231
Cdd:cd19072 133 RYIGVSNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEKGKLS-NAKGSPLLDE- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
2PDK_A 232 prikaIAAKHNKTTAQVLIRFPMQR-NLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19072 209 -----IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-289 |
2.58e-48 |
|
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: 162.42 E-value: 2.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 5 ILLNNGAKMPILGLGTW-----KSPPGQVTEAVKVAIDVGYRHIDCAHVYQN---ENEVGVAIQEKlreqvvkREELFIV 76
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 77 SKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGfkpgkefFPLDEsgnvvpsdtnildTWAAMEELVDEGLVKA 156
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG-------VPLAE-------------TVAAMEELKKEGKIRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 157 IGISNFNHLQVEMILNKPGLKyKPAVNQIECHpyLTQE----KLIQYCQSKGIVVTAYSPLGSPDRPwakpeDPSLLEDP 232
Cdd:cd19138 136 WGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLL-----RRGLLENP 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
2PDK_A 233 RIKAIAAKHNKTTAQVLIRFPMQRNLVV-IPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19138 208 TLKEIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-289 |
6.03e-42 |
|
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: 145.79 E-value: 6.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 10 GAKMPILGLGTWK---------SPPGQVTEAVKVAIDVGYRHIDCAHVY---QNENEVGVAIQEklreqvVKREELFIVS 77
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 78 KLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkEFFPLDEsgnvvpsdtnildTWAAMEELVDEGLVKAI 157
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPN------PNIPLEE-------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 158 GISNFNHLQVEMILNKpgLKYKPAVNQIECHPY---LTQEKLIQYCQSKGIVVTAYSPLgspDRPWAKPEDpslledpRI 234
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL---RRGLEKTNR-------TL 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
2PDK_A 235 KAIAAKHNKTTAQVLIRFPMQR-NLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19137 204 EEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-289 |
1.21e-32 |
|
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: 122.34 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 12 KMPILGLGTWK-----------SPPGQVTEAVKVAIDVGYRHIDCAHVY---QNENEVGVAIQEKlreqvVKREELFIVS 77
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKEL-----GDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 78 KLWCTYHEKGL--VKGACQKTLSDLKLDYLDLYLIHWPTGFkpgkeFFPLDEsgnvvpsdtnildTWAAMEELVDEGLVK 155
Cdd:cd19093 76 KFAPLPWRLTRrsVVKALKASLERLGLDSIDLYQLHWPGPW-----YSQIEA-------------LMDGLADAVEEGLVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 156 AIGISNFNHLQVEMI---LNKPGlkYKPAVNQIE---CHPYLTQEKLIQYCQSKGIVVTAYSPLG--------SPDRP-- 219
Cdd:cd19093 138 AVGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPpp 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2PDK_A 220 ---------WAKPEDPSLLEdpRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19093 216 ggrrrlfgrKNLEKVQPLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-289 |
2.62e-32 |
|
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: 121.82 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 1 MASRILLNNGAKMPILGLGTWK--SPPGQVTEA-----VKVAIDVGYRHIDCAHVYQN-ENE--VGVAIQEKLREQVVkr 70
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTfgGPWGGVDEAeaiaiLDAALDAGINFFDTADVYGPgRSEelLGEALKGRPRDDVV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 71 eelfIVSKLWCTYHEKGLVKG--------AC---------------QktlsdlkldyldlylIHWPtgfkpgkeffplde 127
Cdd:COG0667 79 ----IATKVGRRMGPGPNGRGlsrehirrAVeaslrrlgtdyidlyQ---------------LHRP-------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 128 sgnvvPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIEchpY--LTQ---EKLIQYCQS 202
Cdd:COG0667 126 -----DPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 203 KGIVVTAYSPLGS---------------PDR-------PWAKPEDPSLLEdpRIKAIAAKHNKTTAQVLIRFPMQRNLV- 259
Cdd:COG0667 198 LGVGVLAYSPLAGglltgkyrrgatfpeGDRaatnfvqGYLTERNLALVD--ALRAIAAEHGVTPAQLALAWLLAQPGVt 275
|
330 340 350
....*....|....*....|....*....|.
2PDK_A 260 -VIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:COG0667 276 sVIPGARSPEQLEENLAAADLELSAEDLAAL 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-289 |
8.99e-27 |
|
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: 106.52 E-value: 8.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 14 PILGLGTW---------KSPPGQVTEAVKVAIDVGYRHIDCAHVYQN---ENEVGVAIQEKlreqvvkREELFIVSKLWC 81
Cdd:cd19085 2 SRLGLGCWqfgggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 82 TYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgKEFFPLDEsgnvvpsdtnildTWAAMEELVDEGLVKAIGISN 161
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP------SSDVPLEE-------------TMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 162 FNHLQVEMILnKPGlkyKPAVNQIECHPYLTQ-EK-LIQYCQSKGIVVTAYSPL------GSPDRPWAKPED------PS 227
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQLPYNLLWRAiEYeILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlFR 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2PDK_A 228 LLEDP----------RIKAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19085 212 HFEPGaeeetfealeKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-286 |
2.70e-25 |
|
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: 102.60 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 10 GAKMPILGLGTW--------KSPPGQVTEAVKVAIDVGYRHIDCAHVYQN---ENEVGVAIQEKlREQVVkreelfIVSK 78
Cdd:cd19084 1 DLKVSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-RDDVV------IATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 79 LwctyhekGLVKGACQKTLSDLKLDYLDLY----------------LIHWPtgfkpgkeffplDEsgnvvpsDTNILDTW 142
Cdd:cd19084 74 C-------GLRWDGGKGVTKDLSPESIRKEveqslrrlqtdyidlyQIHWP------------DP-------NTPIEETA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 143 AAMEELVDEGLVKAIGISNFNhlqVEMIlnKPGLKY-KPAVNQIechPY--LTQ---EKLIQYCQSKGIVVTAYSPLG-- 214
Cdd:cd19084 128 EALEKLKKEGKIRYIGVSNFS---VEQL--EEARKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAqg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 215 ------------SPD---------RPWAKPEDPSLLEdpRIKAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSVTPERIA 271
Cdd:cd19084 200 lltgkykkeptfPPDdrrsrfpffRGENFEKNLEIVD--KLKEIAEKYGKSLAQLAIAWTLAQPGVtsAIVGAKNPEQLE 277
|
330
....*....|....*
2PDK_A 272 ENFKVFDFELSSQDM 286
Cdd:cd19084 278 ENAGALDWELTEEEL 292
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-286 |
2.64e-22 |
|
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: 94.66 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 16 LGLGTWKSPPGQ------------VTEAVKVAIDVGYRHIDCAHVY---QNENEVGVAIQEKlreqvvkREELFIVSK-- 78
Cdd:cd19102 4 IGLGTWAIGGGGwgggwgpqddrdSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 79 -LW------CTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGfkpgkeffpldesgnvvpsDTNILDTWAAMEELVDE 151
Cdd:cd19102 77 lLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP-------------------DEPIEEAWGALAELKEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 152 GLVKAIGISNFNHLQVEMIlnkpgLKYKP-AVNQIechPY--LTQE---KLIQYCQSKGIVVTAYSPLGS--------PD 217
Cdd:cd19102 138 GKVRAIGVSNFSVDQMKRC-----QAIHPiASLQP---PYslLRRGieaEILPFCAEHGIGVIVYSPMQSglltgkmtPE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 218 RPWAKPED-----------PSLLEDPRI----KAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSVTPERIAENFKVFDFE 280
Cdd:cd19102 210 RVASLPADdwrrrspffqePNLARNLALvdalRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLR 289
|
....*.
2PDK_A 281 LSSQDM 286
Cdd:cd19102 290 LTPEEL 295
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
15-285 |
2.89e-20 |
|
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: 88.77 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 15 ILG---LGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQN---ENEVGvaiqEKLREQVVKREELFIVSKlwctyhekgl 88
Cdd:cd19092 10 VLGcmrLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFG----EALALNPGLREKIEIQTK---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 89 vkgacqktlsdlkldyldlylihwpTGFKPGKEFFP-----LDESG-NVVPSDTNIL----------------------- 139
Cdd:cd19092 76 -------------------------CGIRLGDDPRPgrikhYDTSKeHILASVEGSLkrlgtdyldllllhrpdplmdpe 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 140 DTWAAMEELVDEGLVKAIGISNFNHLQVEMiLNKpGLKYKPAVNQIEC---HPYLTQEKLIQYCQSKGIVVTAYSPLGSp 216
Cdd:cd19092 131 EVAEAFDELVKSGKVRYFGVSNFTPSQIEL-LQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGG- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2PDK_A 217 drpwAKPEDPSLLEDPRIKA----IAAKHNKTTAQV----LIRFPMQrnLVVIPKSVTPERIAENFKVFDFELSSQD 285
Cdd:cd19092 208 ----GRLFGGFDERFQRLRAaleeLAEEYGVTIEAIalawLLRHPAR--IQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-275 |
3.21e-19 |
|
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: 84.49 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 16 LGLGTWK-SPPGQVTEAVKV---AIDVGYRHIDCAHVY---QNENEVGVAIQEKlreqvVKREELFIVSKLWCTYHEKGL 88
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAFALldaALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPGGDPS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 89 VKGA-----------------------CQktlsdlkldyldlylIHWPtgfkpgkeffpldesgnvvPSDTNILDTWAAM 145
Cdd:cd06660 78 RSRLspehirrdleeslrrlgtdyidlYY---------------LHRD-------------------DPSTPVEETLEAL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 146 EELVDEGLVKAIGISNFNHLQVEMILN--KPGLKYKPAVNQIE---CHPYLTQEKLIQYCQSKGIVVTAYSPLGS-Pdrp 219
Cdd:cd06660 124 NELVREGKIRYIGVSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARgP--- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
2PDK_A 220 wakpedpslledprikaiaakhnkttAQVLIRFPMQRNLV--VIPKSVTPERIAENFK 275
Cdd:cd06660 201 --------------------------AQLALAWLLSQPFVtvPIVGARSPEQLEENLA 232
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-285 |
6.21e-18 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 82.12 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 1 MASRIllnngakmpILG---LGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVY---QNENEVGVAiqekLREQVVKREELF 74
Cdd:COG4989 12 SVSRI---------VLGcmrLGEWDLSPAEAAALIEAALELGITTFDHADIYggyTCEALFGEA----LKLSPSLREKIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 75 IVSKlwCtyhekGLVKGAcqktlsdlkLDYLDLY-----------------------------LIHWPTgfkpgkeffPL 125
Cdd:COG4989 79 LQTK--C-----GIRLPS---------EARDNRVkhydtskehiiasvegslrrlgtdyldllLLHRPD---------PL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 126 desgnvvpsdTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMiLNKpGLKYKPAVNQIECHPYLTQ---EKLIQYCQS 202
Cdd:COG4989 134 ----------MDPEEVAEAFDELKASGKVRHFGVSNFTPSQFEL-LQS-ALDQPLVTNQIELSLLHTDafdDGTLDYCQL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 203 KGIVVTAYSPLGSPDrpWAKPEDPsllEDPRIKA----IAAKHNKTTAQVLI----RFPMqrNLVVIPKSVTPERIAENF 274
Cdd:COG4989 202 NGITPMAWSPLAGGR--LFGGFDE---QFPRLRAaldeLAEKYGVSPEAIALawllRHPA--GIQPVIGTTNPERIKAAA 274
|
330
....*....|.
2PDK_A 275 KVFDFELSSQD 285
Cdd:COG4989 275 AALDIELTREE 285
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
32-291 |
2.21e-16 |
|
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: 78.23 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 32 VKVAIDVGYRHIDCAHVY---QNENEVGVAIQEKLREQVVkreelfIVSKlwcTYHEKG-----------LVKGACQKTL 97
Cdd:cd19083 39 VREALDNGVNLLDTAFIYglgRSEELVGEVLKEYNRNEVV------IATK---GAHKFGgdgsvlnnspeFLRSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 98 SDLKLDYLDLYLIHWPTGFKPGKEFFpldesgnvvpsdtnildtwAAMEELVDEGLVKAIGISNFNHLQVEMiLNKPGlk 177
Cdd:cd19083 110 KRLNTDYIDLYYIHFPDGETPKAEAV-------------------GALQELKDEGKIRAIGVSNFSLEQLKE-ANKDG-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 178 ykpAVNQIEcHPY-LTQ----EKLIQYCQSKGIVVTAYSPLGS-------------PDRPWAKpeDPSLLEDP------- 232
Cdd:cd19083 168 ---YVDVLQ-GEYnLLQreaeEDILPYCVENNISFIPYFPLASgllagkytkdtkfPDNDLRN--DKPLFKGErfsenld 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
2PDK_A 233 ---RIKAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSVTPERIAENFKVFDFELSSQDMTTLLS 291
Cdd:cd19083 242 kvdKLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-285 |
7.29e-16 |
|
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: 76.71 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 1 MASRILLNNGAKMPILGLGT-----WKSPPGQVTEAVKV---AIDVGYRHIDCAHVYQ-NENEVGVAIQEKLReqvvKRE 71
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAmglsaFYGPPKPDEERFAVldaAFELGCTFWDTADIYGdSEELIGRWFKQNPG----KRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 72 ELFIVSKL-WCTYHEKGL---------VKGACQKTLSDLKLDYLDLYLIHwptgfkpgkeffpldesgnVVPSDTNILDT 141
Cdd:cd19144 77 KIFLATKFgIEKNVETGEysvdgspeyVKKACETSLKRLGVDYIDLYYQH-------------------RVDGKTPIEKT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 142 WAAMEELVDEGLVKAIGISNfnhLQVEMILNKPGLKYKPAVnQIECHPYLT-----QEKLIQYCQSKGIVVTAYSPLG-- 214
Cdd:cd19144 138 VAAMAELVQEGKIKHIGLSE---CSAETLRRAHAVHPIAAV-QIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGrg 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 215 -------SPD----------RPWAKPED-PSLLE--DpRIKAIAAKHNKTTAQVLIRFPMQR--NLVVIPKSVTPERIAE 272
Cdd:cd19144 214 fltgairSPDdfeegdfrrmAPRFQAENfPKNLElvD-KIKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRLEE 292
|
330
....*....|...
2PDK_A 273 NFKVFDFELSSQD 285
Cdd:cd19144 293 NLGALKVKLTEEE 305
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
8-291 |
1.40e-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: 75.77 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 8 NNGAKMPILGLGTWK----SPPGQVTEAVKV-----AIDVGYRHIDCAHVYQN---ENEVGVAIQeKLREQVVkreelfI 75
Cdd:cd19149 6 KSGIEASVIGLGTWAigggPWWGGSDDNESIrtihaALDLGINLIDTAPAYGFghsEEIVGKAIK-GRRDKVV------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 76 VSKLWCTYHEKGL-------------------VKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkeffpldesgnvvpSDT 136
Cdd:cd19149 79 ATKCGLRWDREGGsfffvrdgvtvyknlspesIREEVEQSLKRLGTDYIDLYQTHWQD-------------------VET 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 137 NILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNkpglKYKPAVNQIechPY-----LTQEKLIQYCQSKGIVVTAYS 211
Cdd:cd19149 140 PIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVK----AGQLDIIQE---KYsmldrGIEKELLPYCKKNNIAFQAYS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 212 PLGS--------PDR-----------PWAKPEDPS----LLEdpRIKAIAAKHNKTTAQVLIRFPMQR--NLVVIPKSVT 266
Cdd:cd19149 213 PLEQglltgkitPDRefdagdarsgiPWFSPENREkvlaLLE--KWKPLCEKYGCTLAQLVIAWTLAQpgITSALCGARK 290
|
330 340
....*....|....*....|....*
2PDK_A 267 PERIAENFKVFDFELSSQDMTTLLS 291
Cdd:cd19149 291 PEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
140-282 |
3.71e-15 |
|
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: 73.79 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 140 DTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLkykpAVNQIECHPYLTQ-EKLIQYCQSKGIVVTAYSPLGSpdR 218
Cdd:cd19088 124 EQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG--G 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2PDK_A 219 PWAKPEDPslledprIKAIAAKHNKTTAQVLIRFPMQR--NLVVIPKSVTPERIAENFKVFDFELS 282
Cdd:cd19088 198 DLAQPGGL-------LAEVAARLGATPAQVALAWLLARspVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-276 |
3.85e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 73.77 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 1 MASRILLNNGAKMPILGLGTWKSPPGQVtEAVKVAIDVGYRHIDCAHVYQN---ENEVGVAIQEklreqvVKREELFIVS 77
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRESP-ELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 78 KlwctyhekglvkgacqktlsdlkldyldlylIHWPTGFKPGKEFFP-LDES--------------GNVVPSDTNILDTW 142
Cdd:cd19105 74 K-------------------------------ASPRLDKKDKAELLKsVEESlkrlqtdyidiyqlHGVDTPEERLLNEE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 143 --AAMEELVDEGLVKAIGIS-NFNhlQVEMILN--KPG------LKYKPAvnqiecHPYLTQEKLIQYCQSKGIVVTAYS 211
Cdd:cd19105 123 llEALEKLKKEGKVRFIGFStHDN--MAEVLQAaiESGwfdvimVAYNFL------NQPAELEEALAAAAEKGIGVVAMK 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2PDK_A 212 PLGS-PDRPWAKPEDPSLLEDPrikaiaakhnkttAQVLIRFPMQRNLV--VIPKSVTPERIAENFKV 276
Cdd:cd19105 195 TLAGgYLQPALLSVLKAKGFSL-------------PQAALKWVLSNPRVdtVVPGMRNFAELEENLAA 249
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
4-286 |
2.35e-14 |
|
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: 72.25 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 4 RILLNNGAKMPILGLG----TWKSPPGQVTEAVKV---AIDVGYRHIDCAHVY-QNENE--VGVAIQEKlreqvvkREEL 73
Cdd:cd19076 3 RKLGTQGLEVSALGLGcmgmSAFYGPADEEESIATlhrALELGVTFLDTADMYgPGTNEelLGKALKDR-------RDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 74 FIVSKlwctyhekglvkgacqktlsdlkldyldlylihWPTGFKPGKEFFPLDES-GNV--------------------- 131
Cdd:cd19076 76 VIATK---------------------------------FGIVRDPGSGFRGVDGRpEYVraaceaslkrlgtdvidlyyq 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 132 --VPSDTNILDTWAAMEELVDEGLVKAIGISNFN----------H----LQVEmilnkpglkYKPAVNQIEchpyltqEK 195
Cdd:cd19076 123 hrVDPNVPIEETVGAMAELVEEGKVRYIGLSEASadtirrahavHpitaVQSE---------YSLWTRDIE-------DE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 196 LIQYCQSKGIVVTAYSPL------GSPDRPWAKPEDPSLLEDPR---------------IKAIAAKHNKTTAQVLIRFPM 254
Cdd:cd19076 187 VLPTCRELGIGFVAYSPLgrgfltGAIKSPEDLPEDDFRRNNPRfqgenfdknlklvekLEAIAAEKGCTPAQLALAWVL 266
|
330 340 350
....*....|....*....|....*....|....
2PDK_A 255 QR--NLVVIPKSVTPERIAENFKVFDFELSSQDM 286
Cdd:cd19076 267 AQgdDIVPIPGTKRIKYLEENVGALDVVLTPEEL 300
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
132-286 |
2.41e-14 |
|
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: 72.27 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 132 VPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILnkpglKYKP-AVNQIECHPyLTQEKL----IQYCQSKGIV 206
Cdd:cd19077 121 VDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAH-----AVHPiAAVEVEYSL-FSREIEengvLETCAELGIP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 207 VTAYSPL------GSPDRPWAKPEDPSLLEDPR---------------IKAIAAKHNKTTAQVLIRFPMQRN---LVVIP 262
Cdd:cd19077 195 IIAYSPLgrglltGRIKSLADIPEGDFRRHLDRfngenfeknlklvdaLQELAEKKGCTPAQLALAWILAQSgpkIIPIP 274
|
170 180
....*....|....*....|....
2PDK_A 263 KSVTPERIAENFKVFDFELSSQDM 286
Cdd:cd19077 275 GSTTLERVEENLKAANVELTDEEL 298
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
8-289 |
2.07e-13 |
|
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: 69.54 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 8 NNGAKMPILGLGT----------WKSPPGQVTEAVKVAIDVGYRHIDCAHVYQN---ENEVGVAIQEklreqVVKREELF 74
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKE-----FAPRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 75 IVSKLwctYHE-------KGL----VKGACQKTLSDLKLDYLDLYLIHWptgfkpgkeffpLDEsgnvvpsDTNILDTWA 143
Cdd:cd19079 82 IATKV---YFPmgdgpngRGLsrkhIMAEVDASLKRLGTDYIDLYQIHR------------WDY-------ETPIEETLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 144 AMEELVDEGLVKAIGISNFNHLQVEMILN---KPGLKyKPAVNQiecHPY--LTQE---KLIQYCQSKGIVVTAYSPL-- 213
Cdd:cd19079 140 ALHDVVKSGKVRYIGASSMYAWQFAKALHlaeKNGWT-KFVSMQ---NHYnlLYREeerEMIPLCEEEGIGVIPWSPLar 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 214 --------GSPDRPWAKPEDPSLLED----------PRIKAIAAKHNKTTAQVLIRFPMQRNLVVIP--KSVTPERIAEN 273
Cdd:cd19079 216 grlarpwgDTTERRRSTTDTAKLKYDyfteadkeivDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDA 295
|
330
....*....|....*.
2PDK_A 274 FKVFDFELSSQDMTTL 289
Cdd:cd19079 296 VAALDIKLSEEEIKYL 311
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
134-289 |
1.80e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 66.85 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 134 SDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPglkYKPAVNQIEC-----HPyltQEKLIQYCQSKGIVVT 208
Cdd:cd19101 117 SDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---VPIVSNQVQYslldrRP---ENGMAALCEDHGIKLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 209 AYSP----------LGSPDRPWAKPEDPSLLEDPRI-----------------KAIAAKHNKTTAQVLIRFPMQRNLV-- 259
Cdd:cd19101 191 AYGTlaggllsekyLGVPEPTGPALETRSLQKYKLMidewggwdlfqellrtlKAIADKHGVSIANVAVRWVLDQPGVag 270
|
170 180 190
....*....|....*....|....*....|
2PDK_A 260 VIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19101 271 VIVGARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
136-289 |
3.70e-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: 63.00 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 136 TNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILnkpGLKYKPAVNQIEC--------HPYLTQEKLIQYCQSKGIVV 207
Cdd:cd19081 128 TPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEAL---ELSRQHGLPRYVSlqpeynlvDRESFEGELLPLCREEGIGV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 208 TAYSPLGS--------PDRPWAK----PEDPSLLEDPR-------IKAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSVT 266
Cdd:cd19081 205 IPYSPLAGgfltgkyrSEADLPGstrrGEAAKRYLNERglrildaLDEVAAEHGATPAQVALAWLLARPGVtaPIAGART 284
|
170 180
....*....|....*....|...
2PDK_A 267 PERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19081 285 VEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-273 |
4.94e-11 |
|
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: 61.87 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 14 PILGLGTWK-------SPPGQVTEAVKVAIDVGYRHIDCAHVYQN-ENEVGVAIQEklreqvVKREELFIVSKLWCTYhe 85
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGTHG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 86 kglvkgacqktlsdlkldyldlylihwpTGFKPGKEFFP------LDES-----------------GNVVPSDTNIldtw 142
Cdd:cd19095 73 ----------------------------EGGRDRKDFSPaairasIERSlrrlgtdyidllqlhgpSDDELTGEVL---- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 143 AAMEELVDEGLVKAIGISNFNhlqvemilnkPGLKYKPAVNQIEC--HPY----LTQEKLIQYCQSKGIVVTAYSPLGSP 216
Cdd:cd19095 121 ETLEDLKAAGKVRYIGVSGDG----------EELEAAIASGVFDVvqLPYnvldREEEELLPLAAEAGLGVIVNRPLANG 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 217 DRPWAKPEDPSLLEDPRIKAIAAKHN-KTTAQVLIRFPMQRNLV--VIPKSVTPERIAEN 273
Cdd:cd19095 191 RLRRRVRRRPLYADYARRPEFAAEIGgATWAQAALRFVLSHPGVssAIVGTTNPEHLEEN 250
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-289 |
1.97e-10 |
|
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: 60.70 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 1 MASRILLNNGAKMPILGLGT--------WKSPPGQVTEA-----VKVAIDVGYRHIDCAHVY---QNENEVGVAIQEKlR 64
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTmtfgggggFFGAWGGVDQEeadrlVDIALDAGINFFDTADVYsegESEEILGKALKGR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 65 EQVVkreelfIVSKLwcTY------HEKGLVKG----ACQKTLSDLKLDYLDLYLIHwptGFKPGKeffPLDEsgnvvps 134
Cdd:cd19091 80 DDVL------IATKV--RGrmgegpNDVGLSRHhiirAVEASLKRLGTDYIDLYQLH---GFDALT---PLEE------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 135 dtnildTWAAMEELVDEGLVKAIGISNFNHLQVEMIL---NKPGL--------KYKPAVNQIEchpyltQEkLIQYCQSK 203
Cdd:cd19091 139 ------TLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLarfvalqaYYSLLGRDLE------HE-LMPLALDQ 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 204 GIVVTAYSPLG--------SPDRPwaKPEDPSL---------LEDPRI-------KAIAAKHNKTTAQVLIRFPMQRNLV 259
Cdd:cd19091 206 GVGLLVWSPLAggllsgkyRRGQP--APEGSRLrrtgfdfppVDRERGydvvdalREIAKETGATPAQVALAWLLSRPTV 283
|
330 340 350
....*....|....*....|....*....|..
2PDK_A 260 --VIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19091 284 ssVIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
17-213 |
4.86e-10 |
|
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: 59.63 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 17 GLGTWK--------SPPGQVTEAVKVAIDVGYRHIDCAHVY---QNENEVGVAIqeklrEQVVKREELFIVSKLWCTYHE 85
Cdd:cd19148 8 ALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKAL-----KEYGKRDRVVIATKVGLEWDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 86 KGLVKGACQKTLSDLKLDYLDL---------YLIHWPtgfkpgKEFFPLDEsgnvvpsdtnildTWAAMEELVDEGLVKA 156
Cdd:cd19148 83 GGEVVRNSSPARIRKEVEDSLRrlqtdyidlYQVHWP------DPLVPIEE-------------TAEALKELLDEGKIRA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
2PDK_A 157 IGISNFNHLQVEMILNKPGLkykpAVNQIechPY-----LTQEKLIQYCQSKGIVVTAYSPL 213
Cdd:cd19148 144 IGVSNFSPEQMETFRKVAPL----HTVQP---PYnlferEIEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
135-273 |
6.00e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 59.27 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 135 DTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEM---ILNKPGLKYKPAVNQIecHPYL--------------TQEkLI 197
Cdd:cd19752 124 DTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERarqIARQQGWAEFSAIQQR--HSYLrprpgadfgvqrivTDE-LL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 198 QYCQSKG-IVVTAYSPL--GSPDRPWAKPEDPSLLEDPR-----IKAIAAKHNKTTAQVLIRFPMQRNLVVIP--KSVTP 267
Cdd:cd19752 201 DYASSRPdLTLLAYSPLlsGAYTRPDRPLPEQYDGPDSDarlavLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTV 280
|
....*.
2PDK_A 268 ERIAEN 273
Cdd:cd19752 281 EQLEEN 286
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-283 |
2.85e-09 |
|
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: 57.22 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 10 GAKMPILGLGTWKSPPGQVT-----EAVKVAIDVGYRHIDCAHVY---QNENEVGVAIQEklreqvVKREELFIVSKL-W 80
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDdedakACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG------WPRESYVISTKVfW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 81 CT---YHEKGL----VKGACQKTLSDLKLDYLDLYLIHWPtgfkpgkeffplDEsgnvvpsDTNILDTWAAMEELVDEGL 153
Cdd:cd19074 75 PTgpgPNDRGLsrkhIFESIHASLKRLQLDYVDIYYCHRY------------DP-------ETPLEETVRAMDDLIRQGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 154 VKAIGISNFNHLQVE--MILNKPGLKYKPAVNQIECHpYLTQEK---LIQYCQSKGIVVTAYSPLGS------------- 215
Cdd:cd19074 136 ILYWGTSEWSAEQIAeaHDLARQFGLIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQglltgkyrdgipp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 216 PDRPWAKPEDP-----SLLEDPRI------KAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSVTPERIAENFKVFDFELS 282
Cdd:cd19074 215 PSRSRATDEDNrdkkrRLLTDENLekvkklKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLS 294
|
.
2PDK_A 283 S 283
Cdd:cd19074 295 P 295
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-275 |
3.01e-09 |
|
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: 56.34 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 4 RILLNNGAKMPILGLGT---WKSPPGQVTEAVKVAIDVGYRHIDCAHVYQN-ENEVGVAIQEKlreqvvkREELFIVSKL 79
Cdd:cd19100 2 RRLGRTGLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 80 WC-TYhekglvKGA------------------CQktlsdlkldyldlylIHwptGFKPGKEFFPLDESGNVvpsdtnild 140
Cdd:cd19100 75 GArDY------EGAkrdlerslkrlgtdyidlYQ---------------LH---AVDTEEDLDQVFGPGGA--------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 141 tWAAMEELVDEGLVKAIGISN---------FNHLQVEMILnkpglkykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAys 211
Cdd:cd19100 122 -LEALLEAKEEGKIRFIGISGhspevllraLETGEFDVVL--------FPINPAGDHIDSFREELLPLAREKGVGVIA-- 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 212 plgspdrpwakpedpslledprIKAIAA----KHNKTTAQVLIRFPMQRNLV--VIPKSVTPERIAENFK 275
Cdd:cd19100 191 ----------------------MKVLAGgrllSGDPLDPEQALRYALSLPPVdvVIVGMDSPEELDENLA 238
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
16-289 |
3.44e-08 |
|
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: 53.98 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 16 LGLGTWKSPPGQVTEAVKV---AIDVGYRHIDCAHVY-QNENEV--GVAIQEKLREQVVkreelfIVSKLWCTYHEKG-- 87
Cdd:cd19145 20 MGLSGDYGAPKPEEEGIALihhAFNSGVTFLDTSDIYgPNTNEVllGKALKDGPREKVQ------LATKFGIHEIGGSgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 88 -------LVKGACQKTLSDLKLDYLDLYLIHwptgfkpgkeffPLDESgnvVPsdtnILDTWAAMEELVDEGLVKAIGIS 160
Cdd:cd19145 94 evrgdpaYVRAACEASLKRLDVDYIDLYYQH------------RIDTT---VP----IEITMGELKKLVEEGKIKYIGLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 161 nfnHLQVEMILNKPGLKYKPAVnQIECHPYL--TQEKLIQYCQSKGIVVTAYSPLGspdRP--WAKPEDPSLLED----- 231
Cdd:cd19145 155 ---EASADTIRRAHAVHPITAV-QLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLG---RGffAGKAKLEELLENsdvrk 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2PDK_A 232 --PR---------------IKAIAAKHNKTTAQVLIRFPMQR--NLVVIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19145 228 shPRfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQgeDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
109-282 |
1.06e-07 |
|
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: 52.57 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 109 LIHWP---TGFKPGKEFFPLDESGNVVPsdtnILDTWAAMEELVDEGLVKAIGISN--------FNHLQVEMilnkpGLK 177
Cdd:cd19094 118 QLHWPdryTPLFGGGYYTEPSEEEDSVS----FEEQLEALGELVKAGKIRHIGLSNetpwgvmkFLELAEQL-----GLP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 178 yKPAVNQiecHPY--LTQ---EKLIQYCQSKGIVVTAYSPLG----------SPDRpwakPEDPSLLEDPRI-------- 234
Cdd:cd19094 189 -RIVSIQ---NPYslLNRnfeEGLAEACHRENVGLLAYSPLAggvltgkyldGAAR----PEGGRLNLFPGYmaryrspq 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
2PDK_A 235 --------KAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSVTPERIAENFKVFDFELS 282
Cdd:cd19094 261 aleavaeyVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLS 318
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-78 |
1.88e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 51.55 E-value: 1.88e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2PDK_A 16 LGLGTWKSPPG-----QVTEAVKVAIDVGYRHIDCAHVYQN---ENEVGVAIQEKLREQVVKREELFIVSK 78
Cdd:cd19099 6 LGLGTYRGDSDdetdeEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTK 76
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-276 |
3.04e-07 |
|
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: 50.55 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 16 LGLGTW--------KSPPGQVTEAVKVAIDVGYRHIDCAHVYQN---ENEVGVAIQEKlreqvvkREELFIVSKLWCTYH 84
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 85 EKGL---------VKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkeffpldesgnvvPSDTNILDTWAAMEELVDEGLVK 155
Cdd:cd19086 79 GGPErpqdfspeyIREAVEASLKRLGTDYIDLYQLHNPP------------------DEVLDNDELFEALEKLKQEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 156 AIGISNFNHLQVEMILNKPGLKykpAV----NQIECHPYltqEKLIQYCQSKGIVVTAYSPLGSpdrpwakpedpSLLED 231
Cdd:cd19086 141 AYGVSVGDPEEALAALRRGGID---VVqviyNLLDQRPE---EELFPLAEEHGVGVIARVPLAS-----------GLLTG 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
2PDK_A 232 prikaiaakhnkTTAQVLIRFPMQRNLV--VIPKSVTPERIAENFKV 276
Cdd:cd19086 204 ------------KLAQAALRFILSHPAVstVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
132-289 |
7.10e-07 |
|
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: 49.92 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 132 VPSDTNILDTWAAMEELVDEGLVKAIGISNFNhlqVEMIlnKPGLKYKP--AVnQIECH-----PyltQEKLIQYCQSKG 204
Cdd:cd19078 119 VDPNVPIEEVAGTMKELIKEGKIRHWGLSEAG---VETI--RRAHAVCPvtAV-QSEYSmmwreP---EKEVLPTLEELG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 205 IVVTAYSPLGS--------PDRPWAKPEDPSLLedPR---------------IKAIAAKHNKTTAQVLIRFPMQR--NLV 259
Cdd:cd19078 190 IGFVPFSPLGKgfltgkidENTKFDEGDDRASL--PRftpealeanqalvdlLKEFAEEKGATPAQIALAWLLAKkpWIV 267
|
170 180 190
....*....|....*....|....*....|
2PDK_A 260 VIPKSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19078 268 PIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-282 |
1.66e-06 |
|
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: 48.70 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 14 PILGLGT--WKSPPGQVT-----EAVKVAIDVGYRHIDCAHVYQN-ENEVGVAIQEklreqvVKREELFIVSKLwCTYHE 85
Cdd:cd19090 1 SALGLGTagLGGVFGGVDddeavATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKV-GRLPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 86 K------GLVKGA---------------CQktlsdlkldyldlylIHWPTGFKPGKEFFPldesGNVVPsdtnildtwaA 144
Cdd:cd19090 74 DtadysaDRVRRSveeslerlgrdridlLM---------------IHDPERVPWVDILAP----GGALE----------A 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 145 MEELVDEGLVKAIGISnfnhlqvemiLNKPGLkYKPAV--NQIEC----HPY--LTQE---KLIQYCQSKGIVVTAYSPL 213
Cdd:cd19090 125 LLELKEEGLIKHIGLG----------GGPPDL-LRRAIetGDFDVvltaNRYtlLDQSaadELLPAAARHGVGVINASPL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 214 GS-------PDRPWAKPEDPSLLEDPR---IKAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSVTPERIAENFKVFDFEL 281
Cdd:cd19090 194 GMgllagrpPERVRYTYRWLSPELLDRakrLYELCDEHGVPLPALALRFLLRDPRIstVLVGASSPEELEQNVAAAEGPL 273
|
.
2PDK_A 282 S 282
Cdd:cd19090 274 P 274
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-283 |
5.20e-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: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 14 PILGLGT-------WKSPPGQVTEAVKVAIDVGYRHIDCAHVYQN---ENEVGVAIQEKLREQVVkreelfIVSKL-WCT 82
Cdd:cd19152 1 PKLGFGTaplgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRELGREDYV------ISTKVgRLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 83 YHEKGLVKGAcqktlsdlkldyldlylihwPTGFKPGKEFFP--------------------------------LDE--- 127
Cdd:cd19152 75 VPLQEVEPTF--------------------EPGFWNPLPFDAvfdysydgilrsiedslqrlglsridllsihdPDEdla 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 128 -SGNVVPSDTNILDTWAAMEELVDEGLVKAIGI-SNfnhlQVEMILnKPGLKYKPAVNQIEC------HPYLTqeKLIQY 199
Cdd:cd19152 135 gAESDEHFAQAIKGAFRALEELREEGVIKAIGLgVN----DWEVIL-RILEEADLDWVMLAGrytlldHSAAR--ELLPE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 200 CQSKGIVVTAYSPLGS--------PDRPWAKPEDPSLLE--DpRIKAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSVTP 267
Cdd:cd19152 208 CEKRGVKVVNAGPFNSgflaggdnFDYYEYGPAPPELIArrD-RIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSP 286
|
330
....*....|....*.
2PDK_A 268 ERIAENFKVFDFELSS 283
Cdd:cd19152 287 ERVEENVALLATEIPA 302
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-305 |
8.87e-06 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 46.74 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 1 MASRILLNNGAKMPILGLGTW---KSPPGQVTEAVKVAIDVGYRHIDCAHVY-QNENEVGVAIQEKlreqvvkREELFIV 76
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 77 SKL--WC-------TYHEKGLVKgaCQktlsdlkldyldLYLIH-------WPTGFKPGkeffpldesgnvvpsdtnilD 140
Cdd:COG1453 74 TKLppWVrdpedmrKDLEESLKR--LQtdy-------idLYLIHglnteedLEKVLKPG--------------------G 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 141 TWAAMEELVDEGLVKAIGISnfNHLQVEMIlnkpglkyKPAVN-------QIECHPYLTQ----EKLIQYCQSKGIVVTA 209
Cdd:COG1453 125 ALEALEKAKAEGKIRHIGFS--THGSLEVI--------KEAIDtgdfdfvQLQYNYLDQDnqagEEALEAAAEKGIGVII 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 210 YSPLGspdrpwakpeDPSLLEDP-RIKAIaAKHNKTTAQVLIRFPMQ--RNLVVIPKSVTPERIAENFKVFD-FE-LSSQ 284
Cdd:COG1453 195 MKPLK----------GGRLANPPeKLVEL-LCPPLSPAEWALRFLLShpEVTTVLSGMSTPEQLDENLKTADnLEpLTEE 263
|
330 340
....*....|....*....|.
2PDK_A 285 DMTTLLSYNRNWRVCALMSCT 305
Cdd:COG1453 264 ELAILERLAEELGELLKDFCT 284
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
135-274 |
1.21e-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: 46.20 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 135 DTNILDTWAAMEELVDEGLVKAIGIS-----------NFNHLQVEMILNKPGLKYKPAvnqiechpyltQEKLIQYCQSK 203
Cdd:cd19162 124 LQALTDAFPALEELRAEGVVGAIGVGvtdwaallraaRRADVDVVMVAGRYTLLDRRA-----------ATELLPLCAAK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 204 GIVVTAYSPLGS---------PDRPWAKPEDPSLLEDP-RIKAIAAKHNKTTAQVLIRFPMQRNLVVipkSV-----TPE 268
Cdd:cd19162 193 GVAVVAAGVFNSgilatddpaGDRYDYRPATPEVLARArRLAAVCRRYGVPLPAAALQFPLRHPAVA---SVvvgaaSPA 269
|
....*.
2PDK_A 269 RIAENF 274
Cdd:cd19162 270 ELRDNL 275
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
196-289 |
1.86e-05 |
|
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: 45.67 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 196 LIQYCQSKGIVVTAYSPLGS------------------PDRPWAKPEdpsllEDPR-------IKAIAAKHNKTTAQVLI 250
Cdd:cd19080 191 LLPMARALGLGVTPWSPLGGglltgkyqrgeegrageaKGVTVGFGK-----LTERnwaivdvVAAVAEELGRSAAQVAL 265
|
90 100 110 120
....*....|....*....|....*....|....*....|.
2PDK_A 251 RFPMQRNLVVIP--KSVTPERIAENFKVFDFELSSQDMTTL 289
Cdd:cd19080 266 AWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
134-285 |
3.01e-05 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 44.87 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 134 SDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILN---KPGL--------KYKPAVNQIECHpyltqekLIQYCQS 202
Cdd:cd19087 123 RDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaaRRGLlrfvseqpMYNLLKRQAELE-------ILPAARA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 203 KGIVVTAYSPLGS-----PDRPWAKPEDPSLLEDPRIKA----------------IAAKHNKTTAQVLIRFPMQRNLV-- 259
Cdd:cd19087 196 YGLGVIPYSPLAGglltgKYGKGKRPESGRLVERARYQArygleeyrdiaerfeaLAAEAGLTPASLALAWVLSHPAVts 275
|
170 180
....*....|....*....|....*...
2PDK_A 260 -VI-PKsvTPERIAENFKVFDFELSSQD 285
Cdd:cd19087 276 pIIgPR--TLEQLEDSLAALEITLTPEL 301
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
140-252 |
5.73e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 44.18 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 140 DTWAAMEELVDEGLVKAIGISNFNHLQ-VEMIL--NKPG--------LKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVT 208
Cdd:cd19104 142 GVADAFERLRSEGKIRFIGITGLGNPPaIRELLdsGKFDavqvyynlLNPSAAEARPRGWSAQDYGGIIDAAAEHGVGVM 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
2PDK_A 209 AYSPL------GSPDRPwakPEDPSLLEDP---------RIKAIAAKHNKTTAQVLIRF 252
Cdd:cd19104 222 GIRVLaagaltTSLDRG---REAPPTSDSDvaidfrraaAFRALAREWGETLAQLAHRF 277
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
132-284 |
1.38e-04 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 42.92 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 132 VPSDTNILD-TWAAMEELVDEGLVKAIGISNFN-HLQVEMILNKPG-----LKYkpavnqieCHPYL---TQEKLIQYCQ 201
Cdd:cd19163 128 APSLDQILNeTLPALQKLKEEGKVRFIGITGYPlDVLKEVLERSPVkidtvLSY--------CHYTLndtSLLELLPFFK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 202 SKGIVVTAYSPLG------SPDRPW--AKPEdpslledprIKAIAAK-------HNKTTAQVLIRFPMQR-----NLVVI 261
Cdd:cd19163 200 EKGVGVINASPLSmgllteRGPPDWhpASPE---------IKEACAKaaaycksRGVDISKLALQFALSNpdiatTLVGT 270
|
170 180
....*....|....*....|...
2PDK_A 262 PKsvtPERIAENFKVFDFELSSQ 284
Cdd:cd19163 271 AS---PENLRKNLEAAEEPLDAH 290
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
142-252 |
5.83e-04 |
|
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: 40.97 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 142 WAAMEELVDEGLVKAIGISNFNHLQVEMILNkpglKYKPAVNQIechPY------LTQEKLIQYCQSKGIVVTAYSP--- 212
Cdd:cd19097 121 VEALLELKKEGLIRKIGVSVYSPEELEKALE----SFKIDIIQL---PFnildqrFLKSGLLAKLKKKGIEIHARSVflq 193
|
90 100 110 120
....*....|....*....|....*....|....*....|....
2PDK_A 213 ---LGSPDRPWAKPED-PSLLEdpRIKAIAAKHNKTTAQVLIRF 252
Cdd:cd19097 194 gllLMEPDKLPAKFAPaKPLLK--KLHELAKKLGLSPLELALGF 235
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
138-278 |
6.74e-04 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 40.61 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 138 ILDTwaaMEELVDEGLVKAIGISNFNHlqvEMIL---------NKPGlkykPAVNQI---------ECHPYLT----QEK 195
Cdd:cd19082 123 IVDT---LNELVRAGKIRAFGASNWST---ERIAeanayakahGLPG----FAASSPqwslarpnePPWPGPTlvamDEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 196 LIQYCQSKGIVVTAYSPLGS---PDRpwAKPEDPSLLEDP-------------RIKAIAAKHNKTTAQVLIRFPMQRNLV 259
Cdd:cd19082 193 MRAWHEENQLPVFAYSSQARgffSKR--AAGGAEDDSELRrvyyseenferleRAKELAEEKGVSPTQIALAYVLNQPFP 270
|
170 180
....*....|....*....|.
2PDK_A 260 VIP--KSVTPERIAENFKVFD 278
Cdd:cd19082 271 TVPiiGPRTPEQLRDSLAAAD 291
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
133-289 |
7.73e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 40.34 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 133 PSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEmilnkPGLKYKPAVNqIECHPYLTQ---EKLIQYCQSKGIVVTA 209
Cdd:PRK10376 138 PAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVA-----EARKIAEIVC-VQNHYNLAHradDALIDALARDGIAYVP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 210 YSPLG--SPdrpwakpedpslLEDPRIKAIAAKHNKTTAQVLIRFPMQR--NLVVIPKSVTPERIAENFKVFDFELSSQD 285
Cdd:PRK10376 212 FFPLGgfTP------------LQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEV 279
|
....
2PDK_A 286 MTTL 289
Cdd:PRK10376 280 LAEL 283
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-80 |
1.74e-03 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 39.64 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 1 MASRILLNNGAKMPILGLGTWKSPPGQVTEAV-----KVAIDVGYRHIDCAHVYQnENEVGVAIQEKLREQVVKREELFI 75
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYA-AGKAEVILGSIIKKKGWRRSSLVI 79
|
....*
2PDK_A 76 VSKLW 80
Cdd:cd19159 80 TTKLY 84
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
135-287 |
8.81e-03 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 37.38 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 135 DTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEM---ILNK---PGLKYKPAVNQIECHPyltQEKLIQYCQSKGIVVT 208
Cdd:cd19151 130 ETPLEETMGALDQIVRQGKALYVGISNYPPEEAREaaaILKDlgtPCLIHQPKYSMFNRWV---EEGLLDVLEEEGIGCI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PDK_A 209 AYSPL-----------GSPD-----RPWA--KPED--PSLLEDPR-IKAIAAKHNKTTAQVLIRFPMQRNLV--VIPKSV 265
Cdd:cd19151 207 AFSPLaqglltdrylnGIPEdsraaKGSSflKPEQitEEKLAKVRrLNEIAQARGQKLAQMALAWVLRNKRVtsVLIGAS 286
|
170 180
....*....|....*....|...
2PDK_A 266 TPERIAENFKVFD-FELSSQDMT 287
Cdd:cd19151 287 KPSQIEDAVGALDnREFSEEELA 309
|
|
| |
