|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
1-276 |
0e+00 |
|
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: 617.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 1 MVAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVD 80
Cdd:cd19108 28 KALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCTFHRPELVRPALEKSLKKLQLDYVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 81 LYLIHCPVSMKPGNDLIPTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRYKPVCNQVE 160
Cdd:cd19108 108 LYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 161 CHPYLNQSKLLDYCKSKDIVLVAYGALGSQRCKNWIEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSF 240
Cdd:cd19108 188 CHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSF 267
|
250 260 270
....*....|....*....|....*....|....*.
gi 890826288 241 NEKRIKENLKVFEFHLPAEDMAVIDRLNRNYRYATA 276
Cdd:cd19108 268 NEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
2-287 |
4.40e-160 |
|
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: 447.71 E-value: 4.40e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19109 23 CAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHPPELVRPTLERTLKVLQLDYVDL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKPGNDLIPTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRYKPVCNQVEC 161
Cdd:cd19109 103 YIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRRQLELILNKPGLKHKPVSNQVEC 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGSQRCKNWIEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:cd19109 183 HPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFN 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVIDRLNRNYRYATARIISAHPNYPF 287
Cdd:cd19109 263 PERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
2-291 |
1.77e-128 |
|
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: 367.51 E-value: 1.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19107 19 VTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLVKGACQKTLSDLKLDYLDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKPGNDLIPTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRYKPVCNQVEC 161
Cdd:cd19107 99 YLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIERILNKPGLKYKPAVNQIEC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGSQRcKNWIEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:cd19107 179 HPYLTQEKLIQYCQSKGIVVTAYSPLGSPD-RPWAKPEDPSLLEDPKIKEIAAKHNKTTAQVLIRFPIQRNLVVIPKSVT 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVIDRLNRNYRYATARIISAHPNYPFLDEY 291
Cdd:cd19107 258 PERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
2-273 |
3.12e-120 |
|
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: 346.68 E-value: 3.12e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKV-ADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVD 80
Cdd:cd19106 22 VKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLWNTKHHPEDVEPALRKTLKDLQLDYLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 81 LYLIHCPVSMKPGNDLIPTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQVE 160
Cdd:cd19106 102 LYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVA--RIKPAVLQVE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 161 CHPYLNQSKLLDYCKSKDIVLVAYGALGSQRcKNWIEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSF 240
Cdd:cd19106 180 CHPYLAQNELIAHCKARGLVVTAYSPLGSPD-RPWAKPDEPVLLEEPKVKALAKKYNKSPAQILLRWQVQRGVVVIPKSV 258
|
250 260 270
....*....|....*....|....*....|...
gi 890826288 241 NEKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19106 259 TPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
2-291 |
1.49e-116 |
|
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: 337.32 E-value: 1.49e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19110 19 VTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKTACTRSLKALKLNYLDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKPGNDLIPTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRYKPVCNQVEC 161
Cdd:cd19110 99 YLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLNKPGLRVKPVTNQIEC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGSQrcknwiEENAPyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:cd19110 179 HPYLTQKKLISFCQSRNVSVTAYRPLGGS------CEGVD-LIDDPVIQRIAKKHGKSPAQILIRFQIQRNVIVIPKSVT 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVIDRLNRNYRYATARIISAHPNYPFLDEY 291
Cdd:cd19110 252 PSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
2-273 |
2.43e-115 |
|
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: 333.87 E-value: 2.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19116 27 VRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHEREQVEPALRESLKRLGLDYVDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKPGNDlipTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNkpGLRYKPVCNQVEC 161
Cdd:cd19116 107 YLIHWPVAFKENND---SESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLS--NCNIKPAVNQIEV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGSQRCKNwiEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:cd19116 182 HPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRG--QTNPPPRLDDPTLVAIAKKYGKTTAQIVLRYLIDRGVVPIPKSSN 259
|
250 260 270
....*....|....*....|....*....|..
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19116 260 KKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
2-265 |
3.26e-115 |
|
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: 331.75 E-value: 3.26e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVadgtVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19071 16 TAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREALEESLKDLGLDYLDL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSmkpgndliptdenGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQVEC 161
Cdd:cd19071 92 YLIHWPVP-------------GKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAA--RIKPAVNQIEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGSQRCKnwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:cd19071 157 HPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP---------LLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSN 227
|
250 260
....*....|....*....|....
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19071 228 PERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
5-272 |
2.03e-112 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 326.68 E-value: 2.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 5 ATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYLI 84
Cdd:cd19154 30 AVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTHEHAPEDVEEALRESLKKLQLEYVDLYLI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 85 HCPVSMKPGNDLIPTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQVECHPY 164
Cdd:cd19154 110 HAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNA--RVKPHNNQVECHLY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 165 LNQSKLLDYCKSKDIVLVAYGALGSQRCKN----WIEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSF 240
Cdd:cd19154 188 FPQKELVEFCKKHNISVTSYATLGSPGRANftksTGVSPAPNLLQDPIVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSA 267
|
250 260 270
....*....|....*....|....*....|..
gi 890826288 241 NEKRIKENLKVFEFHLPAEDMAVIDRLNRNYR 272
Cdd:cd19154 268 TPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
2-273 |
6.66e-109 |
|
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: 317.43 E-value: 6.66e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19123 27 VGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNSHAPEDVLPALEKTLADLQLDYLDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKPGNdLIPTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQVEC 161
Cdd:cd19123 107 YLMHWPVALKKGV-GFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLATA--RIKPAVNQVEL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGS-QRCKNWIEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSF 240
Cdd:cd19123 184 HPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSV 263
|
250 260 270
....*....|....*....|....*....|...
gi 890826288 241 NEKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19123 264 NPERIQQNLEAAEVELDASDMATIAALDRHHRY 296
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
2-273 |
2.88e-106 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 309.29 E-value: 2.88e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRskvADGtVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:COG0656 20 AAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA---ASG-VPREELFVTTKVWNDNHGYDDTLAAFEESLERLGLDYLDL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSmkpgndliptdengkllfdtVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGlrYKPVCNQVEC 161
Cdd:COG0656 96 YLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG--VKPAVNQVEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:COG0656 154 HPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVT 222
|
250 260 270
....*....|....*....|....*....|..
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:COG0656 223 PERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
1-265 |
4.56e-98 |
|
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: 289.63 E-value: 4.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 1 MVAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVD 80
Cdd:cd19125 25 VVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAPEDVPPALEKTLKDLQLDYLD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 81 LYLIHCPVSMKPGNdliPTDENGKLLfdTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQVE 160
Cdd:cd19125 105 LYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVA--RVPPAVNQVE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 161 CHPYLNQSKLLDYCKSKDIVLVAYGALGSQRcKNWIEENapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSF 240
Cdd:cd19125 178 CHPGWQQDKLHEFCKSKGIHLSAYSPLGSPG-TTWVKKN---VLKDPIVTKVAEKLGKTPAQVALRWGLQRGTSVLPKST 253
|
250 260
....*....|....*....|....*
gi 890826288 241 NEKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19125 254 NEERIKENIDVFDWSIPEEDFAKFS 278
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
2-272 |
2.71e-96 |
|
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: 285.96 E-value: 2.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19155 27 IETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGNRREKVEKFLLKSLEKLQLDYVDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPV-SMKPGNDLIPTDENGKLLFD-TVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQV 159
Cdd:cd19155 107 YLIHFPVgSLSKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNA--RIKPANLQV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 160 ECHPYLNQSKLLDYCKSKDIVLVAYGALGSQRCKNW------IEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGI 233
Cdd:cd19155 185 ELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFspgtgsPSGSSPDLLQDPVVKAIAERHGKSPAQVLLRWLMQRGV 264
|
250 260 270
....*....|....*....|....*....|....*....
gi 890826288 234 VIVTKSFNEKRIKENLKVFEFHLPAEDMAVIDRLNRNYR 272
Cdd:cd19155 265 VVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
2-273 |
6.50e-89 |
|
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: 266.29 E-value: 6.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19111 19 VRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDTEKSLEKSLENLKLPYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKpgndlipTDENGKLLFDT-VDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQVE 160
Cdd:cd19111 99 YLIHHPCGFV-------NKKDKGERELAsSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA--KVKPSNLQLE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 161 CHPYLNQSKLLDYCKSKDIVLVAYGALGS-QRCKNWIEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKS 239
Cdd:cd19111 170 CHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELDKTPAQVLLRFVLQRGTGVLPKS 249
|
250 260 270
....*....|....*....|....*....|....
gi 890826288 240 FNEKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19111 250 TNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
2-271 |
1.03e-87 |
|
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: 263.20 E-value: 1.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRskvaDGTVRREDIFYTSKLPCTCHRPelVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19117 29 VAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLWCTWHRR--VEEALDQSLKKLGLDYVDL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKPGNDLIPTDENGKLLFDTV--DLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRYKPVCNQV 159
Cdd:cd19117 103 YLMHWPVPLDPDGNDFLFKKDDGTKDHEPdwDFIKTWELMQKLPATGKVKAIGVSNFSIKNLEKLLASPSAKIVPAVNQI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 160 ECHPYLNQSKLLDYCKSKDIVLVAYGALGSQrcknwieeNAPyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKS 239
Cdd:cd19117 183 ELHPLLPQPKLVDFCKSKGIHATAYSPLGST--------NAP-LLKEPVIIKIAKKHGKTPAQVIISWGLQRGYSVLPKS 253
|
250 260 270
....*....|....*....|....*....|..
gi 890826288 240 FNEKRIKENLKVFEfhLPAEDMAVIDRLNRNY 271
Cdd:cd19117 254 VTPSRIESNFKLFT--LSDEEFKEIDELHKEY 283
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-267 |
4.79e-87 |
|
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: 4.79e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVR-REDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYLIHCP 87
Cdd:cd19124 29 AIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAHPDLVLPALKKSLRNLQLEYVDLYLIHWP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 88 VSMKPGNDLIPTDENGKLLFdtvDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRykPVCNQVECHPYLNQ 167
Cdd:cd19124 109 VSLKPGKFSFPIEEEDFLPF---DIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFATIP--PAVNQVEMNPAWQQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 168 SKLLDYCKSKDIVLVAYGALGSqRCKNWieeNAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFNEKRIKE 247
Cdd:cd19124 184 KKLREFCKANGIHVTAYSPLGA-PGTKW---GSNAVMESDVLKEIAAAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQ 259
|
250 260
....*....|....*....|
gi 890826288 248 NLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19124 260 NLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
2-267 |
1.13e-86 |
|
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: 260.42 E-value: 1.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIR-SKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVD 80
Cdd:cd19118 22 VGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKeLLKEEPGVKREDLFITSKLWNNSHRPEYVEPALDDTLKELGLDYLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 81 LYLIHCPVSMKPGNDL-----IPTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRykPV 155
Cdd:cd19118 102 LYLIHWPVAFKPTGDLnpltaVPTNGGEVDLDLSVSLVDTWKAMVELKKTGKVKSIGVSNFSIDHLQAIIEETGVV--PA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 156 CNQVECHPYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVI 235
Cdd:cd19118 180 VNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEVKAIAAKLGKTPAQVLIAWGIQRGHSV 253
|
250 260 270
....*....|....*....|....*....|..
gi 890826288 236 VTKSFNEKRIKENLKVFEfhLPAEDMAVIDRL 267
Cdd:cd19118 254 IPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
5-273 |
1.75e-86 |
|
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: 260.47 E-value: 1.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 5 ATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYLI 84
Cdd:cd19129 24 AVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERVKPAFEASLKRLQLDYLDLYLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 85 HCPVSMKPGNDLIPTDENGKLLFDT-VDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQVECHP 163
Cdd:cd19129 104 HTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAA--RIKPAVVQVESHP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 164 YLNQSKLLDYCKSKDIVLVAYGALGSQrcknwIEenaPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFNEK 243
Cdd:cd19129 182 YLPEWELLDFCKNHGIVLQAFAPLGHG-----ME---PKLLEDPVITAIARRVNKTPAQVLLAWAIQRGTALLTTSKTPS 253
|
250 260 270
....*....|....*....|....*....|.
gi 890826288 244 RIKENLKVFEfhLPAEDMAVI-DRLNRNYRY 273
Cdd:cd19129 254 RIRENFDIST--LPEDAMREInEGIKTRYRF 282
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
1-265 |
1.55e-84 |
|
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: 253.73 E-value: 1.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 1 MVAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIrskvADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVD 80
Cdd:cd19073 15 DCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDLKKSVDRSLEKLGTDYVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 81 LYLIHCPVSmkpgndliptdengkllfdTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLryKPVCNQVE 160
Cdd:cd19073 91 LLLIHWPNP-------------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL--PIAVNQVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 161 CHPYLNQSKLLDYCKSKDIVLVAYGALGsQRCknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSF 240
Cdd:cd19073 150 FHPFLYQAELLEYCRENDIVITAYSPLA-RGE----------VLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKAS 218
|
250 260
....*....|....*....|....*
gi 890826288 241 NEKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19073 219 SEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
2-273 |
2.50e-81 |
|
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: 246.38 E-value: 2.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRskvaDGTVRREDIFYTSKLPCtchRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19120 27 LVDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP---GIKDPREALRKSLAKLGVDYVDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKPGndliptdengkllfdTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQVEC 161
Cdd:cd19120 100 YLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTA--KIKPAVNQIEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLN--QSKLLDYCKSKDIVLVAYGALGSqrcknwIEENAPYLLeDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKS 239
Cdd:cd19120 163 HPYLYpqQPALLEYCREHGIVVSAYSPLSP------LTRDAGGPL-DPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTS 235
|
250 260 270
....*....|....*....|....*....|....
gi 890826288 240 FNEKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19120 236 SKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
2-267 |
6.46e-81 |
|
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: 245.90 E-value: 6.46e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGtVRREDIFYTSKLPCTCHRPelVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19121 27 VKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWSTYHRR--VELCLDRSLKSLGLDYVDL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKP-GN-DLIPTDENGKLLFD-TVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILnkPGLRYKPVCNQ 158
Cdd:cd19121 104 YLVHWPVLLNPnGNhDLFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTKAIGVSNYSIPYLEELL--KHATVVPAVNQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 159 VECHPYLNQSKLLDYCKSKDIVLVAYGALGSQrcknwieeNAPyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTK 238
Cdd:cd19121 182 VENHPYLPQQELVDFCKEKGILIEAYSPLGST--------GSP-LISDEPVVEIAKKHNVGPGTVLISYQVARGAVVLPK 252
|
250 260
....*....|....*....|....*....
gi 890826288 239 SFNEKRIKENLKVFEFHlpAEDMAVIDRL 267
Cdd:cd19121 253 SVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
1-267 |
9.54e-79 |
|
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: 239.46 E-value: 9.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 1 MVAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVD 80
Cdd:cd19136 16 EVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARAACLGSLERLGTDYLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 81 LYLIHCP-VSMKPGNDliptDENGKLLFdtvdlcDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLryKPVCNQV 159
Cdd:cd19136 96 LYLIHWPgVQGLKPSD----PRNAELRR------ESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEV--PPAVNQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 160 ECHPYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenaPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKS 239
Cdd:cd19136 164 EFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD---------LRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKS 234
|
250 260
....*....|....*....|....*...
gi 890826288 240 FNEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19136 235 TNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
9-273 |
3.53e-78 |
|
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: 240.02 E-value: 3.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYLIHCPV 88
Cdd:cd19115 35 AIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 89 SMK---PGNDLIPT--DENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNrRQLEMILnkpgLRY---KPVCNQVE 160
Cdd:cd19115 115 ALKyvdPAVRYPPGwfYDGKKVEFSNAPIQETWTAMEKLVDKGLARSIGVSNFS-AQLLMDL----LRYariRPATLQIE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 161 CHPYLNQSKLLDYCKSKDIVLVAYGALGSQrckNWIE------ENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIV 234
Cdd:cd19115 190 HHPYLTQPRLVKYAQKEGIAVTAYSSFGPQ---SFLEldlpgaKDTPPLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIA 266
|
250 260 270
....*....|....*....|....*....|....*....
gi 890826288 235 IVTKSFNEKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19115 267 VIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
4-268 |
1.39e-77 |
|
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: 236.18 E-value: 1.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSkvadGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYL 83
Cdd:cd19126 27 RAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWNDDQRARRTEDAFQESLDRLGLDYVDLYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 84 IHCPVSMKpgndliptdengkllfdtvdLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCNQVECHP 163
Cdd:cd19126 103 IHWPGKDK--------------------FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHA--DVVPAVNQVEFHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 164 YLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFNEK 243
Cdd:cd19126 161 YLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHAS 229
|
250 260
....*....|....*....|....*
gi 890826288 244 RIKENLKVFEFHLPAEDMAVIDRLN 268
Cdd:cd19126 230 RIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
2-268 |
3.66e-77 |
|
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: 235.34 E-value: 3.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRskvaDGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19131 25 AASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWNSDQGYDSTLRAFDESLRKLGLDYVDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKpgndliptdenGKLLfdtvdlcDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLryKPVCNQVEC 161
Cdd:cd19131 101 YLIHWPVPAQ-----------DKYV-------ETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGV--VPVVNQIEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:cd19131 161 HPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVT 229
|
250 260
....*....|....*....|....*..
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVIDRLN 268
Cdd:cd19131 230 PSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
1-269 |
3.57e-76 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 232.93 E-value: 3.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 1 MVAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIR-SKVAdgtvrREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYV 79
Cdd:cd19132 21 EGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRrSGVP-----REELFVTTKLPGRHHGYEEALRTIEESLYRLGLDYV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 80 DLYLIHCPVsmkPGNDLiptdengkllfdtvdLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLryKPVCNQV 159
Cdd:cd19132 96 DLYLIHWPN---PSRDL---------------YVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGV--TPAVNQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 160 ECHPYLNQSKLLDYCKSKDIVLVAYGALGsqrcknwieeNAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKS 239
Cdd:cd19132 156 ELHPYFPQAEQRAYHREHGIVTQSWSPLG----------RGSGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKS 225
|
250 260 270
....*....|....*....|....*....|
gi 890826288 240 FNEKRIKENLKVFEFHLPAEDMAVIDRLNR 269
Cdd:cd19132 226 ANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
2-273 |
2.38e-75 |
|
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: 231.13 E-value: 2.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRskvaDGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19157 26 VVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKVWNADQGYDSTLKAFEASLERLGLDYLDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVsmkpgndliptdeNGKLLfdtvdlcDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLryKPVCNQVEC 161
Cdd:cd19157 102 YLIHWPV-------------KGKYK-------ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEI--VPMVNQVEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:cd19157 160 HPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIK 228
|
250 260 270
....*....|....*....|....*....|..
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19157 229 EHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-273 |
3.19e-75 |
|
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: 232.34 E-value: 3.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYLIHCPV 88
Cdd:cd19113 33 AIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 89 SMKPgndlIPTDE----------NGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNkpGLRYKPVCNQ 158
Cdd:cd19113 113 AFKF----VPIEEkyppgfycgdGDNFVYEDVPILDTWKALEKLVDAGKIKSIGVSNFPGALILDLLR--GATIKPAVLQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 159 VECHPYLNQSKLLDYCKSKDIVLVAYGALGSQ---RCKNWIEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVI 235
Cdd:cd19113 187 IEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvELNQGRALNTPTLFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAV 266
|
250 260 270
....*....|....*....|....*....|....*...
gi 890826288 236 VTKSFNEKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19113 267 IPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
2-267 |
2.82e-73 |
|
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: 225.22 E-value: 2.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAI-RSKVAdgtvrREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVD 80
Cdd:cd19140 23 CTRAVEHALELGYRHIDTAQMYGNEAQVGEAIaASGVP-----RDELFLTTKVWPDNYSPDDFLASVEESLRKLRTDYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 81 LYLIHCPVSmkpgndliptdengkllfdTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLryKPVCNQVE 160
Cdd:cd19140 98 LLLLHWPNK-------------------DVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEA--PLFTNQVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 161 CHPYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQR-GIVIVTKS 239
Cdd:cd19140 157 YHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAIPKA 225
|
250 260
....*....|....*....|....*...
gi 890826288 240 FNEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19140 226 TNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-275 |
4.38e-73 |
|
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: 226.60 E-value: 4.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHrpELVQPCLEQSLRKLQLDYVDLYLIHCPV 88
Cdd:cd19112 33 AIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNSDH--GHVIEACKDSLKKLQLDYLDLYLVHFPV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 89 SMK------PGNDLiptDENGKLLFD-TVDLCDTWEAMEKCKDSGLAKSIGVSNFnrrqlEMILNKPGLRY---KPVCNQ 158
Cdd:cd19112 111 ATKhtgvgtTGSAL---GEDGVLDIDvTISLETTWHAMEKLVSAGLVRSIGISNY-----DIFLTRDCLAYskiKPAVNQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 159 VECHPYLNQSKLLDYCKSKDIVLVAYGALGSQRC-KNWIEENAPylLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVT 237
Cdd:cd19112 183 IETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAAnAEWFGSVSP--LDDPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIP 260
|
250 260 270
....*....|....*....|....*....|....*...
gi 890826288 238 KSFNEKRIKENLKVFEFHLPAEDMAVIDRLNRNYRYAT 275
Cdd:cd19112 261 KSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQ 298
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
2-267 |
9.16e-73 |
|
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: 224.71 E-value: 9.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19128 16 SKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQLLITLQDLQLEYLDL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKPGNDLIPTDENGKLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKpgLRYKPVCNQVEC 161
Cdd:cd19128 96 FLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY--CKIKPFMNQIEC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGAL-GSQRCKNwieeNAPylLEDPTLCAMAEKHKQTPALISLRYLLQR---GIVIVT 237
Cdd:cd19128 174 HPYFQNDKLIKFCIENNIHVTAYRPLgGSYGDGN----LTF--LNDSELKALATKYNTTPPQVIIAWHLQKwpkNYSVIP 247
|
250 260 270
....*....|....*....|....*....|
gi 890826288 238 KSFNEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19128 248 KSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
3-273 |
1.07e-72 |
|
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: 224.32 E-value: 1.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 3 AKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKvadgTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLY 82
Cdd:cd19156 26 ENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWNSDQGYESTLAAFEESLEKLGLDYVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 83 LIHCPVSmkpgndliptdenGKLLfdtvdlcDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRykPVCNQVECH 162
Cdd:cd19156 102 LIHWPVK-------------GKFK-------DTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVA--PMVNQIELH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 163 PYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFNE 242
Cdd:cd19156 160 PLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHE 228
|
250 260 270
....*....|....*....|....*....|.
gi 890826288 243 KRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19156 229 ERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
4-268 |
3.66e-69 |
|
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: 214.75 E-value: 3.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSAYFYQNEEEVGLAIRskvaDGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYL 83
Cdd:cd19133 27 RAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLWIQDAGYEKAKKAFERSLKRLGLDYLDLYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 84 IHCPVSmkpgndliptDENGkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILnkPGLRYKPVCNQVECHP 163
Cdd:cd19133 103 IHQPFG----------DVYG-----------AWRAMEELYKEGKIRAIGVSNFYPDRLVDLI--LHNEVKPAVNQIETHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 164 YLNQSKLLDYCKSKDIVLVAYGALGsqrcknwieENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFNEK 243
Cdd:cd19133 160 FNQQIEAVEFLKKYGVQIEAWGPFA---------EGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPE 230
|
250 260
....*....|....*....|....*
gi 890826288 244 RIKENLKVFEFHLPAEDMAVIDRLN 268
Cdd:cd19133 231 RIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
9-273 |
2.40e-68 |
|
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: 214.34 E-value: 2.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYLIHCPV 88
Cdd:cd19114 26 AIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHVREAFDRQLKDYGLDYIDLYLIHFPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 89 SMK---PGNDLIPTDENG---KLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNrrqLEMILNKpgLRY---KPVCNQV 159
Cdd:cd19114 106 PAAyvdPAENYPFLWKDKelkKFPLEQSPMQECWREMEKLVDAGLVRNIGIANFN---VQLILDL--LTYakiKPAVLQI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 160 ECHPYLNQSKLLDYCKSKDIVLVAYGALGSQRCKNWIEENAPY--LLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVT 237
Cdd:cd19114 181 EHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVVKKLADKHKRDTGQVLLRWAVQRNITVIP 260
|
250 260 270
....*....|....*....|....*....|....*.
gi 890826288 238 KSFNEKRIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19114 261 KSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
11-267 |
3.48e-67 |
|
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: 210.26 E-value: 3.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 11 DAGFRHIDSAYFYQNEEEVGLAIRskvADGtVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYLIHCPVSM 90
Cdd:cd19135 37 ECGYRHIDTAKRYGCEELLGKAIK---ESG-VPREDLFLTTKLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 91 KPGNDLIPTDEngkllfdtvdlcDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRykPVCNQVECHPYLNQSKL 170
Cdd:cd19135 113 SSGKNVKETRA------------ETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 171 LDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFNEKRIKENLK 250
Cdd:cd19135 179 IEYCRDNNIVFEGYCPLAKGK-----------ALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQ 247
|
250
....*....|....*..
gi 890826288 251 VFEFHLPAEDMAVIDRL 267
Cdd:cd19135 248 VFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
2-271 |
1.76e-66 |
|
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: 209.28 E-value: 1.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADGTVRREDIFYTSKLPCTCHRPelVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19119 29 VKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPTFYDE--VERSLDESLKALGLDYVDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVSMKPGND-----LIPTDENGKLLF-DTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKpgLRYKPV 155
Cdd:cd19119 107 LLVHWPVCFEKDSDdsgkpFTPVNDDGKTRYaASGDHITTYKQLEKIYLDGRAKAIGVSNYSIVYLERLIKE--CKVVPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 156 CNQVECHPYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenAPyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVI 235
Cdd:cd19119 185 VNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHG--------AP-NLKNPLVKKIAEKYNVSTGDILISYHVRQGVIV 255
|
250 260 270
....*....|....*....|....*....|....*.
gi 890826288 236 VTKSFNEKRIKENLKVfeFHLPAEDMAVIDRLNRNY 271
Cdd:cd19119 256 LPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGEKY 289
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
2-268 |
8.17e-66 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 207.55 E-value: 8.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFY---QNEEEVGLAIRSKVadgtVRREDIFYTSKLP------CTCHRPELVQPCLEQSLR 72
Cdd:pfam00248 20 ALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYP----VKRDKVVIATKVPdgdgpwPSGGSKENIRKSLEESLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 73 KLQLDYVDLYLIHCPvsmkpgndliptdengkllFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGlrY 152
Cdd:pfam00248 96 RLGTDYIDLYYLHWP-------------------DPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK--I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 153 KPVCNQVECHPY--LNQSKLLDYCKSKDIVLVAYGALGS----------------QRCKNWIEENAPYLLEDPTLCAMAE 214
Cdd:pfam00248 155 PIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgERRRLLKKGTPLNLEALEALEEIAK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 890826288 215 KHKQTPALISLRYLLQR---GIVIVtKSFNEKRIKENLKVFEFHLPAEDMAVIDRLN 268
Cdd:pfam00248 235 EHGVSPAQVALRWALSKpgvTIPIP-GASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
3-268 |
1.67e-65 |
|
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: 206.10 E-value: 1.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 3 AKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADgtvrREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLY 82
Cdd:cd19127 25 ADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVD----RSDIFVTTKLWISDYGYDKALRGFDASLRRLGLDYVDLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 83 LIHCPVsmkpgndliPTDengkllFDtvDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLryKPVCNQVECH 162
Cdd:cd19127 101 LLHWPV---------PND------FD--RTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTV--VPAVNQVELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 163 PYLNQSKLLDYCKSKDIVLVAYGALGS--QRCKNWIEEnAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSF 240
Cdd:cd19127 162 PYFSQKDLRAFHRRLGIVTQAWSPIGGvmRYGASGPTG-PGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSV 240
|
250 260
....*....|....*....|....*...
gi 890826288 241 NEKRIKENLKVFEFHLPAEDMAVIDRLN 268
Cdd:cd19127 241 HPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
2-267 |
8.14e-64 |
|
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: 201.04 E-value: 8.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIrskvADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDL 81
Cdd:cd19139 16 VIDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKDKLLPSLEESLEKLRTDYVDL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPvsmkPGNDLIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRyKPVCNQVEC 161
Cdd:cd19139 92 TLIHWP----SPNDEVPVEE-------------YIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAG-AIATNQIEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:cd19139 154 SPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTK 222
|
250 260
....*....|....*....|....*.
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19139 223 REHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
4-267 |
2.72e-60 |
|
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: 193.61 E-value: 2.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSKVADG-TVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLY 82
Cdd:cd19122 28 AAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHLHEPEDVKWSIDNSLKNLKLDYIDLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 83 LIHCPVSMKPGNDLIPT-DENGKLLFDTvDLCD----TWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglRYKPVCN 157
Cdd:cd19122 108 LVHWPIAAEKNDQRSPKlGPDGKYVILK-DLTEnpepTWRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFA--KVKPHVN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 158 QVECHPYLNQSKLLDYCKSKDIVLVAYGALGSQrckNWIEENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVT 237
Cdd:cd19122 185 QIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQ---NQVPSTGERVSENPTLNEVAEKGGYSLAQVLIAWGLRRGYVVLP 261
|
250 260 270
....*....|....*....|....*....|
gi 890826288 238 KSFNEKRIKENLKVFEfhLPAEDMAVIDRL 267
Cdd:cd19122 262 KSSTPSRIESNFKSIE--LSDEDFEAINQV 289
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
3-268 |
5.19e-59 |
|
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: 188.97 E-value: 5.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 3 AKATKIAIDAGFRHIDSAYFYQNEEEVGLAIrskvADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLY 82
Cdd:cd19130 26 QRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDRHDGDEPAAAFAESLAKLGLDQVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 83 LIHCPVsmkPGNDliptdengkllfdtvDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLryKPVCNQVECH 162
Cdd:cd19130 102 LVHWPT---PAAG---------------NYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGV--VPAVNQIELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 163 PYLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFNE 242
Cdd:cd19130 162 PAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRR 230
|
250 260
....*....|....*....|....*.
gi 890826288 243 KRIKENLKVFEFHLPAEDMAVIDRLN 268
Cdd:cd19130 231 ERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-273 |
2.70e-58 |
|
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: 187.37 E-value: 2.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSAYFYQNEEEVGLAIRskvADGtVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYL 83
Cdd:cd19134 28 RSVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASG-IPRGELFVTTKLATPDQGFTASQAACRASLERLGLDYVDLYL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 84 IHCPVSmkpgndliptdENGKLLfdtvdlcDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGlrYKPVCNQVECHP 163
Cdd:cd19134 104 IHWPAG-----------REGKYV-------DSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTF--FTPAVNQIELHP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 164 YLNQSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFNEK 243
Cdd:cd19134 164 LLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPE 232
|
250 260 270
....*....|....*....|....*....|
gi 890826288 244 RIKENLKVFEFHLPAEDMAVIDRLNRNYRY 273
Cdd:cd19134 233 RIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
4-265 |
1.57e-55 |
|
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: 180.12 E-value: 1.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSAYFYQN---EEEVGLAIRskvadgTVRREDIFYTSKL-PCTCHRPELVQPClEQSLRKLQLDYV 79
Cdd:cd19072 30 EALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITTKVsPDHLKYDDVIKAA-KESLKRLGTDYI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 80 DLYLIHCPvsmkpgNDLIPtdengkllfdtvdLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGlRYKPVCNQV 159
Cdd:cd19072 103 DLYLIHWP------NPSIP-------------IEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLK-KGPIVANQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 160 ECHpYLNQ---SKLLDYCKSKDIVLVAYGALGSQRCKNWIeenapyllEDPTLCAMAEKHKQTPALISLRYLLQR-GIVI 235
Cdd:cd19072 163 EYN-LFDReeeSGLLPYCQKNGIAIIAYSPLEKGKLSNAK--------GSPLLDEIAKKYGKTPAQIALNWLISKpNVIA 233
|
250 260 270
....*....|....*....|....*....|
gi 890826288 236 VTKSFNEKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19072 234 IPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
2-272 |
1.19e-52 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 173.33 E-value: 1.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQNEEEVGLAIRSkvadGTVRREDIFYTSKLPCTCHRPelVQPCLEQSLRKLQLDYVDL 81
Cdd:PRK11565 30 VITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLWNDDHKR--PREALEESLKKLQLDYVDL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPVsmkPGNDLiptdengkllfdtvdLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLryKPVCNQVEC 161
Cdd:PRK11565 104 YLMHWPV---PAIDH---------------YVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGV--TPVINQIEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPYLNQSKLLDYCKSKDIVLVAYGALgSQRCKNwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFN 241
Cdd:PRK11565 164 HPLMQQRQLHAWNATHKIQTESWSPL-AQGGKG--------VFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVT 234
|
250 260 270
....*....|....*....|....*....|.
gi 890826288 242 EKRIKENLKVFEFHLPAEDMAVIDRLNRNYR 272
Cdd:PRK11565 235 PSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
7-272 |
4.03e-52 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 171.75 E-value: 4.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 7 KIAIDAGFRHIDSAYFYQNEEEVGLAIrskvADGTVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDYVDLYLIHC 86
Cdd:PRK11172 23 KTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDKLIPSLKESLQKLRTDYVDLTLIHW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 87 PvsmKPGNDliptdengkllfdtVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGlRYKPVCNQVECHPYLN 166
Cdd:PRK11172 99 P---SPNDE--------------VSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVG-AENIATNQIELSPYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 167 QSKLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVIVTKSFNEKRIK 246
Cdd:PRK11172 161 NRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLA 229
|
250 260
....*....|....*....|....*.
gi 890826288 247 ENLKVFEFHLPAEDMAVIDRLNRNYR 272
Cdd:PRK11172 230 SNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
4-265 |
1.67e-44 |
|
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: 152.02 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSAYFYQN---EEEVGLAIRSkvadgtvRREDIFYTSK-LPCTCHRPELVQPClEQSLRKLQLDYV 79
Cdd:cd19138 33 EALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG-------RRDKVFLVSKvLPSNASRQGTVRAC-ERSLRRLGTDYL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 80 DLYLIHCPVSmkpgndliptdengkllfdtVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRyKPVCNQV 159
Cdd:cd19138 105 DLYLLHWRGG--------------------VPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGG-NCAANQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 160 ECHpyLNQS----KLLDYCKSKDIVLVAYGALGSQRcknwieENAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRGIVI 235
Cdd:cd19138 164 LYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGG------LLRRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVI 235
|
250 260 270
....*....|....*....|....*....|.
gi 890826288 236 -VTKSFNEKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19138 236 aIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
2-265 |
4.19e-41 |
|
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: 143.09 E-value: 4.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFY---QNEEEVGLAIRSkvadgtVRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDY 78
Cdd:cd19137 28 MVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVTKVWPTNLRYDDLLRSLQNSLRRLDTDY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 79 VDLYLIHCPvsmkpgNDLIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKpgLRYKPVCNQ 158
Cdd:cd19137 102 IDLYLIHWP------NPNIPLEE-------------TLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISK--SQTPIVCNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 159 VECHPY---LNQSKLLDYCKSKDIVLVAYGALGSQrcknwieenapYLLEDPTLCAMAEKHKQTPALISLRYLLQR-GIV 234
Cdd:cd19137 161 VKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRG-----------LEKTNRTLEEIAKNYGKTIAQIALAWLIQKpNVV 229
|
250 260 270
....*....|....*....|....*....|.
gi 890826288 235 IVTKSFNEKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19137 230 AIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
9-267 |
2.23e-40 |
|
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: 142.62 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRSKvadgtvRREDIFYTSKLPCT--------CHRPELVQPCLEQSLRKLQLD 77
Cdd:COG0667 42 ALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIATKVGRRmgpgpngrGLSREHIRRAVEASLRRLGTD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 78 YVDLYLIHCPvsmkpgndliptDENgkllfdtVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLRYKPVCN 157
Cdd:COG0667 116 YIDLYQLHRP------------DPD-------TPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 158 QVEchpY--LNQS---KLLDYCKSKDIVLVAYGAL-----------------GSQRCKNWIeenAPYLLED-----PTLC 210
Cdd:COG0667 177 QNE---YslLDRSaeeELLPAARELGVGVLAYSPLagglltgkyrrgatfpeGDRAATNFV---QGYLTERnlalvDALR 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 890826288 211 AMAEKHKQTPALISLRYLLQRGIVIV----TKSfnEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:COG0667 251 AIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
9-270 |
7.97e-35 |
|
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: 127.32 E-value: 7.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQN---EEEVGLAIRSkvadgtvRREDIFYTSKL-PCTCHRPELVQPClEQSLRKLQLDYVDLYLI 84
Cdd:cd19085 32 ALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVsPDNLTPEDVRKSC-ERSLKRLGTDYIDLYQI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 85 HCPVSMkpgndliptdengkllfdtVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNkpglRYKPVCNQVechPY 164
Cdd:cd19085 104 HWPSSD-------------------VPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALD----AGRIDSNQL---PY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 165 --LNQSK---LLDYCKSKDIVLVAYGAL-----------------GSQRCKNWI---EENAPYLLED-PTLCAMAEKHKQ 218
Cdd:cd19085 158 nlLWRAIeyeILPFCREHGIGVLAYSPLaqglltgkfssaedfppGDARTRLFRhfePGAEEETFEAlEKLKEIADELGV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 890826288 219 TPALISLRYLLQR-GI--VIVTKSfNEKRIKENLKVFEFHLPAEDMAVIDRLNRN 270
Cdd:cd19085 238 TMAQLALAWVLQQpGVtsVIVGAR-NPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
4-265 |
3.87e-34 |
|
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: 125.72 E-value: 3.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSAYFYQN---EEEVGLAI---RSKV--AD--GTVRREDIFYTSKLpctchRPELVQPCLEQSLRK 73
Cdd:cd19084 29 EAIKAAIDLGINFFDTAPVYGFghsEEILGKALkgrRDDVviATkcGLRWDGGKGVTKDL-----SPESIRKEVEQSLRR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 74 LQLDYVDLYLIHCPvsmkpgndliptDENgkllfdtVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNkpglRYK 153
Cdd:cd19084 104 LQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARK----YGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 154 PVCNQVechPY--LNQ---SKLLDYCKSKDIVLVAYGALGS-------------------QRCKNWIEENAPYLLE--Dp 207
Cdd:cd19084 161 IVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAQglltgkykkeptfppddrrSRFPFFRGENFEKNLEivD- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 890826288 208 TLCAMAEKHKQTPALISLRYLLQR---GIVIV-TKsfNEKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19084 237 KLKEIAEKYGKSLAQLAIAWTLAQpgvTSAIVgAK--NPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
2-265 |
9.07e-34 |
|
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: 124.65 E-value: 9.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFY---QNEEEVGLAIRskvadGTVRREDIFYTSKLPCTCHR--PELVQPCLEQSLRKLQL 76
Cdd:cd19093 28 LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIATKFAPLPWRltRRSVVKALKASLERLGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 77 DYVDLYLIHCPVSMKPGNDLIptdengkllfdtvdlcdtWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNK-PGLRYKPV 155
Cdd:cd19093 103 DSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLVRAVGVSNYSADQLRRAHKAlKERGVPLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 156 CNQVE---CHPYLNQSKLLDYCKSKDIVLVAY-----GAL-GSQRCKNWIEEN-----APYLLE--DP---TLCAMAEKH 216
Cdd:cd19093 165 SNQVEyslLYRDPEQNGLLPACDELGITLIAYsplaqGLLtGKYSPENPPPGGrrrlfGRKNLEkvQPlldALEEIAEKY 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 890826288 217 KQTPALISLRYLLQRGIVIVTKSFNEKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19093 245 GKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
9-189 |
2.81e-26 |
|
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: 102.98 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRSKVadgtvRREDIFYTSKLpctCHR-----------PELVQPCLEQSLRKL 74
Cdd:cd06660 26 ALEAGGNFFDTADVYgdgRSERLLGRWLKGRG-----NRDDVVIATKG---GHPpggdpsrsrlsPEHIRRDLEESLRRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 75 QLDYVDLYLIHCPvsmkpgNDLIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILN---KPGLR 151
Cdd:cd06660 98 GTDYIDLYYLHRD------DPSTPVEE-------------TLEALNELVREGKIRYIGVSNWSAERLAEALAyakAHGLP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 890826288 152 yKPVCNQVE---CHPYLNQSKLLDYCKSKDIVLVAYGALGS 189
Cdd:cd06660 159 -GFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR 198
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
3-272 |
3.42e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 105.67 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 3 AKATKI---AIDAGFRHIDSAYFYQNEEE-VGLAIRSkvadgtvRREDIFYTSKLPCTCHRPELVQPCLEQSLRKLQLDY 78
Cdd:COG1453 29 EEAEALirrAIDNGINYIDTARGYGDSEEfLGKALKG-------PRDKVILATKLPPWVRDPEDMRKDLEESLKRLQTDY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 79 VDLYLIHCpvsMKPGNDL-IPTDENGkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQL----------EMILnk 147
Cdd:COG1453 102 IDLYLIHG---LNTEEDLeKVLKPGG-----------ALEALEKAKAEGKIRHIGFSTHGSLEVikeaidtgdfDFVQ-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 148 pgLRYkpvcNqvechpYLNQS-----KLLDYCKSKDIVLVAYGALGSQRcknwieenapyLLEDPTLCAMAEKHKQTPAL 222
Cdd:COG1453 166 --LQY----N------YLDQDnqageEALEAAAEKGIGVIIMKPLKGGR-----------LANPPEKLVELLCPPLSPAE 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 890826288 223 ISLRYLLQR-GIVIVTKSF-NEKRIKENLKVFEFHLP--AEDMAVIDRLNRNYR 272
Cdd:COG1453 223 WALRFLLSHpEVTTVLSGMsTPEQLDENLKTADNLEPltEEELAILERLAEELG 276
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
9-260 |
5.20e-26 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 104.08 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSA--Y-FYQNEEEVGLAIRSKvadgTVRREDIFYTSK----LPCTcHRPELVQP----------CLEQSL 71
Cdd:COG4989 40 ALELGITTFDHAdiYgGYTCEALFGEALKLS----PSLREKIELQTKcgirLPSE-ARDNRVKHydtskehiiaSVEGSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 72 RKLQLDYVDLYLIHCPvsmkpgndliptdengkllfDT-VDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMiLNKpGL 150
Cdd:COG4989 115 RRLGTDYLDLLLLHRP--------------------DPlMDPEEVAEAFDELKASGKVRHFGVSNFTPSQFEL-LQS-AL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 151 RYKPVCNQVECHPyLNQSKL----LDYCKSKDIVLVAYGALGSQRCKNWIEENAPYLLEdpTLCAMAEKHKQTPALISLR 226
Cdd:COG4989 173 DQPLVTNQIELSL-LHTDAFddgtLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRA--ALDELAEKYGVSPEAIALA 249
|
250 260 270
....*....|....*....|....*....|....*.
gi 890826288 227 YLLQR--GIVIVTKSFNEKRIKENLKVFEFHLPAED 260
Cdd:COG4989 250 WLLRHpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
2-260 |
5.61e-25 |
|
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: 101.09 E-value: 5.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAIDAGFRHIDSAYFYQN---EEEVGLAIRSKvadgTVRREDIFYTSK---LPCTCHRPELVQPC--------- 66
Cdd:cd19092 26 LLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKcgiRLGDDPRPGRIKHYdtskehila 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 67 -LEQSLRKLQLDYVDLYLIHCPvsmkpgndliptdengkllfDTvdLCDTWE---AMEKCKDSGLAKSIGVSNFNRRQLE 142
Cdd:cd19092 102 sVEGSLKRLGTDYLDLLLLHRP--------------------DP--LMDPEEvaeAFDELVKSGKVRYFGVSNFTPSQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 143 MiLNKpGLRYKPVCNQVEC---HPYLNQSKLLDYCKSKDIVLVAYGALGSQRCKNWIEENAPYLLEdpTLCAMAEKHKQT 219
Cdd:cd19092 160 L-LQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA--ALEELAEEYGVT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 890826288 220 PALISLRYLLQR--GIVIVTKSFNEKRIKENLKVFEFHLPAED 260
Cdd:cd19092 236 IEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
7-267 |
5.19e-24 |
|
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: 98.65 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 7 KIAIDAGFRHIDSAYFY---QNEEEVGLAIRSKvadgtvRREDIFYTSKlpcTCHR-----------PELVQPCLEQSLR 72
Cdd:cd19083 40 REALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATK---GAHKfggdgsvlnnsPEFLRSAVEKSLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 73 KLQLDYVDLYLIHCPvsmkpgNDLIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLEMiLNKPGlry 152
Cdd:cd19083 111 RLNTDYIDLYYIHFP------DGETPKAE-------------AVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDG--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 153 kpvcnQVEC--HPY--LNQ---SKLLDYCKSKDIVLV-----AYGALGSQRCKN-------WIEENAPYLLED------- 206
Cdd:cd19083 168 -----YVDVlqGEYnlLQReaeEDILPYCVENNISFIpyfplASGLLAGKYTKDtkfpdndLRNDKPLFKGERfsenldk 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 890826288 207 -PTLCAMAEKHKQTPALISLRYLLQR-GI-VIVTKSFNEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19083 243 vDKLKSIADEKGVTVAHLALAWYLTRpAIdVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
9-256 |
3.77e-23 |
|
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: 95.36 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRSKVAD-------GTVRREDifyTSKLPCTchRPELVQPCLEQSLRKLQLDY 78
Cdd:cd19088 33 ALELGVNFIDTADSYgpdVNERLIAEALHPYPDDvviatkgGLVRTGP---GWWGPDG--SPEYLRQAVEASLRRLGLDR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 79 VDLYLIHCPvsmkpgndliptdengkllFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLrykpVCNQ 158
Cdd:cd19088 108 IDLYQLHRI-------------------DPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI----VSVQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 159 VECHPYLNQS-KLLDYCKSKDIVLVAYGALGSqrcknwieenAPYLLEDPTLCAMAEKHKQTPALISLRYLLQRG--IVI 235
Cdd:cd19088 165 NRYNLANRDDeGVLDYCEAAGIAFIPWFPLGG----------GDLAQPGGLLAEVAARLGATPAQVALAWLLARSpvMLP 234
|
250 260
....*....|....*....|.
gi 890826288 236 VTKSFNEKRIKENLKVFEFHL 256
Cdd:cd19088 235 IPGTSSVEHLEENLAAAGLRL 255
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-267 |
8.20e-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: 92.74 E-value: 8.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRSkvadgtvRREDIFYTSKL---------PCTCHRPELVQPCLEQSLRKLQL 76
Cdd:cd19102 35 ALDLGINWIDTAAVYglgHSEEVVGRALKG-------LRDRPIVATKCgllwdeegrIRRSLKPASIRAECEASLRRLGV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 77 DYVDLYLIHCPVSmkpgndliptdengkllfdTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMIL-------NKPG 149
Cdd:cd19102 108 DVIDLYQIHWPDP-------------------DEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQaihpiasLQPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 150 lrYKPVCNQVEchpylnqSKLLDYCKSKDIVLVAY---------GALGSQRCKN-----WiEENAPYLLED--------- 206
Cdd:cd19102 169 --YSLLRRGIE-------AEILPFCAEHGIGVIVYspmqsglltGKMTPERVASlpaddW-RRRSPFFQEPnlarnlalv 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 890826288 207 PTLCAMAEKHKQTPALISLRYLLQRGIV---IVtKSFNEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19102 239 DALRPIAERHGRTVAQLAIAWVLRRPEVtsaIV-GARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
9-253 |
2.50e-20 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 87.62 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRskvadgTVRREDIFYTSKLPC-TCHRPELVQPCLEQSLRKLQLDYVDLYLI 84
Cdd:cd19096 30 AIDAGINYFDTAYGYgggKSEEILGEALK------EGPREKFYLATKLPPwSVKSAEDFRRILEESLKRLGVDYIDFYLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 85 HCPVSMKpgndliptdengklLFDTVDLCDTWEAMEKCKDSGLAKSIGVSnF--NRRQLEMILNkpglrykpvCNQVEC- 161
Cdd:cd19096 104 HGLNSPE--------------WLEKARKGGLLEFLEKAKKEGLIRHIGFS-FhdSPELLKEILD---------SYDFDFv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 ---HPYLNQ-----SKLLDYCKSKDIVLVAY-----GALGsqrcknwieENAPYLLEDptLCamaeKHKQTPALISLRYL 228
Cdd:cd19096 160 qlqYNYLDQenqagRPGIEYAAKKGMGVIIMeplkgGGLA---------NNPPEALAI--LC----GAPLSPAEWALRFL 224
|
250 260
....*....|....*....|....*..
gi 890826288 229 L-QRGIVIVTKSFNEKR-IKENLKVFE 253
Cdd:cd19096 225 LsHPEVTTVLSGMSTPEqLDENIAAAD 251
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-134 |
5.49e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 86.38 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQN-EEEVGLAIRSkvadgtvRREDIFYTSKlpcTCHR-PELVQPCLEQSLRKLQLDYVDLYLIHC 86
Cdd:cd19100 36 ALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATK---TGARdYEGAKRDLERSLKRLGTDYIDLYQLHA 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 890826288 87 PVSMKpgnDL-IPTDENGkllfdtvdlcdTWEAMEKCKDSGLAKSIGVS 134
Cdd:cd19100 106 VDTEE---DLdQVFGPGG-----------ALEALLEAKEEGKIRFIGIS 140
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-265 |
6.58e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 87.26 E-value: 6.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 10 IDAGFRHIDSAYFYQNEEE-VGLAIRSKVADGTVRREDIFYT------SKLPCTchrPELVQPCLEQSLRKLQLDYVDLY 82
Cdd:cd19101 33 VDAGLTTFDCADIYGPAEElIGEFRKRLRRERDAADDVQIHTkwvpdpGELTMT---RAYVEAAIDRSLKRLGVDRLDLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 83 LIHCpvsmkpgNDlipTDENGKLlfdtvdlcDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPglrYKPVCNQVEcH 162
Cdd:cd19101 110 QFHW-------WD---YSDPGYL--------DAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---VPIVSNQVQ-Y 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 163 PYLNQ---SKLLDYCKSKDIVLVAYGALG----SQRcknWIEENAP------------Y---------------LLEdpT 208
Cdd:cd19101 168 SLLDRrpeNGMAALCEDHGIKLLAYGTLAggllSEK---YLGVPEPtgpaletrslqkYklmidewggwdlfqeLLR--T 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 209 LCAMAEKHKQTPALISLRYLLQR---GIVIVTKSfNEKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19101 243 LKAIADKHGVSIANVAVRWVLDQpgvAGVIVGAR-NSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
9-267 |
5.70e-19 |
|
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: 84.67 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIR-----------SKVA-----DGTVRREDifytsklpctchRPELVQPCLEQ 69
Cdd:cd19148 34 ALDLGINLIDTAPVYgfgLSEEIVGKALKeygkrdrvviaTKVGlewdeGGEVVRNS------------SPARIRKEVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 70 SLRKLQLDYVDLYLIHCPvsmkpgNDLIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLEmilnkpg 149
Cdd:cd19148 102 SLRRLQTDYIDLYQVHWP------DPLVPIEE-------------TAEALKELLDEGKIRAIGVSNFSPEQME------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 150 lRYKPVCNQVECHPYLN------QSKLLDYCKSKDIVLVAYGAL------GSQRCKNWIEEN--------------APYL 203
Cdd:cd19148 156 -TFRKVAPLHTVQPPYNlfereiEKDVLPYARKHNIVTLAYGALcrgllsGKMTKDTKFEGDdlrrtdpkfqeprfSQYL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 890826288 204 LEDPTLCAMAEKHKQTPAL-ISLRYLLQRGIVIVtkSFNEKRIKENLK----VFEFHLPAEDMAVIDRL 267
Cdd:cd19148 235 AAVEELDKLAQERYGKSVIhLAVRWLLDQPGVSI--ALWGARKPEQLDavdeVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
9-264 |
3.82e-18 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 82.65 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQ---NEEEVGLAIRSkvadgtvRREDIFYTSKLPCTCH----------RPELVQPCLEQSLRKLQ 75
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKD-------RRDEVVIATKFGIVRDpgsgfrgvdgRPEYVRAACEASLKRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 76 LDYVDLYLIHCPvsmkpgnDliptdengkllfDTVDLCDTWEAMEKCKDSGLAKSIGVSNFN----RR----------QL 141
Cdd:cd19076 114 TDVIDLYYQHRV-------D------------PNVPIEETVGAMAELVEEGKVRYIGLSEASadtiRRahavhpitavQS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 142 EmilnkpglrYKPVCNQVECHpylnqskLLDYCKSKDIVLVAY---------GALGSQ--------RCKN--WIEENAPY 202
Cdd:cd19076 175 E---------YSLWTRDIEDE-------VLPTCRELGIGFVAYsplgrgfltGAIKSPedlpeddfRRNNprFQGENFDK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 890826288 203 ---LLEdpTLCAMAEKHKQTPALISLRYLLQRGIVIV----TKSfnEKRIKENLKVFEFHLPAEDMAVI 264
Cdd:cd19076 239 nlkLVE--KLEAIAAEKGCTPAQLALAWVLAQGDDIVpipgTKR--IKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
9-251 |
6.57e-18 |
|
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: 81.13 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQNEEEV-GLAIRskvadgTVRREDIFYTSKLPCTC--------HRPELVQPCLEQSLRKLQLDYV 79
Cdd:cd19095 29 ALDLGINLIDTAPAYGRSEERlGRALA------GLRRDDLFIATKVGTHGeggrdrkdFSPAAIRASIERSLRRLGTDYI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 80 DLYLIHCPVsmkpgndliPTDENGKLLfdtvdlcdtwEAMEKCKDSGLAKSIGVSNFNrrqlemilnkPGLRYkpVCN-- 157
Cdd:cd19095 103 DLLQLHGPS---------DDELTGEVL----------ETLEDLKAAGKVRYIGVSGDG----------EELEA--AIAsg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 158 -----QVechPY--LNQS--KLLDYCKSKDIVLVAYGALGSQRCKNWIEENAPYLLEDPTLCAMAEKHKQTPALISLRYL 228
Cdd:cd19095 152 vfdvvQL---PYnvLDREeeELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIGGATWAQAALRFV 228
|
250 260
....*....|....*....|....*.
gi 890826288 229 LQR---GIVIVTKSfNEKRIKENLKV 251
Cdd:cd19095 229 LSHpgvSSAIVGTT-NPEHLEENLAA 253
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
9-267 |
1.57e-17 |
|
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: 80.95 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQ-NEEEVGLAIrsKVADGtvRREDIFYTSKL----------PCTCHRPELVQPCLEQSLRKLQLD 77
Cdd:cd19144 43 AFELGCTFWDTADIYGdSEELIGRWF--KQNPG--KREKIFLATKFgieknvetgeYSVDGSPEYVKKACETSLKRLGVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 78 YVDLYLIHcPVSMKpgndlIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLemilnKPGLRYKPVCN 157
Cdd:cd19144 119 YIDLYYQH-RVDGK-----TPIEK-------------TVAAMAELVQEGKIKHIGLSECSAETL-----RRAHAVHPIAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 158 -QVECHPYL-----NQSKLLDYCKSKDIVLVAYGALGS-------------------QRCKNWIEENAPYLLE--DpTLC 210
Cdd:cd19144 175 vQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRgfltgairspddfeegdfrRMAPRFQAENFPKNLElvD-KIK 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 890826288 211 AMAEKHKQTPALISLRYLLQRG--IVIVTKSFNEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19144 254 AIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREI 312
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
9-189 |
8.12e-17 |
|
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: 77.52 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQN---EEEVGLAIRSkvadgtvRREDIFYTSKLPCTCH---------RPELVQPCLEQSLRKLQL 76
Cdd:cd19086 33 ALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVVIATKFGNRFDggperpqdfSPEYIREAVEASLKRLGT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 77 DYVDLYLIHCpvsmkPGNDLIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNkpglRYKPVC 156
Cdd:cd19086 106 DYIDLYQLHN-----PPDEVLDNDE-------------LFEALEKLKQEGKIRAYGVSVGDPEEALAALR----RGGIDV 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 890826288 157 NQVECHPyLNQS---KLLDYCKSKDIVLVAYGALGS 189
Cdd:cd19086 164 VQVIYNL-LDQRpeeELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-251 |
1.24e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 77.24 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQN---EEEVGLAIRskvadgTVRREDIFYTSKLPCTCH---RPELVQPcLEQSLRKLQLDYVDLY 82
Cdd:cd19105 34 ALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATKASPRLDkkdKAELLKS-VEESLKRLQTDYIDIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 83 LIHCPvsMKPGNDLIptdeNGKLLfdtvdlcdtwEAMEKCKDSGLAKSIGVS-NFNrrQLEMILnkpglrykpvcNQVEC 161
Cdd:cd19105 107 QLHGV--DTPEERLL----NEELL----------EALEKLKKEGKVRFIGFStHDN--MAEVLQ-----------AAIES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPY---------LNQS----KLLDYCKSKDIVLVAYGALGSqrcknwieenapyLLEDPTLCAMAEKHKQTPALISLRYL 228
Cdd:cd19105 158 GWFdvimvaynfLNQPaeleEALAAAAEKGIGVVAMKTLAG-------------GYLQPALLSVLKAKGFSLPQAALKWV 224
|
250 260
....*....|....*....|....*..
gi 890826288 229 LQR----GIVIVTKSFneKRIKENLKV 251
Cdd:cd19105 225 LSNprvdTVVPGMRNF--AELEENLAA 249
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
3-259 |
2.20e-16 |
|
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: 77.21 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 3 AKAT-KIAIDAGFRHIDSAYFYQNEEE-VGLAIRskvadgTVRREDIFYTSKLpCTCHR------PELVQPCLEQSLRKL 74
Cdd:cd19090 22 AVATiRAALDLGINYIDTAPAYGDSEErLGLALA------ELPREPLVLSTKV-GRLPEdtadysADRVRRSVEESLERL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 75 QLDYVDLYLIHCPVSMKPGNDLIPtdeNGKLlfdtvdlcdtwEAMEKCKDSGLAKSIGVS----NFNRR-----QLEMIL 145
Cdd:cd19090 95 GRDRIDLLMIHDPERVPWVDILAP---GGAL-----------EALLELKEEGLIKHIGLGggppDLLRRaietgDFDVVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 146 nkPGLRYKPvCNQVechpylNQSKLLDYCKSKDIVLVAYGALG----SQRCKNWIeENAPYLLEDPT------LCAMAEK 215
Cdd:cd19090 161 --TANRYTL-LDQS------AADELLPAAARHGVGVINASPLGmgllAGRPPERV-RYTYRWLSPELldrakrLYELCDE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 890826288 216 HKQTPALISLRYLLQ--RGIVIVTKSFNEKRIKENLKVFEFHLPAE 259
Cdd:cd19090 231 HGVPLPALALRFLLRdpRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-267 |
4.35e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 76.60 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYqneeevGLAiRSKVADGTV----RREDIFYTSKLPCTC--HRPELVQPCLEQSLRKLQLDYVDLY 82
Cdd:cd19103 41 AMAAGLNLWDTAAVY------GMG-ASEKILGEFlkryPREDYIISTKFTPQIagQSADPVADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 83 LIHCPVSMkPGN--DLIPTDENGKLlfdtvdlcdtweamekckdsglaKSIGVSNFNRRQLEM---ILNKPGLRYKPVCN 157
Cdd:cd19103 114 WIHNPADV-ERWtpELIPLLKSGKV-----------------------KHVGVSNHNLAEIKRaneILAKAGVSLSAVQN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 158 qvecHPYL-----NQSKLLDYCKSKDIVLVAY-----GAL------------GSQRCKNWieenAPYL--LED--PTLCA 211
Cdd:cd19103 170 ----HYSLlyrssEEAGILDYCKENGITFFAYmvleqGALsgkydtkhplpeGSGRAETY----NPLLpqLEEltAVMAE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 890826288 212 MAEKHKQTPALISLRYLLQRG---IVIVTKSfneKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19103 242 IGAKHGASIAQVAIAWAIAKGttpIIGVTKP---HHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
7-262 |
4.99e-16 |
|
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: 76.47 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 7 KIAIDAGFRHIDSAYFYQN---EEEVGLAIRskvadGTVRREDIFYTSKL-------PCTCH--RPELVQPClEQSLRKL 74
Cdd:cd19079 42 KRALDLGINFFDTANVYSGgasEEILGRALK-----EFAPRDEVVIATKVyfpmgdgPNGRGlsRKHIMAEV-DASLKRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 75 QLDYVDLYLIHcpvsmkpgndliptdengkLLFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILN---KPGLR 151
Cdd:cd19079 116 GTDYIDLYQIH-------------------RWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHlaeKNGWT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 152 yKPVCNQvechPYLN------QSKLLDYCKSKDIVLVAYGALGSQRC---------KNWIEENAPYLLEDPT-------- 208
Cdd:cd19079 177 -KFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLARGRLarpwgdtteRRRSTTDTAKLKYDYFteadkeiv 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 890826288 209 --LCAMAEKHKQTPALISLRYLLQRG-----IVIVTKsfnEKRIKENLKVFEFHLPAEDMA 262
Cdd:cd19079 252 drVEEVAKERGVSMAQVALAWLLSKPgvtapIVGATK---LEHLEDAVAALDIKLSEEEIK 309
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
4-265 |
8.10e-16 |
|
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: 76.16 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSA--YFYQNEEE-VGLAIRSkvadgtvRREDIFYTSKlpC---------------------TCHR 59
Cdd:cd19149 37 RTIHAALDLGINLIDTApaYGFGHSEEiVGKAIKG-------RRDKVVLATK--CglrwdreggsfffvrdgvtvyKNLS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 60 PELVQPCLEQSLRKLQLDYVDLYLIHCPVSMKPgndliptdengkllfdtvdLCDTWEAMEKCKDSGLAKSIGVSNFNRR 139
Cdd:cd19149 108 PESIREEVEQSLKRLGTDYIDLYQTHWQDVETP-------------------IEETMEALEELKRQGKIRAIGASNVSVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 140 QLEMILNkpglrykpvCNQVEchpyLNQSK-----------LLDYCKSKDIVLVAYGAL-----------------GSQR 191
Cdd:cd19149 169 QIKEYVK---------AGQLD----IIQEKysmldrgiekeLLPYCKKNNIAFQAYSPLeqglltgkitpdrefdaGDAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 192 ckNWIEENAPYLLEdpTLCAM-------AEKHKQTPALISLRYLL-QRGIVIV-TKSFNEKRIKENLKVFEFHLPAEDMA 262
Cdd:cd19149 236 --SGIPWFSPENRE--KVLALlekwkplCEKYGCTLAQLVIAWTLaQPGITSAlCGARKPEQAEENAKAGDIRLSAEDIA 311
|
...
gi 890826288 263 VID 265
Cdd:cd19149 312 TMR 314
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
7-267 |
2.61e-15 |
|
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: 74.57 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 7 KIAIDAGFRHIDSAYFY---QNEEEVGLAIRSkvadgtvRREDIFYTSKLPCT---------CHRPELVQPClEQSLRKL 74
Cdd:cd19091 46 DIALDAGINFFDTADVYsegESEEILGKALKG-------RRDDVLIATKVRGRmgegpndvgLSRHHIIRAV-EASLKRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 75 QLDYVDLYLIHCPVSMKPgndliptdengkllfdtvdLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMIL---NKPGLR 151
Cdd:cd19091 118 GTDYIDLYQLHGFDALTP-------------------LEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 152 yKPVCNQVechpYLN------QSKLLDYCKSKDIVLVAYGALGSQRCKNWIEENAP----------------------YL 203
Cdd:cd19091 179 -RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPapegsrlrrtgfdfppvdrergYD 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 890826288 204 LEDpTLCAMAEKHKQTPALISLRYLLQR----GIVIVTKsfNEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19091 254 VVD-ALREIAKETGATPAQVALAWLLSRptvsSVIIGAR--NEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-250 |
1.12e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 72.74 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSA--YFYQ-NEEEVGLAIRSKVADGTVRREDIFYTSK---------------------------- 52
Cdd:cd19099 25 EALKAALDSGINVIDTAinYRGGrSERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgdeplrplkyleeklgrglid 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 53 -----LPCTCHRPELVQPCLEQSLRKLQLDYVDLYLIHCPVSMkpgndLIPTDENGklLFDTVDlcDTWEAMEKCKDSGL 127
Cdd:cd19099 105 vadsaGLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQ-----LLELGEEE--FYDRLE--EAFEALEEAVAEGK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 128 AKSIGVSNFN------------------RRQLEMILNKPGLR-----YKPVCNQVECHPYLNQSK---LLDYCKSKDIVL 181
Cdd:cd19099 176 IRYYGISTWDgfrappalpghlsleklvAAAEEVGGDNHHFKviqlpLNLLEPEALTEKNTVKGEalsLLEAAKELGLGV 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 890826288 182 VAYGALgsqrcknwieeNAPYLLEDPTLCAM-AEKHKQTPALISLRYLLQR---GIVIV-TKsfNEKRIKENLK 250
Cdd:cd19099 256 IASRPL-----------NQGQLLGELRLADLlALPGGATLAQRALQFARSTpgvDSALVgMR--RPEHVDENLA 316
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
9-267 |
1.09e-13 |
|
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: 69.90 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLA------------------IRSKVAdGtvRREDIFYTSKLPcTCHRPELVQPCL 67
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvpPSPETQGRTeeiigswlkkkgnrdkvvLATKVA-G--PGEGITWPRGGG-TRLDRENIREAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 68 EQSLRKLQLDYVDLYLIHCP---VSMKPGNDLIPTDENGkllfDTVDLCDTWEAMEKCKDSGLAKSIGVSN--------F 136
Cdd:cd19094 103 EGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEEE----DSVSFEEQLEALGELVKAGKIRHIGLSNetpwgvmkF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 137 NRrqlemiLNKPGLRYKPVCNQvecHPY--LNQSK---LLDYCKSKDIVLVAYGALG------------SQRCK---NWI 196
Cdd:cd19094 179 LE------LAEQLGLPRIVSIQ---NPYslLNRNFeegLAEACHRENVGLLAYSPLAggvltgkyldgaARPEGgrlNLF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 197 EENAPYLLEDPTLCA------MAEKHKQTPALISLRYLLQRGIV---IVTKSfNEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19094 250 PGYMARYRSPQALEAvaeyvkLARKHGLSPAQLALAWVRSRPFVtstIIGAT-TLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
10-265 |
1.97e-13 |
|
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: 69.17 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 10 IDAGFRHIDSAYFY----------QNEEEVGLAIRSKVadgtvRREDIFYTSKL--PCTCHRPEL----VQPCLEQSLRK 73
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-----KRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 74 LQLDYVDLYLIHCPvsmkpgNDLIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILN---KPGL 150
Cdd:cd19081 111 LQTDYIDLYQAHWD------DPATPLEE-------------TLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 151 -RY---KPVCNQVECHPYlnQSKLLDYCKSKDIVLVAYGALGS------QRCKN------WIEENAPYLLEDPT------ 208
Cdd:cd19081 172 pRYvslQPEYNLVDRESF--EGELLPLCREEGIGVIPYSPLAGgfltgkYRSEAdlpgstRRGEAAKRYLNERGlrilda 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 209 LCAMAEKHKQTPALISLRYLLQR-GI--VIVTKSfNEKRIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19081 250 LDEVAAEHGATPAQVALAWLLARpGVtaPIAGAR-TVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
7-253 |
3.48e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 67.94 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 7 KIAIDAGFRHIDSAYFYQNEEEV-GLAIrskvadgtVRREDIFYTSKLPCTCHRPELVQP----CLEQSLRKLQLDYVDL 81
Cdd:cd19097 33 EYALKAGINTLDTAPAYGDSEKVlGKFL--------KRLDKFKIITKLPPLKEDKKEDEAaieaSVEASLKRLKVDSLDG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 82 YLIHCPvsmkpgNDLiptDENGKLLfdtvdlcdtWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNkpglRYKPVCNQVEC 161
Cdd:cd19097 105 LLLHNP------DDL---LKHGGKL---------VEALLELKKEGLIRKIGVSVYSPEELEKALE----SFKIDIIQLPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 162 HPY---LNQSKLLDYCKSKDIVLVA-----YGAL--GSQRCKNWIEENAPYLLEdptLCAMAEKHKQTPALISLRYLLQR 231
Cdd:cd19097 163 NILdqrFLKSGLLAKLKKKGIEIHArsvflQGLLlmEPDKLPAKFAPAKPLLKK---LHELAKKLGLSPLELALGFVLSL 239
|
250 260
....*....|....*....|....*..
gi 890826288 232 ----GIVI-VTksfNEKRIKENLKVFE 253
Cdd:cd19097 240 peidKIVVgVD---SLEQLKEIIAAFK 263
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
9-259 |
1.14e-12 |
|
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: 66.85 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRskvadgTVRREDIFYTSKL--PCTCH-------RPELVQpCLEQSLRKLQL 76
Cdd:cd19074 31 AYDLGINFFDTADVYaagQAEEVLGKALK------GWPRESYVISTKVfwPTGPGpndrglsRKHIFE-SIHASLKRLQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 77 DYVDLYLIHCPvsmkpgndliptDENgkllfdtVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLE--MILNKPGLRYKP 154
Cdd:cd19074 104 DYVDIYYCHRY------------DPE-------TPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAeaHDLARQFGLIPP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 155 VCNQVECHpYLNQSK---LLDYCKSKDIVLVAYGAL-------------------------GSQRCKNWIEENAPYLLED 206
Cdd:cd19074 165 VVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsrsratdedNRDKKRRLLTDENLEKVKK 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 890826288 207 ptLCAMAEKHKQTPALISLRYLLQRGIVI--VTKSFNEKRIKENLKVFEFHLPAE 259
Cdd:cd19074 244 --LKPIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
9-266 |
2.30e-11 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 63.02 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRSkvadgtvRREDIFYTSKL-----PCTCH------RPELVQPCLEQSLRKL 74
Cdd:cd19078 34 AVELGITFFDTAEVYgpyTNEELVGEALKP-------FRDQVVIATKFgfkidGGKPGplgldsRPEHIRKAVEGSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 75 QLDYVDLYLIHcpvSMKPGndlIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNFNRRQLEmilnkpglRYKP 154
Cdd:cd19078 107 QTDYIDLYYQH---RVDPN---VPIEE-------------VAGTMKELIKEGKIRHWGLSEAGVETIR--------RAHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 155 VC---------NQVECHPylnQSKLLDYCKSKDIVLVAYGALGS-----------------------QRCKNWIEENAPY 202
Cdd:cd19078 160 VCpvtavqseySMMWREP---EKEVLPTLEELGIGFVPFSPLGKgfltgkidentkfdegddraslpRFTPEALEANQAL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 890826288 203 --LLEDptlcaMAEKHKQTPALISLRYLLQRG--IVIVTKSFNEKRIKENLKVFEFHLPAEDMAVIDR 266
Cdd:cd19078 237 vdLLKE-----FAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
9-267 |
2.35e-11 |
|
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: 62.98 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQN---EEEVGLAIRSkvadgtvRREDIFYTSKlpctCHRP-------------ELVQPClEQSLR 72
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATK----VFGPmgddpndrglsrrHIRRAV-EASLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 73 KLQLDYVDLYLIHCPvsmkpgNDLIPTDEngkllfdtvdlcdTWEAMEKCKDSGLAKSIGVSNF-------------NRR 139
Cdd:cd19087 107 RLQTDYIDLYQMHHF------DRDTPLEE-------------TLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaaRRG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 140 QLEMILNKPglRYKPVCNQVECHpylnqskLLDYCKSKDIVLVAY---------GALGSQ--------------RCKNWI 196
Cdd:cd19087 168 LLRFVSEQP--MYNLLKRQAELE-------ILPAARAYGLGVIPYsplagglltGKYGKGkrpesgrlveraryQARYGL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 890826288 197 EENAPYLLEdptLCAMAEKHKQTPALISLRYLLQRGIV---IVTKSfNEKRIKENLKVFEFHLPAEDMAVIDRL 267
Cdd:cd19087 239 EEYRDIAER---FEALAAEAGLTPASLALAWVLSHPAVtspIIGPR-TLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
10-265 |
5.06e-11 |
|
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: 62.24 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 10 IDAGFRHIDSAYFYQN---EEEVGLAIRSkvadgtvRREDIFYTSKL--------PCTC--HRPELVQPcLEQSLRKLQL 76
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKYtmnrrpgdPNAGgnHRKNLRRS-VEASLRRLQT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 77 DYVDLYLIH-----CPVS--MKPGNDLIptdENGKLLFdtVDLCDT--WEAmekCKDSGLAKSIGVSNFNRRQLEmilnk 147
Cdd:cd19080 113 DYIDLLYVHawdftTPVEevMRALDDLV---RAGKVLY--VGISDTpaWVV---ARANTLAELRGWSPFVALQIE----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 148 pglrYKPVCNQVEchpylnqSKLLDYCKSKDIVLVAYGALGS-------QRCKNWIEENAPYLLEDP------------T 208
Cdd:cd19080 180 ----YSLLERTPE-------RELLPMARALGLGVTPWSPLGGglltgkyQRGEEGRAGEAKGVTVGFgklternwaivdV 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 209 LCAMAEKHKQTPALISLRYLLQR---GIVIVTKSFNEKrIKENLKVFEFHLPAEDMAVID 265
Cdd:cd19080 249 VAAVAEELGRSAAQVALAWVRQKpgvVIPIIGARTLEQ-LKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-267 |
6.96e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 61.90 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 4 KATKIAIDAGFRHIDSAYFY---QNEEEVGLAIRSKvadgtvrREDIFYTSKLPCTCHRPELVQPC----LEQSLRKLQL 76
Cdd:cd19104 36 AAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVRLDPDDLGDIGGQiersVEKSLKRLKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 77 DYVDLYLIHcpvsmkpgNDLIPTDENGKLLFDTVD----LCDTWEAMEKCKDSGLAKSIGVSNF-NRRQLEMIL--NKPG 149
Cdd:cd19104 109 DSVDLLQLH--------NRIGDERDKPVGGTLSTTdvlgLGGVADAFERLRSEGKIRFIGITGLgNPPAIRELLdsGKFD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 150 --------LRYKPVCNQVECHPYLNQSKLLDYCKSKD-----IVLVAYGALGSQrcknwieENAPyLLEDPT-------- 208
Cdd:cd19104 181 avqvyynlLNPSAAEARPRGWSAQDYGGIIDAAAEHGvgvmgIRVLAAGALTTS-------LDRG-REAPPTsdsdvaid 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 890826288 209 ------LCAMAEKHKQTPALISLRYLL-QRGIVIVTKSF-NEKRIKENLKVFEF-HLPAEDMAVIDRL 267
Cdd:cd19104 253 frraaaFRALAREWGETLAQLAHRFALsNPGVSTVLVGVkNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
1-189 |
5.24e-10 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 59.11 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 1 MVAKATKIAIDAGFRHIDSAYFYQN---EEEVGLA--------IRSKVADGTVrredifytsklpcTCHRPELVQPCLEQ 69
Cdd:cd19075 21 AAAELLDAFLERGHTEIDTARVYPDgtsEELLGELglgergfkIDTKANPGVG-------------GGLSPENVRKQLET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 70 SLRKLQLDYVDLYLIHCPvsmkpgndliptDEngkllfdTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILN--- 146
Cdd:cd19075 88 SLKRLKVDKVDVFYLHAP------------DR-------STPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEick 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 890826288 147 -----KP----GLrYKPVCNQVEchpylnqSKLLDYCKSKDIVLVAYGALGS 189
Cdd:cd19075 149 engwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLAG 192
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-188 |
8.01e-10 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 58.33 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRskvadgTVRREDIFYTSKlpctCHRPEL------------VQPCLEQSLRK 73
Cdd:cd19163 42 ALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYLATK----VGRYGLdpdkmfdfsaerITKSVEESLKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 74 LQLDYVDLYLIHcPVSMKPGNDLIptdengkllfdtvdLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPG---- 149
Cdd:cd19163 112 LGLDYIDIIQVH-DIEFAPSLDQI--------------LNETLPALQKLKEEGKVRFIGITGYPLDVLKEVLERSPvkid 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 890826288 150 --LRYkpvcnqveCHPYLNQS---KLLDYCKSKDIVLVAYGALG 188
Cdd:cd19163 177 tvLSY--------CHYTLNDTsllELLPFFKEKGVGVINASPLS 212
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
60-250 |
5.28e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 56.19 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 60 PELVQPCLEQSLRKLQLDYVDLYLIHcpvsmkpgndlipTDengkllFDTVDLCDTWEAMEKCKDSGLAKSIGVSNFNRR 139
Cdd:cd19752 94 AETIEQEIDKSLRRLGTDYIDLYYAH-------------VD------DRDTPLEETLEAFNELVKAGKVRAIGASNFAAW 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 140 QLEMI--LNKPGLRYKPVCNQVEcHPYL---------NQS----KLLDYCKS-KDIVLVAYGA-LGSQRCKNWIEENAPY 202
Cdd:cd19752 155 RLERArqIARQQGWAEFSAIQQR-HSYLrprpgadfgVQRivtdELLDYASSrPDLTLLAYSPlLSGAYTRPDRPLPEQY 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 890826288 203 LLEDP-----TLCAMAEKHKQTPALISLRYLLQRG---IVIVTKSFNEKrIKENLK 250
Cdd:cd19752 234 DGPDSdarlaVLEEVAGELGATPNQVVLAWLLHRTpaiIPLLGASTVEQ-LEENLA 288
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
9-251 |
1.34e-08 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 54.96 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY-----QNEEEVGLAIRSkvaDGTVRREDIFYTSKLPCTCH---------RPELVQPcLEQSLRKL 74
Cdd:cd19089 38 AFDLGITHFDLANNYgpppgSAEENFGRILKR---DLRPYRDELVISTKAGYGMWpgpygdggsRKYLLAS-LDQSLKRM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 75 QLDYVDLYLIHCPvsmkpgNDLIPTDENGKLLFDTVdlcdtweamekckDSGLAKSIGVSNFNRRQLEM---ILNKPGLR 151
Cdd:cd19089 114 GLDYVDIFYHHRY------DPDTPLEETMTALADAV-------------RSGKALYVGISNYPGAKARRaiaLLRELGVP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 152 ykPVCNQVechPY--LNQS---KLLDYCKSKDIVLVAYGAL---------------GSQRCKNWIEENAPYLLED----- 206
Cdd:cd19089 175 --LIIHQP---RYslLDRWaedGLLEVLEEAGIGFIAFSPLaqglltdkylngippDSRRAAESKFLTEEALTPEkleql 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 890826288 207 PTLCAMAEKHKQTPALISLRYLLQR-GI--VIVTKSfNEKRIKENLKV 251
Cdd:cd19089 250 RKLNKIAAKRGQSLAQLALSWVLRDpRVtsVLIGAS-SPSQLEDNVAA 296
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
9-189 |
2.03e-08 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 54.29 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRSKvadgtvRREDIFYTSKL----------PCTCHRPEL------VQPCLEQ 69
Cdd:cd19162 28 AWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrllepgaagRPAGADRRFdfsadgIRRSIEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 70 SLRKLQLDYVDLYLIHcpvsmkpgnDLIPTDENGkllfdtvdLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPG 149
Cdd:cd19162 102 SLERLGLDRLDLVFLH---------DPDRHLLQA--------LTDAFPALEELRAEGVVGAIGVGVTDWAALLRAARRAD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 890826288 150 LRYKPVCNQvecHPYLNQS---KLLDYCKSKDIVLVAYGALGS 189
Cdd:cd19162 165 VDVVMVAGR---YTLLDRRaatELLPLCAAKGVAVVAAGVFNS 204
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
9-135 |
8.05e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 52.55 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQ----------NEEEVG-----------LAIRSKVAdGTVRREDifyTSKLPCTCHRPELVQPCL 67
Cdd:PRK10625 39 AVAQGINLIDVAEMYPvpprpetqglTETYIGnwlakrgsrekLIIASKVS-GPSRNND---KGIRPNQALDRKNIREAL 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 890826288 68 EQSLRKLQLDYVDLYLIHCPVSmkpgndliPTDENGKLLFD------TVDLCDTWEAMEKCKDSGLAKSIGVSN 135
Cdd:PRK10625 115 HDSLKRLQTDYLDLYQVHWPQR--------PTNCFGKLGYSwtdsapAVSLLETLDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
10-135 |
2.04e-07 |
|
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: 51.40 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 10 IDAGFRHIDSAYFYQNEEEVGLA-------IRSkvadgTVRREDIFYTSKLpctCHR-----------PELVQPCLEQSL 71
Cdd:cd19082 27 VELGGNFIDTARVYGDWVERGAServigewLKS-----RGNRDKVVIATKG---GHPdledmsrsrlsPEDIRADLEESL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 890826288 72 RKLQLDYVDLYLIHcpvsmkpgNDliptDEN---GKLLfdtvdlcdtwEAMEKCKDSGLAKSIGVSN 135
Cdd:cd19082 99 ERLGTDYIDLYFLH--------RD----DPSvpvGEIV----------DTLNELVRAGKIRAFGASN 143
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
9-264 |
6.75e-07 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 49.74 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFY---QNEEEVGLAIRSKVadgtvrREDIFYTSKLPCTCHR---------PELVQPCLEQSLRKLQL 76
Cdd:cd19145 42 AFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKFGIHEIGgsgvevrgdPAYVRAACEASLKRLDV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 77 DYVDLYLIHcpvsmkpgndLIPTdengkllfdTVDLCDTWEAMEKCKDSGLAKSIGVSNFN----RR----------QLE 142
Cdd:cd19145 116 DYIDLYYQH----------RIDT---------TVPIEITMGELKKLVEEGKIKYIGLSEASadtiRRahavhpitavQLE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 143 MILnkpglrykpVCNQVEchpylnqSKLLDYCKSKDIVLVAYGALG-----SQRCKNWIEENAPYLLEDP---------- 207
Cdd:cd19145 177 WSL---------WTRDIE-------EEIIPTCRELGIGIVPYSPLGrgffaGKAKLEELLENSDVRKSHPrfqgenlekn 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 890826288 208 -----TLCAMAEKHKQTPALISLRYLLQRG--IVIVTKSFNEKRIKENLKVFEFHLPAEDMAVI 264
Cdd:cd19145 241 kvlyeRVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
9-250 |
7.52e-07 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 49.78 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 9 AIDAGFRHIDSAYFYQN---EEEVGLAIRSKvadgTVRREDIFYTSKlpctCHR--------PELVQPCLEQSLRKLQLD 77
Cdd:PLN02587 40 AFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTK----CGRygegfdfsAERVTKSVDESLARLQLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 78 YVDlyLIHCpvsmkpgNDLiptdENGKLlfDTVdLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNK--PG-----L 150
Cdd:PLN02587 112 YVD--ILHC-------HDI----EFGSL--DQI-VNETIPALQKLKESGKVRFIGITGLPLAIFTYVLDRvpPGtvdviL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 151 RYkpvcnqveCHPYLNQSKLLD---YCKSKDIVLV-----AYGALGSQRCKNWieenAPYLLEDPTLCAMAEKH----KQ 218
Cdd:PLN02587 176 SY--------CHYSLNDSSLEDllpYLKSKGVGVIsasplAMGLLTENGPPEW----HPAPPELKSACAAAATHckekGK 243
|
250 260 270
....*....|....*....|....*....|....
gi 890826288 219 TPALISLRY-LLQRGIVIVTKSFNE-KRIKENLK 250
Cdd:PLN02587 244 NISKLALQYsLSNKDISTTLVGMNSvQQVEENVA 277
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
7-160 |
1.79e-06 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 48.36 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 7 KIAIDAGFRHIDSAYFYQN---EEEVGLAIRskvaDGTVRREDIFYTSKL-------PCT---CHRPELVQPClEQSLRK 73
Cdd:cd19143 38 KAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKIfwggggpPPNdrgLSRKHIVEGT-KASLKR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 74 LQLDYVDLYLIHCPvsmkpgnDLI-PTDEngkllfdTVdlcdtwEAMEKCKDSGLAKSIGVSNFNRRQLE---MILNKPG 149
Cdd:cd19143 113 LQLDYVDLVFCHRP-------DPAtPIEE-------TV------RAMNDLIDQGKAFYWGTSEWSAQQIEeahEIADRLG 172
|
170
....*....|.
gi 890826288 150 LRyKPVCNQVE 160
Cdd:cd19143 173 LI-PPVMEQPQ 182
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
7-195 |
1.50e-05 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 45.60 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 7 KIAIDAGFRHIDSAYFYQN---EEEVGLAIR------------SKVADGtvrREDIFYTSKlpctchrpELVQPCLEQSL 71
Cdd:cd19153 40 AEAFAAGINHFDTSPYYGAessEAVLGKALAalqvprssytvaTKVGRY---RDSEFDYSA--------ERVRASVATSL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 72 RKLQLDYVDLYLIHcpvsmkpgnDLiptdENGKLlfDTvDLCDTWEAMEKCKDSGLAKSIGVSNFNRRQLEMILNKPGLR 151
Cdd:cd19153 109 ERLHTTYLDVVYLH---------DI----EFVDY--DT-LVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 890826288 152 YKPVCnQVECHPYLNQSKLLD---YCKSKDIVLV------AYGALGSQRCKNW 195
Cdd:cd19153 173 SLDAV-LSYCHLTLQDARLESdapGLVRGAGPHVinasplSMGLLTSQGPPPW 224
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
2-133 |
2.17e-05 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 45.29 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKAT-KIAIDAGFRHIDSAYFYQN---EEEVGLAIRSKVAD--------GTVRREDI--------FYTSKLPctcHRPE 61
Cdd:cd19152 21 EAKATlVAAWDLGIRYFDTAPWYGAglsEERLGAALRELGREdyvistkvGRLLVPLQeveptfepGFWNPLP---FDAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 62 L------VQPCLEQSLRKLQLDYVDLYLIHcpvsmkpgnDLIPT--DENGKLLFDTvDLCDTWEAMEKCKDSGLAKSIGV 133
Cdd:cd19152 98 FdysydgILRSIEDSLQRLGLSRIDLLSIH---------DPDEDlaGAESDEHFAQ-AIKGAFRALEELREEGVIKAIGL 167
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
1-85 |
8.03e-05 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 43.42 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 1 MVAKATKIAIDAGFRHIDSAYFYQNEEEV-GLAIrSKVADGtVRREDIFYTSKlpctCHR---------PELVQPCLEQS 70
Cdd:cd19164 35 PPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL-KALRDE-FPRDTYFIITK----VGRygpddfdysPEWIRASVERS 108
|
90
....*....|....*
gi 890826288 71 LRKLQLDYVDLYLIH 85
Cdd:cd19164 109 LRRLHTDYLDLVYLH 123
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
66-164 |
6.28e-04 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 40.91 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 66 CLEQSLRKLQLDYVDLYLIH-----CPVS--MKPGNDLIptdENGKLLFDTvdlCDTWEAMEkckdsglaksIGVSNFNR 138
Cdd:cd19142 102 SVRASLRRLQLDYIDIVIIHkadpmCPMEevVRAMSYLI---DNGLIMYWG---TSRWSPVE----------IMEAFSIA 165
|
90 100
....*....|....*....|....*.
gi 890826288 139 RQLEMILnkpglrykPVCNQVECHPY 164
Cdd:cd19142 166 RQFNCPT--------PICEQSEYHMF 183
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
2-136 |
1.45e-03 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 39.71 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 2 VAKATKIAI-----DAGFRHIDSAYFYQNEEE---VG-----------LAIRSKVADGTVRREDIFYTSKLPCTcHRPEL 62
Cdd:cd19146 32 CDKETAFKLldafyEQGGNFIDTANNYQGEESerwVGewmasrgnrdeMVLATKYTTGYRRGGPIKIKSNYQGN-HAKSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890826288 63 VQPcLEQSLRKLQLDYVDLYLIH-----CPVS--MKPGNDLIptdENGKLLFDTVDLCDTWeAMEKCKDsgLAKSIGVSN 135
Cdd:cd19146 111 RLS-VEASLKKLQTSYIDILYVHwwdytTSIPelMQSLNHLV---AAGKVLYLGVSDTPAW-VVSKANA--YARAHGLTQ 183
|
.
gi 890826288 136 F 136
Cdd:cd19146 184 F 184
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