|
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) ... |
6-308 |
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: 709.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 6 QTVRLSDGHFIPILGFGTYAPQEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKV 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 86 WCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 166 SNFNRRQLEKILKKPGLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREKQWVDQSSPVLLDNPVLGSMA 245
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487925 246 KKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRYISG 308
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-319 |
0e+00 |
|
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: 505.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFGTYA-PQEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFHR 91
Cdd:cd19109 1 GNSIPIIGLGTYSePKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 92 PELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 172 QLEKILKKPGLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREKQWVDQSSPVLLDNPVLGSMAKKYNRT 251
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 252 PALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRYISGSSFKDHPDFPF 319
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-323 |
1.48e-139 |
|
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: 397.17 E-value: 1.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFHRPELV 95
Cdd:cd19107 4 MPILGLGTW---KSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 96 RVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 176 ILKKPGLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGShREKQWVDQSSPVLLDNPVLGSMAKKYNRTPALI 255
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGS-PDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 256 ALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRYISGSSFKDHPDFPFWDEY 323
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-306 |
4.65e-135 |
|
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: 385.58 E-value: 4.65e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 10 LSDGHFIPILGFGTY--APQEVpkskaTEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKI-ADGTVKREDIFYTSKVW 86
Cdd:cd19106 1 LHTGQKMPLIGLGTWksKPGQV-----KAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19106 76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 NFNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGShREKQWVDQSSPVLLDNPVLGSMAK 246
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGS-PDRPWAKPDEPVLLEEPKVKALAK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 247 KYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRYI 306
Cdd:cd19106 233 KYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-306 |
1.10e-130 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 373.93 E-value: 1.10e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 7 TVRLSDGHFIPILGFGTYapQEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVW 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTW--KLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENylpKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENND---SESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 NFNRRQLEKILKkpGLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSH-REKQWvdqSSPVLLDNPVLGSMA 245
Cdd:cd19116 157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLvPRGQT---NPPPRLDDPTLVAIA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487925 246 KKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRYI 306
Cdd:cd19116 232 KKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-297 |
6.68e-128 |
|
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: 365.27 E-value: 6.68e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIadgtVKREDIFYTSKVWCTFHRPELV 95
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 96 RVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENylpkdengkliydAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGGS-------------KEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 176 ILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREKqwvdqsspvLLDNPVLGSMAKKYNRTPALI 255
Cdd:cd19071 141 LLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP---------LLDDPVLKEIAKKYGKTPAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 13487925 256 ALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLD 297
Cdd:cd19071 210 LLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-323 |
2.45e-126 |
|
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: 363.51 E-value: 2.45e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTY--APQEVpkskaTEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFHRPE 93
Cdd:cd19110 4 IPAVGLGTWkaSPGEV-----TEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 94 LVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQL 173
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 174 EKILKKPGLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREKqwVDqsspvLLDNPVLGSMAKKYNRTPA 253
Cdd:cd19110 159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEG--VD-----LIDDPVIQRIAKKHGKSPA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 254 LIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRYISGSSFKDHPDFPFWDEY 323
Cdd:cd19110 232 QILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
7-306 |
1.28e-118 |
|
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: 343.62 E-value: 1.28e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 7 TVRLSDGHFIPILGFGTY--APQEVpkskaTEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSK 84
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWksKPGEV-----GQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 85 VWCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYlPKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19123 78 LWNNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGVGF-PESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 165 VSNFNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGS-HREKQWVDQSSPVLLDNPVLGS 243
Cdd:cd19123 157 VSNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487925 244 MAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRYI 306
Cdd:cd19123 235 IAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-305 |
2.68e-117 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 338.57 E-value: 2.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 12 DGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRskiADGtVKREDIFYTSKVWCTFHR 91
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA---ASG-VPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 92 PELVRVCLEQSLKQLQLDYVDLYLIHFPMAmkpgenylpkdengkliydaVDICDTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 172 QLEKILKKPGlkYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPVLGSMAKKYNRT 251
Cdd:COG0656 134 HLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKT 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 13487925 252 PALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:COG0656 201 PAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-304 |
2.40e-115 |
|
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: 335.54 E-value: 2.40e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 8 VRLSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWC 87
Cdd:cd19154 4 ITLSNGVKMPLIGLGTW---QSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 88 TFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 168 FNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGS-----HREKQWVdQSSPVLLDNPVLG 242
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranFTKSTGV-SPAPNLLQDPIVK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487925 243 SMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIR 304
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
10-297 |
1.09e-109 |
|
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: 320.45 E-value: 1.09e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 10 LSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTF 89
Cdd:cd19125 5 LNTGAKIPAVGLGTW---QADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 90 HRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGEnylPKDENGKLIydAVDICDTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19125 82 HAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 170 RRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGShREKQWVdqsSPVLLDNPVLGSMAKKYN 249
Cdd:cd19125 157 VKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGS-PGTTWV---KKNVLKDPIVTKVAEKLG 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 13487925 250 RTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLD 297
Cdd:cd19125 231 KTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFS 278
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-305 |
1.82e-100 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 297.10 E-value: 1.82e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFHRP 92
Cdd:cd19111 1 GFPMPVIGLGTY---QSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 93 ELVRVCLEQSLKQLQLDYVDLYLIHFPMamkpGENYlpKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19111 78 KDTEKSLEKSLENLKLPYVDLYLIHHPC----GFVN--KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 173 LEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGS-HREKQWVDQSSPVLLDNPVLGSMAKKYNRT 251
Cdd:cd19111 152 INKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELDKT 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 13487925 252 PALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:cd19111 230 PAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-299 |
4.38e-98 |
|
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: 290.71 E-value: 4.38e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 12 DGHFIPILGFGTYAPQEVPKsKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVK-REDIFYTSKVWCTFH 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE-DIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 91 RPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLiydAVDICDTWEAMEKCKDAGLAKSIGVSNFNR 170
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFL---PFDIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 171 RQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREKqWvdqSSPVLLDNPVLGSMAKKYNR 250
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK-W---GSNAVMESDVLKEIAAAKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 13487925 251 TPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-304 |
8.63e-98 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 290.97 E-value: 8.63e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 5 QQTVRLSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSK 84
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTW---QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 85 VWCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMK-PGENYLPKDENGKLIYD-AVDICDTWEAMEKCKDAGLAKS 162
Cdd:cd19155 78 LPPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 163 IGVSNFNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGS------HREKQWVDQSSPVLL 236
Cdd:cd19155 158 IGLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfSPGTGSPSGSSPDLL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 237 DNPVLGSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIR 304
Cdd:cd19155 236 QDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-299 |
4.36e-97 |
|
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: 288.16 E-value: 4.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 10 LSDGHFIPILGFGTY--APQEVpkskaTEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIAD-GTVKREDIFYTSKVW 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaEPGEV-----GAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPG---ENYLPKDENGKLIY--DAVDICDTWEAMEKCKDAGLAK 161
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTgdlNPLTAVPTNGGEVDldLSVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 162 SIGVSNFNRRQLEKILKKPGLkyKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdQSSPVLLDNPVL 241
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 242 GSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEfqLTSEDMKVLDDL 299
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-301 |
1.03e-95 |
|
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: 284.78 E-value: 1.03e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 5 QQTVRLSDGHFIPILGFGTY--APQEVPKskateATKIAIDAGFRHIDSASMYQNEKEVGLAIRskiaDGTVKREDIFYT 82
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTWqsKPNEVAK-----AVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 83 SKVWCTFHRPelVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPG--ENYLPKDENGKLIYDAVDICDTWEAMEKCKDAGLA 160
Cdd:cd19117 74 TKLWCTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 161 KSIGVSNFNRRQLEKILKKPGLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGShrekqwvdQSSPvLLDNPV 240
Cdd:cd19117 152 KAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS--------TNAP-LLKEPV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487925 241 LGSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEfqLTSEDMKVLDDLNK 301
Cdd:cd19117 223 IIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHK 281
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
16-283 |
2.77e-93 |
|
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: 278.96 E-value: 2.77e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYAPQevpKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFHRPELV 95
Cdd:cd19129 6 IPALGFGTLIPD---PSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 96 RVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLIYD-AVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLE 174
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDdGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 175 KILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREkqwvdqssPVLLDNPVLGSMAKKYNRTPAL 254
Cdd:cd19129 163 EIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME--------PKLLEDPVITAIARRVNKTPAQ 232
|
250 260
....*....|....*....|....*....
gi 13487925 255 IALRYQLQRGVVVLAKSFSEKRIKENMQV 283
Cdd:cd19129 233 VLLAWAIQRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-299 |
5.52e-92 |
|
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: 274.51 E-value: 5.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTY---APQEVpkSKATEAtkiAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFHRP 92
Cdd:cd19136 1 MPILGLGTFrlrGEEEV--RQAVDA---ALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 93 ELVRVCLEQSLKQLQLDYVDLYLIHFpmamkPGENYLPKDENGKLIYDAvdicDTWEAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19136 76 EKARAACLGSLERLGTDYLDLYLIHW-----PGVQGLKPSDPRNAELRR----ESWRALEDLYKEGKLRAIGVSNYTVRH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 173 LEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGShrekqwvdqSSPVLLDNPVLGSMAKKYNRTP 252
Cdd:cd19136 147 LEELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS---------GDLRLLEDPTVLAIAKKYGRTP 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 13487925 253 ALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19136 216 AQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-297 |
2.81e-91 |
|
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: 271.84 E-value: 2.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTFHRPELV 95
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 96 RVCLEQSLKQLQLDYVDLYLIHFPMAmkpgenylpkdengkliydAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNP-------------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 176 ILKKPGLKykPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGsHREkqwvdqsspvLLDNPVLGSMAKKYNRTPALI 255
Cdd:cd19073 135 ALDISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA-RGE----------VLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 13487925 256 ALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLD 297
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-305 |
5.09e-91 |
|
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: 272.18 E-value: 5.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFGT-----YAPQEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRskiaDGTVKREDIFYTSKVWC 87
Cdd:cd19120 1 GSKIPAIAFGTgtawyKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 88 tfhRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGenylpkdengkliydAVDICDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19120 77 ---GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 168 FNRRQLEKILKKPglKYKPVCNQVECHPYLN--QGKLLDFCRSKDIVLVAYSALGShrekQWVDQSSPVlldNPVLGSMA 245
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSP----LTRDAGGPL---DPVLEKIA 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 246 KKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
5-299 |
3.99e-90 |
|
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: 270.56 E-value: 3.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 5 QQTVRLSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGtVKREDIFYTSK 84
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTW---QAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 85 VWCTFH-RPELvrvCLEQSLKQLQLDYVDLYLIHFPMAMKPGENY--LPKDENGK--LIYDAvDICDTWEAMEKCKDAGL 159
Cdd:cd19121 77 LWSTYHrRVEL---CLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHdlFPTLPDGSrdLDWDW-NHVDTWKQMEKVLKTGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 160 AKSIGVSNFNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGShrekqwvdQSSPVLLDNP 239
Cdd:cd19121 153 TKAIGVSNYSIPYLEELLKHA--TVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS--------TGSPLISDEP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 240 VLgSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFqlTSEDMKVLDDL 299
Cdd:cd19121 223 VV-EIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-305 |
1.11e-88 |
|
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: 267.77 E-value: 1.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 6 QTVRLSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKV 85
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCW---KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 86 WCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKP---GENYLPKDENG---KLIYDAVDICDTWEAMEKCKDAGL 159
Cdd:cd19113 78 WNNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFvpiEEKYPPGFYCGdgdNFVYEDVPILDTWKALEKLVDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 160 AKSIGVSNFNRRQLEKILKkpGLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALG--SHRE-KQWVDQSSPVLL 236
Cdd:cd19113 158 IKSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqSFVElNQGRALNTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13487925 237 DNPVLGSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
6-305 |
7.29e-88 |
|
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: 265.82 E-value: 7.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 6 QTVRLSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKV 85
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 86 WCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMK---PGENYLP--KDENGKLIYDAVDICDTWEAMEKCKDAGLA 160
Cdd:cd19115 80 WNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 161 KSIGVSNFNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALG--SHREKQWVD-QSSPVLLD 237
Cdd:cd19115 160 RSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqSFLELDLPGaKDTPPLFE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 238 NPVLGSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:cd19115 238 HDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-300 |
1.84e-87 |
|
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: 262.69 E-value: 1.84e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 7 TVRLSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRskiaDGTVKREDIFYTSKVW 86
Cdd:cd19131 1 TITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKpgenylpkdenGKLIydavdicDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19131 74 NSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQ-----------DKYV-------ETWKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 NFNRRQLEKILKKPGLKykPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPVLGSMAK 246
Cdd:cd19131 136 NFTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAE 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 13487925 247 KYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLN 300
Cdd:cd19131 203 KHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-305 |
1.73e-86 |
|
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: 260.79 E-value: 1.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 7 TVRLSDGHFIPILGFGTYAPQEvpKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRskiaDGTVKREDIFYTSKVW 86
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEE--GSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPmamKPGENYlpkdengkliydavdicDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19157 75 NADQGYDSTLKAFEASLERLGLDYLDLYLIHWP---VKGKYK-----------------ETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 NFNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPVLGSMAK 246
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 13487925 247 KYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:cd19157 202 KYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-300 |
4.13e-86 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 259.29 E-value: 4.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 8 VRLSDGHFIPILGFGTYapQEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSkiadGTVKREDIFYTSKVWC 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVF--QTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 88 TFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKpgenylpkdengkliydavdICDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19126 75 DDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDK--------------------FIDTWKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 168 FNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPVLGSMAKK 247
Cdd:cd19126 135 FQEHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 13487925 248 YNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLN 300
Cdd:cd19126 202 YGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
7-305 |
7.79e-86 |
|
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: 260.50 E-value: 7.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 7 TVRLSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVW 86
Cdd:cd19112 2 TITLNSGHKMPVIGLGVW---RMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CTFHrpELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKP---GENYLPKDENGKLIYDA-VDICDTWEAMEKCKDAGLAKS 162
Cdd:cd19112 79 NSDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLDIDVtISLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 163 IGVSNFNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALG-SHREKQWVDQSSPvlLDNPVL 241
Cdd:cd19112 157 IGISNYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDDPVL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13487925 242 GSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:cd19112 233 KDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-300 |
6.60e-85 |
|
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: 256.43 E-value: 6.60e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 10 LSDGHFIPILGFGTYApqeVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSkiadGTVKREDIFYTSKVWCTF 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYP---LKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 90 HRPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenyLPKdeNGKLIydavdicDTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWP---------NPS--RDLYV-------EAWQALIEAREEGLVRSIGVSNFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 170 RRQLEKILKKPGLKykPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREkqwvdqsspvLLDNPVLGSMAKKYN 249
Cdd:cd19132 136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG----------LLDEPVIKAIAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 13487925 250 RTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLN 300
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-299 |
1.50e-84 |
|
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: 256.66 E-value: 1.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 8 VRLSDGHFIPILGFGTYAPQEvPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWC 87
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 88 TFHRPelVRVCLEQSLKQLQLDYVDLYLIHFPMAMK-----PGENYLPKDENGKLIYDA-VDICDTWEAMEKCKDAGLAK 161
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAAsGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 162 SIGVSNFNRRQLEKILKKpgLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREKqwvdqsspvLLDNPVL 241
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPLV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 242 GSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVfeFQLTSEDMKVLDDL 299
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDI 285
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-300 |
9.19e-84 |
|
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: 253.27 E-value: 9.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 8 VRLSDGHFIPILGFGTYapqEVPKSKATE-ATKIAIDAGFRHIDSASMYQNEKEVGLAIRskiaDGTVKREDIFYTSKVW 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAmkpgenylpkdengkliydavDICDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 NFNRRQLEKILkkPGLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqssPVLLDNPVLGSMAK 246
Cdd:cd19133 133 NFYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGR---------NNLFENPVLTEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 13487925 247 KYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLN 300
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-299 |
7.07e-83 |
|
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: 251.02 E-value: 7.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTFHRP 92
Cdd:cd19140 5 GVRIPALGLGTY---PLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 93 ELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylPKDengkliydaVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWP----------NKD---------VPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 173 LEKILKKPGLKYkpVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPVLGSMAKKYNRTP 252
Cdd:cd19140 139 LREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 13487925 253 ALIALRYQLQR-GVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19140 206 AQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-305 |
3.63e-81 |
|
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: 247.05 E-value: 3.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 8 VRLSDGHFIPILGFGTYAPQEvpKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKiadgTVKREDIFYTSKVWC 87
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQD--GAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 88 TFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAmkpgenylpkdenGKLIydavdicDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19156 75 SDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVK-------------GKFK-------DTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 168 FNRRQLEKILKKpgLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPVLGSMAKK 247
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 248 YNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:cd19156 202 YGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-299 |
6.05e-81 |
|
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: 247.05 E-value: 6.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 17 PILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFHRPELVR 96
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 97 VCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKI 176
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 177 LKKpgLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvDQSSPVLLDNPVLGSMAKKYNRTPALIA 256
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSY-----GDGNLTFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 13487925 257 LRYQLQR---GVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19128 232 IAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-299 |
1.54e-77 |
|
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: 237.99 E-value: 1.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 7 TVRLSDGHFIPILGFGT-----YApqevpkskaTEATKIAI-DAGFRHIDSASMYQNEKEVGLAIRskiADGtVKREDIF 80
Cdd:cd19135 4 TVRLSNGVEMPILGLGTshsggYS---------HEAVVYALkECGYRHIDTAKRYGCEELLGKAIK---ESG-VPREDLF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 81 YTSKVWCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENylPKDEngkliydavdICDTWEAMEKCKDAGLA 160
Cdd:cd19135 71 LTTKLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN--VKET----------RAETWRALEELYDEGLC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 161 KSIGVSNFNRRQLEKILKKPGLKykPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPV 240
Cdd:cd19135 139 RAIGVSNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEPT 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 13487925 241 LGSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19135 206 VTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-305 |
1.62e-77 |
|
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: 239.00 E-value: 1.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFHRP 92
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 93 ELVRVCLEQSLKQLQLDYVDLYLIHFPMAMK---PGENYLP---KDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFlwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 NFNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREKQWVDQSSPV--LLDNPVLGSM 244
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487925 245 AKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-300 |
2.78e-71 |
|
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: 221.90 E-value: 2.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 8 VRLSDGHFIPILGFGTYApqeVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKiadgTVKREDIFYTSKVWC 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQ---TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 88 TFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMkpgenylpkdengkliyDAVDICDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPVPN-----------------DFDRTIQAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 168 FNRRQLEKILKKPGLKykPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGS-HREKQWVDQSSPVLLDNPVLGSMAK 246
Cdd:cd19127 137 FTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvMRYGASGPTGPGDVLQDPTITGLAE 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 13487925 247 KYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLN 300
Cdd:cd19127 215 KYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-301 |
2.61e-70 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 220.19 E-value: 2.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 10 LSDGHFIPILGFGTYApQEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADG-TVKREDIFYTSKVWCT 88
Cdd:cd19122 3 LNNGVKIPAVGFGTFA-NEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 89 FHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPK-DENGKLIYDAvDICD----TWEAMEKCKDAGLAKSI 163
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILK-DLTEnpepTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 164 GVSNFNRRQLEKILKKPglKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREkqwVDQSSPVLLDNPVLGS 243
Cdd:cd19122 161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ---VPSTGERVSENPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 244 MAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEfqLTSEDMKVLDDLNK 301
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQVAK 291
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
7-305 |
5.57e-70 |
|
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: 218.57 E-value: 5.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 7 TVRLSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRskiADGtVKREDIFYTSKVW 86
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVG---ELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASG-IPRGELFVTTKLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAmkpgenylpkdENGKLIydavdicDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19134 75 TPDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKYV-------DSWGGLMKLREEGLARSIGVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 NFNRRQLEKILKKPGlkYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPVLGSMAK 246
Cdd:cd19134 137 NFTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAA 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 13487925 247 KYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRY 305
Cdd:cd19134 204 AHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-300 |
6.06e-69 |
|
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: 215.54 E-value: 6.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 10 LSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTF 89
Cdd:cd19130 4 LNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 90 HRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKpgENYLpkdengkliydavdicDTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAA--GNYV----------------HTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 170 RRQLEKILKKPGLKykPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGshrekqwvdQSSpvLLDNPVLGSMAKKYN 249
Cdd:cd19130 139 PPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLG---------QGK--LLGDPPVGAIAAAHG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 13487925 250 RTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLN 300
Cdd:cd19130 206 KTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-300 |
6.00e-67 |
|
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: 211.40 E-value: 6.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFGTYA----PQEVPKSKATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIrskiADGTVKREDIFYTSKV------ 85
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 86 WCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkDENgkliydaVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP------------DPD-------TPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 166 SNFNRRQLEKILKKPglKYKPVCNQVECHPY--LNQGKLLDFCRSKDIVLVAYSALGS----------------HREKQW 227
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487925 228 VDQSSPVLLDNPVLGSMAKKYNRTPALIALRY--QLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLN 300
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-299 |
8.72e-67 |
|
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: 209.90 E-value: 8.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTY--APQEVpkskaTEATKIAIDAGFRHIDSASMYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTFHRPE 93
Cdd:cd19139 1 IPAFGLGTFrlKDDVV-----IDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 94 LVRVCLEQSLKQLQLDYVDLYLIHFPMamkpgenylpkdengklIYDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQL 173
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVDLTLIHWPS-----------------PNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 174 EKILKKPGlKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPVLGSMAKKYNRTPA 253
Cdd:cd19139 135 DEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPA 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 13487925 254 LIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19139 203 QIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
16-297 |
2.51e-65 |
|
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: 206.31 E-value: 2.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYA---PQEVPKS---KATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRskiadgTVKREDIFYTSKVW 86
Cdd:cd19072 4 VPVLGLGTWGiggGMSKDYSddkKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CT-FHRPELVRVClEQSLKQLQLDYVDLYLIHFPmamkpgenylpkdengkliYDAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19072 78 PDhLKYDDVIKAA-KESLKRLGTDYIDLYLIHWP-------------------NPSIPIEETLRAMEELVEEGKIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 166 SNFNRRQLEKILKKPGlKYKPVCNQVECHpYLNQG---KLLDFCRSKDIVLVAYSALGsHREKQWVDQSspvlldnPVLG 242
Cdd:cd19072 138 SNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLE-KGKLSNAKGS-------PLLD 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 13487925 243 SMAKKYNRTPALIALRYQLQR-GVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLD 297
Cdd:cd19072 208 EIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-304 |
6.37e-65 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 206.08 E-value: 6.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 3 SKQQTVRLSDGHFIPILGFGTYapqEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSkiadGTVKREDIFYT 82
Cdd:PRK11565 2 ANPTVIKLQDGNVMPQLGLGVW---QASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 83 SKVWCTFHRPelVRVCLEQSLKQLQLDYVDLYLIHFPMAMKpgENYLpkdengkliydavdicDTWEAMEKCKDAGLAKS 162
Cdd:PRK11565 75 TKLWNDDHKR--PREALEESLKKLQLDYVDLYLMHWPVPAI--DHYV----------------EAWKGMIELQKEGLIKS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 163 IGVSNFNRRQLEKILKKPGLKykPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGshrekqwvdQSSPVLLDNPVLG 242
Cdd:PRK11565 135 IGVCNFQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLA---------QGGKGVFDQKVIR 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487925 243 SMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIR 304
Cdd:PRK11565 204 DLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-297 |
1.14e-55 |
|
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: 181.68 E-value: 1.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 6 QTVRLSDGHFIPILGFGTYAPQEVPKSKATE--ATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgtvkREDIF 80
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAQEieALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 81 YTSKVWCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkdengkliyDAVDICDTWEAMEKCKDAGLA 160
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR--------------------GGVPLAETVAAMEELKKEGKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 161 KSIGVSNFNRRQLEKILKKPGLKyKPVCNQVECHpYLNQG---KLLDFCRSKDIVLVAYSALGSHREkqwvdqSSPVLLD 237
Cdd:cd19138 134 RAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN-LGSRGieyDLLPWCREHGVPVMAYSPLAQGGL------LRRGLLE 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487925 238 NPVLGSMAKKYNRTPALIALRYQL-QRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLD 297
Cdd:cd19138 206 NPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-321 |
2.16e-52 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 173.29 E-value: 2.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYAPQEVPkskATEATKIAIDAGFRHIDSASMYQNEKEVGLAIrskiADGTVKREDIFYTSKVWCTFHRPELV 95
Cdd:PRK11172 3 IPAFGLGTFRLKDQV---VIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 96 RVCLEQSLKQLQLDYVDLYLIHFPmamKPGenylpkdengkliyDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:PRK11172 76 IPSLKESLQKLRTDYVDLTLIHWP---SPN--------------DEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 176 ILKKPGlKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHRekqwvdqsspVLLDnPVLGSMAKKYNRTPALI 255
Cdd:PRK11172 139 AIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK----------VLKD-PVIARIAAKHNATPAQV 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487925 256 ALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRYISGSSFKdhpdfPFWD 321
Cdd:PRK11172 207 ILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSPEGLA-----PEWD 267
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-297 |
1.72e-48 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 163.13 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFGTYA------PQEVPKSKATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRSkiadgtVKREDIFYTS 83
Cdd:cd19137 1 GEKIPALGLGTWGiggfltPDYSRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 84 KVWCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgENYLPKDEngkliydavdicdTWEAMEKCKDAGLAKSI 163
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP------NPNIPLEE-------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 164 GVSNFNRRQLEKILKKpgLKYKPVCNQVEC----HPYLNQGkLLDFCRSKDIVLVAYSALgshrekqwvdqSSPVLLDNP 239
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYnledRDPERDG-LLEYCQKNGITVVAYSPL-----------RRGLEKTNR 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 13487925 240 VLGSMAKKYNRTPALIALRYQLQR-GVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLD 297
Cdd:cd19137 202 TLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-297 |
9.26e-43 |
|
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: 149.21 E-value: 9.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFGTYA-----PQEVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgtvkREDIFYTSK 84
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 85 V---WCTFH------RPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkDENgkliydaVDICDTWEAMEKCK 155
Cdd:cd19084 74 CglrWDGGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 156 DAGLAKSIGVSNFNRRQLEKIlkkpgLKY-KPVCNQVechPY--LNQG---KLLDFCRSKDIVLVAYSAL------GSHR 223
Cdd:cd19084 135 KEGKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEREieeELLPYCRENGIGVLPYGPLaqglltGKYK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 224 EKQWVDQ----------SSPVLLDNP----VLGSMAKKYNRTPALIALRYQLQR-GV-VVLAKSFSEKRIKENMQVFEFQ 287
Cdd:cd19084 207 KEPTFPPddrrsrfpffRGENFEKNLeivdKLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWE 286
|
330
....*....|
gi 13487925 288 LTSEDMKVLD 297
Cdd:cd19084 287 LTEEELKEID 296
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
16-297 |
3.17e-42 |
|
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: 147.76 E-value: 3.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYA---------PQEVPKSkATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRskiadGTVKREDIFYTS 83
Cdd:cd19093 2 VSPLGLGTWQwgdrlwwgyGEYGDED-LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 84 KVWCTFHR--PELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpGENYLPkdengkliydavdICDTWEAMEKCKDAGLAK 161
Cdd:cd19093 76 KFAPLPWRltRRSVVKALKASLERLGLDSIDLYQLHWP-----GPWYSQ-------------IEALMDGLADAVEEGLVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 162 SIGVSNFNRRQLEKI---LKKPGlkYKPVCNQVE---CHPYLNQGKLLDFCRSKDIVLVAYSALG----------SHR-- 223
Cdd:cd19093 138 AVGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspENPpp 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 224 --------EKQWvDQSSPVLLdnpVLGSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKV 295
Cdd:cd19093 216 ggrrrlfgRKNL-EKVQPLLD---ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAE 291
|
..
gi 13487925 296 LD 297
Cdd:cd19093 292 LD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
6-299 |
3.62e-42 |
|
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: 148.02 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 6 QTVRL-SDGHFIPILGFGT----YAPQEVPKSKATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRSKiadgtvKRE 77
Cdd:COG0667 2 EYRRLgRSGLKVSRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 78 DIFYTSKV--------WCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkDENgkliydaVDICDTWE 149
Cdd:COG0667 76 DVVIATKVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP------------DPD-------TPIEETLG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 150 AMEKCKDAGLAKSIGVSNFNRRQLEKILKKPGLKYKPVCNQVEchpY--LNQ---GKLLDFCRSKDIVLVAYSALGS--- 221
Cdd:COG0667 137 ALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAYSPLAGgll 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 222 ---HREKQWVDQSS--------PVLLDN-----PVLGSMAKKYNRTPALIALRYQLQRGVVVL----AKsfSEKRIKENM 281
Cdd:COG0667 214 tgkYRRGATFPEGDraatnfvqGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSvipgAR--SPEQLEENL 291
|
330
....*....|....*...
gi 13487925 282 QVFEFQLTSEDMKVLDDL 299
Cdd:COG0667 292 AAADLELSAEDLAALDAA 309
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-303 |
1.92e-39 |
|
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: 140.41 E-value: 1.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYA--------PQEVPKSKATeaTKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgtvkREDIFYTSK 84
Cdd:cd19085 1 VSRLGLGCWQfgggywwgDQDDEESIAT--IHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 85 VWCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMkpgenylpkdengkliydaVDICDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19085 72 VSPDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSD-------------------VPLEETMEALEKLKEEGKIRAIG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 165 VSNFNRRQLEKILkKPGlkyKPVCNQVechPYlN------QGKLLDFCRSKDIVLVAYSALGS----------------- 221
Cdd:cd19085 133 VSNFGPAQLEEAL-DAG---RIDSNQL---PY-NllwraiEYEILPFCREHGIGVLAYSPLAQglltgkfssaedfppgd 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 222 -------HREKQWVDQSSPVLldnPVLGSMAKKYNRTPALIALRYQLQRGVV--VLAKSFSEKRIKENMQVFEFQLTSED 292
Cdd:cd19085 205 artrlfrHFEPGAEEETFEAL---EKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSV 281
|
330
....*....|.
gi 13487925 293 MKVLDDLNKNI 303
Cdd:cd19085 282 LERLDEISDPL 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
19-282 |
2.43e-32 |
|
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: 119.93 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFGTYA-PQEVPKSKATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRSKiadgtVKREDIFYTSKVWCTFHR--- 91
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPGGdps 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 92 -----PELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkDENgkliydaVDICDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd06660 78 rsrlsPEHIRRDLEESLRRLGTDYIDLYYLHRD------------DPS-------TPVEETLEALNELVREGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 NFNRRQLEKILK--KPGLKYKPVCNQVE---CHPYLNQGKLLDFCRSKDIVLVAYSALGShrekqwvdqsspvlldnpvl 241
Cdd:cd06660 139 NWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR-------------------- 198
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 13487925 242 GsmakkynrtPALIALRYQLQR--GVVVLAKSFSEKRIKENMQ 282
Cdd:cd06660 199 G---------PAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-299 |
6.65e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 104.68 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYA-----------PQEVPKSKAteATKIAIDAGFRHIDSASMY---QNEKEVGLAIRSKiadgtvkREDIFY 81
Cdd:cd19102 1 LTTIGLGTWAiggggwgggwgPQDDRDSIA--AIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 82 TSK---VW------CTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGEnylpkdengkliydavdicDTWEAME 152
Cdd:cd19102 72 ATKcglLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIE-------------------EAWGALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 153 KCKDAGLAKSIGVSNFNRRQLEKILKKPGLKYkpvcNQVechPY--LNQG---KLLDFCRSKDIVLVAYSALGS-----H 222
Cdd:cd19102 133 ELKEEGKVRAIGVSNFSVDQMKRCQAIHPIAS----LQP---PYslLRRGieaEILPFCAEHGIGVIVYSPMQSglltgK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 223 REKQWV--------DQSSPV-----------LLDnpVLGSMAKKYNRTPALIALRYQLQR----GVVVLAKsfSEKRIKE 279
Cdd:cd19102 206 MTPERVaslpaddwRRRSPFfqepnlarnlaLVD--ALRPIAERHGRTVAQLAIAWVLRRpevtSAIVGAR--RPDQIDE 281
|
330 340
....*....|....*....|
gi 13487925 280 NMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19102 282 TVGAADLRLTPEELAEIEAL 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-292 |
7.48e-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: 101.48 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 18 ILGFGTYAPQEVPKSKATEATKIAIDAG---FRHIDSASMYQNEKEVGLAIRSKiadgTVKREDIFYTSKV--------- 85
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGittFDHADIYGGGKCEELFGEALALN----PGLREKIEIQTKCgirlgddpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 86 -WCTFH---RPELVRVCLEQSLKQLQLDYVDLYLIHFP-MAMKPGEnylpkdengkliydavdicdTWEAMEKCKDAGLA 160
Cdd:cd19092 86 pGRIKHydtSKEHILASVEGSLKRLGTDYLDLLLLHRPdPLMDPEE--------------------VAEAFDELVKSGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 161 KSIGVSNFNRRQLEkILKKpGLKYKPVCNQVEC---HPYLNQGKLLDFCRSKDIVLVAYSALGSHREKQWVDQSSPVLLD 237
Cdd:cd19092 146 RYFGVSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 238 npVLGSMAKKYNRTPALIALRYQLQ---RGVVVLAKSFSEkRIKENMQVFEFQLTSED 292
Cdd:cd19092 224 --ALEELAEEYGVTIEAIALAWLLRhpaRIQPILGTTNPE-RIRSAVKALDIELTREE 278
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-299 |
2.27e-24 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 101.43 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYAPQEVPKSKATEATKIAIDAGFRHIDSASMY-QNEKEVGLAIRSKiadgtvkREDIFYTSKVWCTFHRPEL 94
Cdd:COG1453 13 VSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWVRDPED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 95 VRVCLEQSLKQLQLDYVDLYLIHfpmamkpgenYLPKDENGKLIYDAVDIcdtWEAMEKCKDAGLAKSIGVSNFNRRQ-L 173
Cdd:COG1453 86 MRKDLEESLKRLQTDYIDLYLIH----------GLNTEEDLEKVLKPGGA---LEALEKAKAEGKIRHIGFSTHGSLEvI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 174 EKILKkpglKYK-PVCN-QVEchpYLNQG-----KLLDFCRSKDIVLVAYSALGSHRekqwvdqsspvLLDNPVLGSMAK 246
Cdd:COG1453 153 KEAID----TGDfDFVQlQYN---YLDQDnqageEALEAAAEKGIGVIIMKPLKGGR-----------LANPPEKLVELL 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 13487925 247 KYNRTPALIALRYQLQR-GVVVL---AKSFSEkrIKENMQVFE--FQLTSEDMKVLDDL 299
Cdd:COG1453 215 CPPLSPAEWALRFLLSHpEVTTVlsgMSTPEQ--LDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-299 |
5.14e-24 |
|
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: 99.61 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFG--TYAPQEVPKSK-----ATEAT---KIAIDAGFRHIDSASMY---QNEKEVGLAIRSKiadgtvkREDI 79
Cdd:cd19091 10 GLKVSELALGtmTFGGGGGFFGAwggvdQEEADrlvDIALDAGINFFDTADVYsegESEEILGKALKGR-------RDDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 80 FYTSKVwcTFH-----------RPELVRVClEQSLKQLQLDYVDLYLIHFPMAMKPGEnylpkdengkliydavdicDTW 148
Cdd:cd19091 83 LIATKV--RGRmgegpndvglsRHHIIRAV-EASLKRLGTDYIDLYQLHGFDALTPLE-------------------ETL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 149 EAMEKCKDAGLAKSIGVSNFNRRQLEKIL---KKPGLKyKPVCNQVEchpYLNQGK-----LLDFCRSKDIVLVAYSALG 220
Cdd:cd19091 141 RALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQAY---YSLLGRdleheLMPLALDQGVGLLVWSPLA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 221 SHR--EKQWVDQSSPVL-------LDNP------------VLGSMAKKYNRTPALIALRYQLQR----GVVVLAKsfSEK 275
Cdd:cd19091 217 GGLlsGKYRRGQPAPEGsrlrrtgFDFPpvdrergydvvdALREIAKETGATPAQVALAWLLSRptvsSVIIGAR--NEE 294
|
330 340
....*....|....*....|....
gi 13487925 276 RIKENMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19091 295 QLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
41-292 |
8.50e-24 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 98.69 E-value: 8.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 41 AIDAGFRHIDSA---SMYQNEKEVGLAIRSKiadgTVKREDIFYTSKvwC--------TFHRP-------ELVRVCLEQS 102
Cdd:COG4989 40 ALELGITTFDHAdiyGGYTCEALFGEALKLS----PSLREKIELQTK--CgirlpseaRDNRVkhydtskEHIIASVEGS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 103 LKQLQLDYVDLYLIHFPmamkpgenylpkdengkliyDA-VDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEkILKKpG 181
Cdd:COG4989 114 LRRLGTDYLDLLLLHRP--------------------DPlMDPEEVAEAFDELKASGKVRHFGVSNFTPSQFE-LLQS-A 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 182 LKYKPVCNQVECHPY----LNQGkLLDFCRSKDIVLVAYSALGSHREKQWVDQSSPVLldNPVLGSMAKKYNRTPALIAL 257
Cdd:COG4989 172 LDQPLVTNQIELSLLhtdaFDDG-TLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRL--RAALDELAEKYGVSPEAIAL 248
|
250 260 270
....*....|....*....|....*....|....*...
gi 13487925 258 RYqLQR---GVVVLAKSFSEKRIKENMQVFEFQLTSED 292
Cdd:COG4989 249 AW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-269 |
2.24e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 96.40 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFGTYAPQEVPKSKATEATKIAIDAGFRHIDSASMYQN-EKEVGLAIRSKiadgtvkREDIFYTSKVWctFHR 91
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTG--ARD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 92 PELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKpgENYLPKDENGkliydavdicdTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19100 79 YEGAKRDLERSLKRLGTDYIDLYQLHAVDTEE--DLDQVFGPGG-----------ALEALLEAKEEGKIRFIGISGHSPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 172 QLEKILKKPglkykpvcnqvechpylnqgkllDFcrskDIVLVAYSALGSHREKQwVDQSSPVLLDN--------PVLGS 243
Cdd:cd19100 146 VLLRALETG-----------------------EF----DVVLFPINPAGDHIDSF-REELLPLAREKgvgviamkVLAGG 197
|
250 260
....*....|....*....|....*.
gi 13487925 244 MAKKYNRTPALIALRYQLQRGVVVLA 269
Cdd:cd19100 198 RLLSGDPLDPEQALRYALSLPPVDVV 223
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-221 |
5.48e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 97.00 E-value: 5.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFGTY--APQEVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKIADGTVKREDIFYTSKV-------- 85
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 86 --------------------------WCTFHrPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgENYLPKDeNGKLIY 139
Cdd:cd19099 86 eplrplkyleeklgrglidvadsaglRHCIS-PAYLEDQIERSLKRLGLDTIDLYLLHNP------EEQLLEL-GEEEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 140 DAVDicDTWEAMEKCKDAGLAKSIGVSNFN------------------RRQLEKILKKPGLK-----YKPVCNQVECHPY 196
Cdd:cd19099 158 DRLE--EAFEALEEAVAEGKIRYYGISTWDgfrappalpghlsleklvAAAEEVGGDNHHFKviqlpLNLLEPEALTEKN 235
|
250 260
....*....|....*....|....*...
gi 13487925 197 LNQGK---LLDFCRSKDIVLVAYSALGS 221
Cdd:cd19099 236 TVKGEalsLLEAAKELGLGVIASRPLNQ 263
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-297 |
7.64e-23 |
|
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: 96.13 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 42 IDAGFRHIDSASMY----------QNEKEVGLAIRSKiadgtVKREDIFYTSKV--WCTFHRPEL----VRVCLEQSLKQ 105
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSR-----GKRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 106 LQLDYVDLYLIHFPmamkpgenylpkDengkliyDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKIL---KKPGL 182
Cdd:cd19081 111 LQTDYIDLYQAHWD------------D-------PATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALelsRQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 183 KyKPVCNQ-----VECHPYlnQGKLLDFCRSKDIVLVAYSALGS------HREKQWVDQSSPV-----LLDNP------- 239
Cdd:cd19081 172 P-RYVSLQpeynlVDRESF--EGELLPLCREEGIGVIPYSPLAGgfltgkYRSEADLPGSTRRgeaakRYLNErglrild 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 240 VLGSMAKKYNRTPALIALRYQLQRGVV--VLAKSFSEKRIKENMQVFEFQLTSEDMKVLD 297
Cdd:cd19081 249 ALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
41-289 |
2.63e-22 |
|
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: 93.82 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 41 AIDAGFRHIDSASMY---QNEKEVGLAIRSKIAD-------GTVKREDifytsKVWCTFHRPELVRVCLEQSLKQLQLDY 110
Cdd:cd19088 33 ALELGVNFIDTADSYgpdVNERLIAEALHPYPDDvviatkgGLVRTGP-----GWWGPDGSPEYLRQAVEASLRRLGLDR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 111 VDLYLIHFPMamkpgenylpkdengkliyDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKILKKPGLkykpVCNQ 190
Cdd:cd19088 108 IDLYQLHRID-------------------PKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI----VSVQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 191 VECHPYLNQG-KLLDFCRSKDIVLVAYSALGSHrekqwvdqssPVLLDNPVLGSMAKKYNRTPALIALRYQLQRG--VVV 267
Cdd:cd19088 165 NRYNLANRDDeGVLDYCEAAGIAFIPWFPLGGG----------DLAQPGGLLAEVAARLGATPAQVALAWLLARSpvMLP 234
|
250 260
....*....|....*....|..
gi 13487925 268 LAKSFSEKRIKENMQVFEFQLT 289
Cdd:cd19088 235 IPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
6-294 |
5.36e-22 |
|
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: 93.82 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 6 QTVRL-SDGHFIPILGFGT------YAPQEVPKSKATeaTKIAIDAGFRHIDSASMYQ---NEKEVGLAIRSKiadgtvk 75
Cdd:cd19076 1 PTRKLgTQGLEVSALGLGCmgmsafYGPADEEESIAT--LHRALELGVTFLDTADMYGpgtNEELLGKALKDR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 76 REDIFYTSK---VWCTFH-------RPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkDENgkliydaVDIC 145
Cdd:cd19076 72 RDEVVIATKfgiVRDPGSgfrgvdgRPEYVRAACEASLKRLGTDVIDLYYQHRV------------DPN-------VPIE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 146 DTWEAMEKCKDAGLAKSIGVSNFN----RR----------QLEkilkkpglkYKPVCNQVEchpylnqGKLLDFCRSKDI 211
Cdd:cd19076 133 ETVGAMAELVEEGKVRYIGLSEASadtiRRahavhpitavQSE---------YSLWTRDIE-------DEVLPTCRELGI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 212 VLVAYSALG-----------SHREKQWVDQSSP-----------VLLDNpvLGSMAKKYNRTPALIALRYQLQRG--VVV 267
Cdd:cd19076 197 GFVAYSPLGrgfltgaikspEDLPEDDFRRNNPrfqgenfdknlKLVEK--LEAIAAEKGCTPAQLALAWVLAQGddIVP 274
|
330 340
....*....|....*....|....*..
gi 13487925 268 LAKSFSEKRIKENMQVFEFQLTSEDMK 294
Cdd:cd19076 275 IPGTKRIKYLEENVGALDVVLTPEELA 301
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
6-302 |
6.13e-22 |
|
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: 94.05 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 6 QTVRLS-DGHFIPILGFGT------YAPQEvPKSKATEATKIAIDAGFRHIDSASMYQ-NEKEVGLAIrsKIADGtvKRE 77
Cdd:cd19144 2 PTRTLGrNGPSVPALGFGAmglsafYGPPK-PDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWF--KQNPG--KRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 78 DIFYTSKVWCTFHR----------PELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENylpkdengkliydavdicdT 147
Cdd:cd19144 77 KIFLATKFGIEKNVetgeysvdgsPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEK-------------------T 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 148 WEAMEKCKDAGLAKSIGVSNFNRRQLEKilkkpGLKYKPVCN-QVECHPYL-----NQGKLLDFCRSKDIVLVAYSAL-- 219
Cdd:cd19144 138 VAAMAELVQEGKIKHIGLSECSAETLRR-----AHAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLgr 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 220 ----GSHR-----EKQWVDQSSP-----------VLLDNpvLGSMAKKYNRTPALIALRYQLQRG--VVVLAKSFSEKRI 277
Cdd:cd19144 213 gfltGAIRspddfEEGDFRRMAPrfqaenfpknlELVDK--IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRL 290
|
330 340
....*....|....*....|....*
gi 13487925 278 KENMQVFEFQLTSEDMKVLDDLNKN 302
Cdd:cd19144 291 EENLGALKVKLTEEEEKEIREIAEE 315
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-166 |
2.22e-21 |
|
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: 91.85 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 17 PILGFGTY----APQEVPKSKATEATKIAIDAGFRHIDSASMYQN-EKEVGLAIRskiadgTVKREDIFYTSKVwCTFHR 91
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA------ELPREPLVLSTKV-GRLPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 92 ------PELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPkdeNGKLiydavdicdtwEAMEKCKDAGLAKSIGV 165
Cdd:cd19090 74 dtadysADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP---GGAL-----------EALLELKEEGLIKHIGL 139
|
.
gi 13487925 166 S 166
Cdd:cd19090 140 G 140
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-298 |
5.74e-21 |
|
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: 91.18 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYA------PQEVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgtvkREDIFYTSK-- 84
Cdd:cd19149 11 ASVIGLGTWAigggpwWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATKcg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 85 -VWCT----FH------------RPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPgenylpkdengkliydavdICDT 147
Cdd:cd19149 84 lRWDReggsFFfvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETP-------------------IEET 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 148 WEAMEKCKDAGLAKSIGVSNFNRRQLEKILKKPGL-----KYKPVCNQVEchpylnqGKLLDFCRSKDIVLVAYSAL--- 219
Cdd:cd19149 145 MEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLdiiqeKYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLeqg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 220 --------------GSHRE-KQWVDQSS----PVLLDNpvLGSMAKKYNRTPALIALRYQLQRG--VVVLAKSFSEKRIK 278
Cdd:cd19149 218 lltgkitpdrefdaGDARSgIPWFSPENrekvLALLEK--WKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAE 295
|
330 340
....*....|....*....|
gi 13487925 279 ENMQVFEFQLTSEDMKVLDD 298
Cdd:cd19149 296 ENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-283 |
8.85e-21 |
|
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: 89.57 E-value: 8.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 13 GHFIPILGFGTYAPQevpkSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRskiadgTVKREDIFYTSKVWCT- 88
Cdd:cd19105 10 GLKVSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATKASPRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 89 -FHRPELVRVCLEQSLKQLQLDYVDLYLIHfpMAMKPGENYLpkdeNGKLIydavdicdtwEAMEKCKDAGLAKSIGVS- 166
Cdd:cd19105 80 dKKDKAELLKSVEESLKRLQTDYIDIYQLH--GVDTPEERLL----NEELL----------EALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 -NFNRRQLEKILKKPG-----LKYkpvcNqvechpYLNQG----KLLDFCRSKDIVLVAYSALGShrekqwvdqsspvLL 236
Cdd:cd19105 144 hDNMAEVLQAAIESGWfdvimVAY----N------FLNQPaeleEALAAAAEKGIGVVAMKTLAG-------------GY 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 13487925 237 DNPVLGSMAKKYNRTPALIALRYQLQR----GVVVLAKSFSEkrIKENMQV 283
Cdd:cd19105 201 LQPALLSVLKAKGFSLPQAALKWVLSNprvdTVVPGMRNFAE--LEENLAA 249
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-169 |
1.14e-20 |
|
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: 89.22 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 17 PILGFGTY----APQEVPKSKATEATKIAIDAGFRHIDSASMYQN-EKEVGLAIRskiadgTVKREDIFYTSKVWCTF-- 89
Cdd:cd19095 1 SVLGLGTSgigrVWGVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 90 ------HRPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenyLPKDENGKLIydavdicdtwEAMEKCKDAGLAKSI 163
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGP---------SDDELTGEVL----------ETLEDLKAAGKVRYI 135
|
....*.
gi 13487925 164 GVSNFN 169
Cdd:cd19095 136 GVSGDG 141
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
39-299 |
1.64e-20 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 89.79 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 39 KIAIDAGFRHIDSASMY---QNEKEVGLAIRSKiadgtvKREDIFYTSKVWCTF--------HRPELVRVCLEQSLKQLQ 107
Cdd:cd19083 40 REALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKFggdgsvlnNSPEFLRSAVEKSLKRLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 108 LDYVDLYLIHFPmamkpgENYLPKDEngkliydAVDicdtweAMEKCKDAGLAKSIGVSNFNRRQLeKILKKPGlkykpv 187
Cdd:cd19083 114 TDYIDLYYIHFP------DGETPKAE-------AVG------ALQELKDEGKIRAIGVSNFSLEQL-KEANKDG------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 188 cnQVEC--HPY--LNQ---GKLLDFCRSKDIVLVAYSALGS------------HREKQWVDQSSpvLLDNPV-------- 240
Cdd:cd19083 168 --YVDVlqGEYnlLQReaeEDILPYCVENNISFIPYFPLASgllagkytkdtkFPDNDLRNDKP--LFKGERfsenldkv 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487925 241 --LGSMAKKYNRTPALIALRYQLQRGVV--VLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19083 244 dkLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-297 |
1.65e-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: 89.58 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 9 RLSDGHfipilgfgTYAPQEvpkSKATEATKIAIDAGFRHIDSASMYQNEKE-VGLAIRSKIADGTVKREDIFYTSkvWC 87
Cdd:cd19101 11 QLSGGH--------GGIRDE---DAAVRAMAAYVDAGLTTFDCADIYGPAEElIGEFRKRLRRERDAADDVQIHTK--WV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 88 TFHR-----PELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGenYLpkdengkliydavdicDTWEAMEKCKDAGLAKS 162
Cdd:cd19101 78 PDPGeltmtRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPG--YL----------------DAAKHLAELQEEGKIRH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 163 IGVSNFNRRQLEKILKKPglkYKPVCNQVEcHPYLNQ---GKLLDFCRSKDIVLVAYSAL--GSHREKqWVDQSSP--VL 235
Cdd:cd19101 140 LGLTNFDTERLREILDAG---VPIVSNQVQ-YSLLDRrpeNGMAALCEDHGIKLLAYGTLagGLLSEK-YLGVPEPtgPA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 236 LDNP-----------------------VLGSMAKKYNRTPALIALRYQLQR----GVVVLAKsFSEkRIKENMQVFEFQL 288
Cdd:cd19101 215 LETRslqkyklmidewggwdlfqellrTLKAIADKHGVSIANVAVRWVLDQpgvaGVIVGAR-NSE-HIDDNVRAFSFRL 292
|
....*....
gi 13487925 289 TSEDMKVLD 297
Cdd:cd19101 293 DDEDRAAID 301
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
36-297 |
3.13e-20 |
|
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: 89.18 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 36 EATKI---AIDAGFRHIDSASMYQN---EKEVGLAIRSKIadgtvKREDIFYTSKVW---------CTFHRPELVRVClE 100
Cdd:cd19079 36 ESRPIikrALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYfpmgdgpngRGLSRKHIMAEV-D 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 101 QSLKQLQLDYVDLYLIHFPmamkpgenylpkDENgkliydaVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKIL--- 177
Cdd:cd19079 110 ASLKRLGTDYIDLYQIHRW------------DYE-------TPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALhla 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 178 KKPGLKyKPVCNQvechPYLN------QGKLLDFCRSKDIVLVAYSALGSHR---------EKQWVDQSSPVL------- 235
Cdd:cd19079 171 EKNGWT-KFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLARGRlarpwgdttERRRSTTDTAKLkydyfte 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487925 236 LDNPVL---GSMAKKYNRTPALIALRYQLQRGVVV--LAKSFSEKRIKENMQVFEFQLTSEDMKVLD 297
Cdd:cd19079 246 ADKEIVdrvEEVAKERGVSMAQVALAWLLSKPGVTapIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-285 |
2.92e-18 |
|
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: 82.61 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 17 PILGFGTY-APQEVPKSK-ATEATKI---AIDAGFRHIDSASMY---QNEKEVGLAIRskiadgTVKREDIFYTSK--VW 86
Cdd:cd19096 1 SVLGFGTMrLPESDDDSIdEEKAIEMiryAIDAGINYFDTAYGYgggKSEEILGEALK------EGPREKFYLATKlpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 cTFHRPELVRVCLEQSLKQLQLDYVDLYLIHfpMAMKPgeNYLPKDENGKLiydavdicdtWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19096 75 -SVKSAEDFRRILEESLKRLGVDYIDFYLLH--GLNSP--EWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 nF--NRRQLEKILKkpglkykpvCNQVEC----HPYLNQ-----GKLLDFCRSKDIVLVAysalgshrekqwvdqSSPV- 234
Cdd:cd19096 140 -FhdSPELLKEILD---------SYDFDFvqlqYNYLDQenqagRPGIEYAAKKGMGVII---------------MEPLk 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 13487925 235 ----LLDNPVLGSMAKKYNRTPALIALRYQL-QRGVVVLAKSFSEKR-IKENMQVFE 285
Cdd:cd19096 195 ggglANNPPEALAILCGAPLSPAEWALRFLLsHPEVTTVLSGMSTPEqLDENIAAAD 251
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
19-221 |
4.17e-18 |
|
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: 81.75 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFGTYA-----PQEVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgtvkREDIFYTSKVWCTFH 90
Cdd:cd19086 6 IGFGTWGlggdwWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 91 ---------RPELVRVCLEQSLKQLQLDYVDLYLIHFPMamkpgenylpkdengkliYDAVDICDTWEAMEKCKDAGLAK 161
Cdd:cd19086 79 ggperpqdfSPEYIREAVEASLKRLGTDYIDLYQLHNPP------------------DEVLDNDELFEALEKLKQEGKIR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487925 162 SIGVSNFNRRQLEKILKKPGlkykpvCNQVEcHPY--LNQG---KLLDFCRSKDIVLVAYSALGS 221
Cdd:cd19086 141 AYGVSVGDPEEALAALRRGG------IDVVQ-VIYnlLDQRpeeELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
36-299 |
1.60e-17 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 81.84 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 36 EATKI---AIDAGFRHIDSASMY----------QNEKEVGLAIRSKiadgtVKREDIFYTSKV-----WCTFHRPELVRV 97
Cdd:cd19094 19 EAHEQldyAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKK-----GNRDKVVLATKVagpgeGITWPRGGGTRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 98 -------CLEQSLKQLQLDYVDLYLIHFP---MAMKPGENYLPKDENgkliYDAVDICDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19094 94 drenireAVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEE----EDSVSFEEQLEALGELVKAGKIRHIGLSN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 168 ---FNRRQLEKILKKPGLKyKPVCNQvecHPY--LNQGKLLDF---CRSKDIVLVAYSALG------------------- 220
Cdd:cd19094 170 etpWGVMKFLELAEQLGLP-RIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLAggvltgkyldgaarpeggr 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 221 ----SHREKQWvdQSSPVLLDNPVLGSMAKKYNRTPALIALRYQLQR----GVVVLAKSFSEkrIKENMQVFEFQLTSED 292
Cdd:cd19094 246 lnlfPGYMARY--RSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRpfvtSTIIGATTLEQ--LKENIDAFDVPLSDEL 321
|
....*..
gi 13487925 293 MKVLDDL 299
Cdd:cd19094 322 LAEIDAV 328
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
19-291 |
6.00e-16 |
|
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: 76.86 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFGTYAP--QEVPKSKATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRskiadgTVKREDIFYTSKV-WCT---- 88
Cdd:cd19074 7 LSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALK------GWPRESYVISTKVfWPTgpgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 89 ----FHRPELVRvCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkDENgkliydaVDICDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19074 81 ndrgLSRKHIFE-SIHASLKRLQLDYVDIYYCHRY------------DPE-------TPLEETVRAMDDLIRQGKILYWG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 165 VSNFNRRQLEK---ILKKPGLkYKPVCNQVECHpYLNQGK---LLDFCRSKDIVLVAYSAL------GSHREKQWVDQSS 232
Cdd:cd19074 141 TSEWSAEQIAEahdLARQFGL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltGKYRDGIPPPSRS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487925 233 ------------PVLLDNPV-----LGSMAKKYNRTPALIALRYQLQRGVV--VLAKSFSEKRIKENMQVFEFQLTSE 291
Cdd:cd19074 219 ratdednrdkkrRLLTDENLekvkkLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
33-219 |
6.21e-16 |
|
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: 76.96 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 33 KATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRskiadGTVKREDIFYTSKV---W------CTFHRPELVRVCLE 100
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALK-----EYGKRDRVVIATKVgleWdeggevVRNSSPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 101 QSLKQLQLDYVDLYLIHFPmamkpgenylpkDEngkliydAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEkilkkp 180
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWP------------DP-------LVPIEETAEALKELLDEGKIRAIGVSNFSPEQME------ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13487925 181 glKYKPVCNQVECHPYLN------QGKLLDFCRSKDIVLVAYSAL 219
Cdd:cd19148 156 --TFRKVAPLHTVQPPYNlfereiEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-221 |
3.48e-15 |
|
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: 74.51 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 18 ILGFGTYAPQE--VPKSKATEATKIAIDAGFRHIDSASMYQ-----------NEKEVGLAIRSKIADGTVKRedifytsk 84
Cdd:cd19075 4 ILGTMTFGSQGrfTTAEAAAELLDAFLERGHTEIDTARVYPdgtseellgelGLGERGFKIDTKANPGVGGG-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 85 vwctfHRPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkDEngkliydAVDICDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19075 76 -----LSPENVRKQLETSLKRLKVDKVDVFYLHAP------------DR-------STPLEETLAAIDELYKEGKFKEFG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13487925 165 VSNFNRRQLEKILK--------KP----GLkYKPVCNQVEchpylnqGKLLDFCRSKDIVLVAYSALGS 221
Cdd:cd19075 132 LSNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLAG 192
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-299 |
5.79e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 73.91 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 41 AIDAGFRHIDSASMY---QNEKEVGLAIRskiadgTVKREDIFYTSKV--WCTFHRPELVRVCLEQSLKQLQLDYVDLYL 115
Cdd:cd19103 41 AMAAGLNLWDTAAVYgmgASEKILGEFLK------RYPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 116 IHFPMAMkpgENYLPKdengkLIydavdicdtweAMEKckdAGLAKSIGVSNFNRRQLEK---ILKKPGLKYKPVCNqve 192
Cdd:cd19103 115 IHNPADV---ERWTPE-----LI-----------PLLK---SGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQN--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 193 cHPYL-----NQGKLLDFCRSKDIVLVAYSAL-----------------GSHREKQWVDqsspvLLD-----NPVLGSMA 245
Cdd:cd19103 170 -HYSLlyrssEEAGILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGRAETYNP-----LLPqleelTAVMAEIG 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 13487925 246 KKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDL 299
Cdd:cd19103 244 AKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
18-297 |
5.48e-14 |
|
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: 71.10 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 18 ILGFGTYAPQEVPKSKATEATKIA---IDAGFRHIDSASMYQN---EKEVGLAIRSKiadgtvkREDIFYTSKVwcTF-- 89
Cdd:cd19080 14 ALGTMTFGTEWGWGADREEARAMFdayVEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKY--TMnr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 90 ----------HRPELVRvCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPK-DE---NGKLIYdaVDICDT--WEAmek 153
Cdd:cd19080 85 rpgdpnaggnHRKNLRR-SVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRAlDDlvrAGKVLY--VGISDTpaWVV--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 154 CKDAGLAKSIGVSNFNRRQLEkilkkpglkYKPVCNQVEchpylnqGKLLDFCRSKDIVLVAYSALG------------- 220
Cdd:cd19080 159 ARANTLAELRGWSPFVALQIE---------YSLLERTPE-------RELLPMARALGLGVTPWSPLGgglltgkyqrgee 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 221 SHREKQWVDQSSPVLLDN------PVLGSMAKKYNRTPALIALRYQLQRGVVVL----AKSFSEkrIKENMQVFEFQLTS 290
Cdd:cd19080 223 GRAGEAKGVTVGFGKLTErnwaivDVVAAVAEELGRSAAQVALAWVRQKPGVVIpiigARTLEQ--LKDNLGALDLTLSP 300
|
....*..
gi 13487925 291 EDMKVLD 297
Cdd:cd19080 301 EQLARLD 307
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
32-220 |
2.41e-13 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 69.52 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 32 SKATEATKIAI-----DAGFRHIDSASMYQN---EKEVGLAIRSKiadgtvkREDIFYTSKVWCTFH---------RPEL 94
Cdd:cd19087 25 GRTDEETSFAImdralDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVFGPMGddpndrglsRRHI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 95 VRVClEQSLKQLQLDYVDLYLIHFPmamkpgENYLPKDEngkliydavdicdTWEAMEKCKDAGLAKSIGVSNFNRRQLE 174
Cdd:cd19087 98 RRAV-EASLRRLQTDYIDLYQMHHF------DRDTPLEE-------------TLRALDDLVRQGKIRYIGVSNFAAWQIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13487925 175 KIL---KKPGL--------KYKPVCNQVECHpylnqgkLLDFCRSKDIVLVAYSALG 220
Cdd:cd19087 158 KAQgiaARRGLlrfvseqpMYNLLKRQAELE-------ILPAARAYGLGVIPYSPLA 207
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
20-297 |
1.24e-12 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 67.26 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 20 GFG----TYAPQEVPKSKATEATKIAIDAGFRHIDSASMY------QNEKEVGLAIRSKIADgtvkREDIFYTSKVWCTF 89
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEY----ADKVVLSVKGGLDP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 90 H------RPELVRVCLEQSLKQL-QLDYVDLylihFPMAMKPgenylpkdengkliyDAVDICDTWEAMEKCKDAGLAKS 162
Cdd:cd19077 85 DtlrpdgSPEAVRKSIENILRALgGTKKIDI----FEPARVD---------------PNVPIEETIKALKELVKEGKIRG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 163 IGVSNFNRRQLEKILKkpglKYKPVCNQVECHPY----LNQGkLLDFCRSKDIVLVAYSALGS----------------- 221
Cdd:cd19077 146 IGLSEVSAETIRRAHA----VHPIAAVEVEYSLFsreiEENG-VLETCAELGIPIIAYSPLGRglltgriksladipegd 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 222 HREKQwvDQSSP-------VLLDnpVLGSMAKKYNRTPALIAL---RYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSE 291
Cdd:cd19077 221 FRRHL--DRFNGenfeknlKLVD--ALQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDE 296
|
....*.
gi 13487925 292 DMKVLD 297
Cdd:cd19077 297 ELKEIN 302
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-221 |
1.54e-12 |
|
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: 67.00 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 17 PILGFGTYAPQEVPKSKATEATKI---AIDAGFRHIDSASMY---QNEKEVGLAIRSKiadgtvKREDIFYTSKV----- 85
Cdd:cd19162 1 PRLGLGAASLGNLARAGEDEAAATldaAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 86 -----WCTFHRPEL------VRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkDEngkliYDAVDICDTWEAMEKC 154
Cdd:cd19162 75 pgaagRPAGADRRFdfsadgIRRSIEASLERLGLDRLDLVFLHDP------------DR-----HLLQALTDAFPALEEL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 155 KDAGLAKSIGVSNFNRRQLEKILKKPGLKYKPVCNQvecHPYLNQG---KLLDFCRSKDIVLVAYSALGS 221
Cdd:cd19162 138 RAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAGR---YTLLDRRaatELLPLCAAKGVAVVAAGVFNS 204
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-298 |
3.60e-12 |
|
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: 65.72 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFG----TYAPQEVP-KSKATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRSKiadgtvkREDIFYTSKVWCTFH 90
Cdd:cd19078 7 IGLGcmgmSHGYGPPPdKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKFGFKID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 91 -----------RPELVRVCLEQSLKQLQLDYVDLYLIHFPmamkpgenylpkDENgkliydaVDICDTWEAMEKCKDAGL 159
Cdd:cd19078 80 ggkpgplgldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRV------------DPN-------VPIEEVAGTMKELIKEGK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 160 AKSIGVSNFNrrqlEKILKKpGLKYKPVCN-QVECH-----PylnQGKLLDFCRSKDIVLVAYSALG------------- 220
Cdd:cd19078 141 IRHWGLSEAG----VETIRR-AHAVCPVTAvQSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGkgfltgkidentk 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 221 --SHREKQWVDQSSP-------VLLDnpVLGSMAKKYNRTPALIALRYQLQRG--VVVLAKSFSEKRIKENMQVFEFQLT 289
Cdd:cd19078 213 fdEGDDRASLPRFTPealeanqALVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELT 290
|
....*....
gi 13487925 290 SEDMKVLDD 298
Cdd:cd19078 291 PEELREIED 299
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-259 |
4.93e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 64.86 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 31 KSKATEATKI---AIDAGFRHIDSASMYQN-EKEVGLAIRSKiadgtvkrEDIFYTSKV----WCTFHRPELVRVCLEQS 102
Cdd:cd19097 22 KPSEKEAKKIleyALKAGINTLDTAPAYGDsEKVLGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 103 LKQLQLDYVDLYLIHfpmamkpGENYLPKDeNGKLiydavdicdtWEAMEKCKDAGLAKSIGVSNFNRRQLEKILKKPGL 182
Cdd:cd19097 94 LKRLKVDSLDGLLLH-------NPDDLLKH-GGKL----------VEALLELKKEGLIRKIGVSVYSPEELEKALESFKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 183 KYkpVcnQVECHPY---LNQGKLLDFCRSKDIVLVAYSA-----LGSHREKqWVDQSSPV--LLDNpvLGSMAKKYNRTP 252
Cdd:cd19097 156 DI--I--QLPFNILdqrFLKSGLLAKLKKKGIEIHARSVflqglLLMEPDK-LPAKFAPAkpLLKK--LHELAKKLGLSP 228
|
....*..
gi 13487925 253 ALIALRY 259
Cdd:cd19097 229 LELALGF 235
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
7-296 |
5.33e-12 |
|
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: 65.53 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 7 TVRL-SDGHFIPILGFG------TYAPqEVPKSKATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRSKIadgtvkR 76
Cdd:cd19145 2 RVKLgSQGLEVSAQGLGcmglsgDYGA-PKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 77 EDIFYTSKVWCTFHR---------PELVRVCLEQSLKQLQLDYVDLYLIHfpmamkpgenylpkdengkLIYDAVDICDT 147
Cdd:cd19145 75 EKVQLATKFGIHEIGgsgvevrgdPAYVRAACEASLKRLDVDYIDLYYQH-------------------RIDTTVPIEIT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 148 WEAMEKCKDAGLAKSIGVSNFN----RR----------QLEKILKKpglkykpvcNQVEchpylnqGKLLDFCRSKDIVL 213
Cdd:cd19145 136 MGELKKLVEEGKIKYIGLSEASadtiRRahavhpitavQLEWSLWT---------RDIE-------EEIIPTCRELGIGI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 214 VAYSALG-----------SHREKQWVDQSSPV-----LLDNPVL----GSMAKKYNRTPALIALRYQLQRG--VVVLAKS 271
Cdd:cd19145 200 VPYSPLGrgffagkakleELLENSDVRKSHPRfqgenLEKNKVLyervEALAKKKGCTPAQLALAWVLHQGedVVPIPGT 279
|
330 340
....*....|....*....|....*
gi 13487925 272 FSEKRIKENMQVFEFQLTSEDMKVL 296
Cdd:cd19145 280 TKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-220 |
1.37e-11 |
|
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: 64.11 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTyAP-----QEVPKSKATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRskiadgTVKREDIF------- 80
Cdd:cd19163 13 VSKLGFGA-SPlggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYlatkvgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 81 YTSKVWCTF-HRPELVRVCLEQSLKQLQLDYVDLYLIHfpmamkpgenylpkD-ENGKLIyDAVdICDTWEAMEKCKDAG 158
Cdd:cd19163 86 YGLDPDKMFdFSAERITKSVEESLKRLGLDYIDIIQVH--------------DiEFAPSL-DQI-LNETLPALQKLKEEG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487925 159 LAKSIGVSNFNRRQLEKILKKPG------LKYkpvcnqveCHPYLNQ---GKLLDFCRSKDIVLVAYSALG 220
Cdd:cd19163 150 KVRFIGITGYPLDVLKEVLERSPvkidtvLSY--------CHYTLNDtslLELLPFFKEKGVGVINASPLS 212
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-219 |
3.01e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 63.12 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 42 IDAGFRHIDSASMY----------QNEKEVG--LAIRSKiadgtvkREDIFYTSKVWCTFHRP------------ELVRV 97
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGrwLKDRGN-------RDDVVIATKVGAGPRDPdggpespeglsaETIEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 98 CLEQSLKQLQLDYVDLYLIHfpmamkpgenylpkdengklIYD-AVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEK- 175
Cdd:cd19752 100 EIDKSLRRLGTDYIDLYYAH--------------------VDDrDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERa 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 176 --ILKKPGLKyKPVCNQVEcHPYL--NQG-----------KLLDFCRS-KDIVLVAYSAL 219
Cdd:cd19752 160 rqIARQQGWA-EFSAIQQR-HSYLrpRPGadfgvqrivtdELLDYASSrPDLTLLAYSPL 217
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-166 |
4.64e-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: 62.67 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 34 ATEATKIAIDAGFRHIDSASMY---QNEKEVGLAIRSKiadgtvkREDIFYTSKVWCTFHRPE----LVRVCLEQSLKQL 106
Cdd:cd19104 34 QIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVRLDPDDLGdiggQIERSVEKSLKRL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487925 107 QLDYVDLYLIH-FPMAMKPGenylPKDENGKLIYDAVDIcDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19104 107 KRDSVDLLQLHnRIGDERDK----PVGGTLSTTDVLGLG-GVADAFERLRSEGKIRFIGIT 162
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-167 |
4.71e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 62.95 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 14 HFIP-------ILGFGTYA-PQEVPKSKATEATKIAIDAGFRHIDSASMYQ----------NEKEVGLAIRSKiadgtVK 75
Cdd:PRK10625 4 HRIPhsslevsTLGLGTMTfGEQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKR-----GS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 76 REDIFYTSKVWCTFH------RPEL------VRVCLEQSLKQLQLDYVDLYLIHFPMAmkpgenylPKDENGKLIYD--- 140
Cdd:PRK10625 79 REKLIIASKVSGPSRnndkgiRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWPQR--------PTNCFGKLGYSwtd 150
|
170 180 190
....*....|....*....|....*....|
gi 13487925 141 ---AVDICDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:PRK10625 151 sapAVSLLETLDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
19-262 |
5.75e-11 |
|
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: 62.19 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFGT-YAPQEVPKSKATEATKIAIDAGFRHIDSASMYQN-------EKEVGLAIRSKIadgtvKREDIFYTSK----VW 86
Cdd:cd19082 3 IVLGTaDFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwvergasERVIGEWLKSRG-----NRDKVVIATKgghpDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 CTFHR----PELVRVCLEQSLKQLQLDYVDLYLIH-----FPMamkpgenylpkdenGKLIydavdicdtwEAMEKCKDA 157
Cdd:cd19082 78 EDMSRsrlsPEDIRADLEESLERLGTDYIDLYFLHrddpsVPV--------------GEIV----------DTLNELVRA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 158 GLAKSIGVSNFN--R-RQLEKILKKPGLkYKPVCNQV---------ECHP-----YLNQgKLLDFCRSKDIVLVAYSALG 220
Cdd:cd19082 134 GKIRAFGASNWSteRiAEANAYAKAHGL-PGFAASSPqwslarpnePPWPgptlvAMDE-EMRAWHEENQLPVFAYSSQA 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 13487925 221 ----SHREKQWVDQSSPVL--LDNPV-------LGSMAKKYNRTPALIALRYQLQ 262
Cdd:cd19082 212 rgffSKRAAGGAEDDSELRrvYYSEEnferlerAKELAEEKGVSPTQIALAYVLN 266
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-165 |
4.78e-10 |
|
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: 59.55 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 17 PILGFGTyAP-----QEVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgtvKREDIFYTSKVWCT 88
Cdd:cd19152 1 PKLGFGT-APlgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVGRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 89 F-------------------HRPEL------VRVCLEQSLKQLQLDYVDLYLIHFPmamkpgENYLPKDENGKLIYDAVD 143
Cdd:cd19152 74 LvplqeveptfepgfwnplpFDAVFdysydgILRSIEDSLQRLGLSRIDLLSIHDP------DEDLAGAESDEHFAQAIK 147
|
170 180
....*....|....*....|..
gi 13487925 144 icDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19152 148 --GAFRALEELREEGVIKAIGL 167
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
16-209 |
5.55e-09 |
|
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: 56.32 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 16 IPILGFGTYA--PQEVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgTVKREDIFYTSKV-W--- 86
Cdd:cd19142 13 VSNVGLGTWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIyWsyg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 87 ---CTFHRPELVRvCLEQSLKQLQLDYVDLYLIHFPMAMKPGE------NYLPKdeNGKLIYDAvdiCDTWEAMEkckda 157
Cdd:cd19142 89 seeRGLSRKHIIE-SVRASLRRLQLDYIDIVIIHKADPMCPMEevvramSYLID--NGLIMYWG---TSRWSPVE----- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13487925 158 glaksIGVSNFNRRQLEKILkkpglkykPVCNQVECHPylnqgklldFCRSK 209
Cdd:cd19142 158 -----IMEAFSIARQFNCPT--------PICEQSEYHM---------FCREK 187
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-266 |
2.99e-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: 54.19 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 20 GFGTYAPQEVpkskATEATKIAIDAGFRHIDSASMY-----QNEKEVGLAIRSkiaDGTVKREDIFYTSKV-WCTFHRP- 92
Cdd:cd19089 21 NFGDYTSPEE----ARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKR---DLRPYRDELVISTKAgYGMWPGPy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 93 ------ELVRVCLEQSLKQLQLDYVDLYLIHfpmamKPGENyLPKDENGKLIYDAVdicdtweamekckDAGLAKSIGVS 166
Cdd:cd19089 94 gdggsrKYLLASLDQSLKRMGLDYVDIFYHH-----RYDPD-TPLEETMTALADAV-------------RSGKALYVGIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 167 NFNRRQLEK---ILKKpgLKYKPVCNQVechPY--LNQ---GKLLDFCRSKDIVLVAYSAL--------------GSHRE 224
Cdd:cd19089 155 NYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIGFIAFSPLaqglltdkylngipPDSRR 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 13487925 225 KQWVDQSSPVLLDNPV------LGSMAKKYNRTPALIALRYQLQRGVV 266
Cdd:cd19089 230 AAESKFLTEEALTPEKleqlrkLNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
19-192 |
1.29e-07 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 52.21 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFG---TYAPQeVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRskiaDGTVKREDIFYTSKVWCTFHRP 92
Cdd:cd19143 16 LSFGswvTFGNQ-VDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKIFWGGGGP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 93 ELVRVCL---------EQSLKQLQLDYVDLYLIHFPMAMKPGEnylpkdengkliydavdicDTWEAMEKCKDAGLAKSI 163
Cdd:cd19143 91 PPNDRGLsrkhivegtKASLKRLQLDYVDLVFCHRPDPATPIE-------------------ETVRAMNDLIDQGKAFYW 151
|
170 180 190
....*....|....*....|....*....|..
gi 13487925 164 GVSNFNRRQLEK---ILKKPGLkYKPVCNQVE 192
Cdd:cd19143 152 GTSEWSAQQIEEaheIADRLGL-IPPVMEQPQ 182
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
20-285 |
3.14e-07 |
|
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: 51.00 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 20 GFGTYAPQEVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgTVKREDIFYTSKVW----CTF-HR 91
Cdd:cd19153 21 ALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVGryrdSEFdYS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 92 PELVRVCLEQSLKQLQLDYVDLYLIHfpmamkpgenylpkD-ENGKLiydAVDICDTWEAMEKCKDAGLAKSIGVSNFNR 170
Cdd:cd19153 97 AERVRASVATSLERLHTTYLDVVYLH--------------DiEFVDY---DTLVDEALPALRTLKDEGVIKRIGIAGYPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 171 RQLEKILKK--PGlkyKPVCNQVECHPYLNQGKLLD----FCRSKDIVLVAYSALG-----SHREKQWVDQSSPVLLDNP 239
Cdd:cd19153 160 DTLTRATRRcsPG---SLDAVLSYCHLTLQDARLESdapgLVRGAGPHVINASPLSmglltSQGPPPWHPASGELRHYAA 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 13487925 240 VLGSMAKKYNRTPALIALRYQLQRGVVV---LAKSFSEKRIKENMQVFE 285
Cdd:cd19153 237 AADAVCASVEASLPDLALQYSLAAHAGVgtvLLGPSSLAQLRSMLAAVD 285
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-117 |
2.51e-06 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 48.43 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 18 ILGFGTYAPQ---EVPKSKATEATKIAIDAGFRHIDSASMYQNEKEV-GLAIrSKIADGtVKREDIFYTSKV----WCTF 89
Cdd:cd19164 17 IFGAATFSYQyttDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL-KALRDE-FPRDTYFIITKVgrygPDDF 94
|
90 100
....*....|....*....|....*....
gi 13487925 90 -HRPELVRVCLEQSLKQLQLDYVDLYLIH 117
Cdd:cd19164 95 dYSPEWIRASVERSLRRLHTDYLDLVYLH 123
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
19-308 |
6.35e-06 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 47.08 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFG------TYAPqeVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgTVKREDIFYTSKvwCTF 89
Cdd:PLN02587 14 VGFGasplgsVFGP--VSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTK--CGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 90 HR------PELVRVCLEQSLKQLQLDYVDLYLIHfpmamkpgenylpKDENGKLiyDAVdICDTWEAMEKCKDAGLAKSI 163
Cdd:PLN02587 86 YGegfdfsAERVTKSVDESLARLQLDYVDILHCH-------------DIEFGSL--DQI-VNETIPALQKLKESGKVRFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 164 GVSNFNRRQLEKILKK--PG-----LKYkpvcnqveCHPYLNQGKLLD---FCRSKDIVLVAYS--ALGSHREK---QWV 228
Cdd:PLN02587 150 GITGLPLAIFTYVLDRvpPGtvdviLSY--------CHYSLNDSSLEDllpYLKSKGVGVISASplAMGLLTENgppEWH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 229 DQSSPVLLDNPVLGSMAKKYNRTPALIALRYQL--QRGVVVLAKSFSEKRIKENMQ-VFEFQLTSEDMKVLDDLN----- 300
Cdd:PLN02587 222 PAPPELKSACAAAATHCKEKGKNISKLALQYSLsnKDISTTLVGMNSVQQVEENVAaATELETSGIDEELLSEVEailap 301
|
....*....
gi 13487925 301 -KNIRYISG 308
Cdd:PLN02587 302 vKNKTWPSG 310
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
41-297 |
1.44e-05 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 46.14 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 41 AIDAGFRHIDSASMY-----QNEKEVGLAIRSKIAdgTVKREDIFYTSKVWCTFHRP-------ELVRVCLEQSLKQLQL 108
Cdd:PRK09912 52 AFDLGITHFDLANNYgpppgSAEENFGRLLREDFA--AYRDELIISTKAGYDMWPGPygsggsrKYLLASLDQSLKRMGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 109 DYVDLYLIHfpmamKPGENyLPKDENGKLIYDAVdicdtweamekckDAGLAKSIGVSNFNRRQLEKIL------KKPGL 182
Cdd:PRK09912 130 EYVDIFYSH-----RVDEN-TPMEETASALAHAV-------------QSGKALYVGISSYSPERTQKMVellrewKIPLL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 183 KYKPVCNQVecHPYLNQGKLLDFCRSKDIVLVAYSALGS-----------------HREKQWVDQSSPVLLDNPVLGS-- 243
Cdd:PRK09912 191 IHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLAQglltgkylngipqdsrmHREGNKVRGLTPKMLTEANLNSlr 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487925 244 ----MAKKYNRTPALIALRYQL--QRGVVVLAKSFSEKRIKENMQVFE-FQLTSEDMKVLD 297
Cdd:PRK09912 269 llneMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALNnLTFSTEELAQID 329
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
99-282 |
9.93e-05 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 43.55 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 99 LEQSLKQLQLDYVDLYLIHFPMAMKPGEnylpkdengkliydavdicDTWEAMEKCKDAGLAKSIGVSNFN---RRQLEK 175
Cdd:cd19151 107 LDQSLKRMGLDYVDIFYHHRPDPETPLE-------------------ETMGALDQIVRQGKALYVGISNYPpeeAREAAA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 176 ILKK---PGLKYKPVCNQVECHPylnQGKLLDFCRSKDIVLVAYSALG---------------SHREKQWV----DQSSP 233
Cdd:cd19151 168 ILKDlgtPCLIHQPKYSMFNRWV---EEGLLDVLEEEGIGCIAFSPLAqglltdrylngipedSRAAKGSSflkpEQITE 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13487925 234 VLLDN-PVLGSMAKKYNRTPALIALRYQLQRGVV--VLAKSFSEKRIKENMQ 282
Cdd:cd19151 245 EKLAKvRRLNEIAQARGQKLAQMALAWVLRNKRVtsVLIGASKPSQIEDAVG 296
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
19-152 |
1.95e-04 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 42.31 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 19 LGFGTyAP-----QEVPKSKATEATKIAIDAGFRHIDSASMYQN---EKEVGLAIRSKiadgtvKREDIFYTSKV----- 85
Cdd:cd19161 3 LGLGT-AGlgnlyTAVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREK------PRDEFVLSTKVgrllk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487925 86 ---------WCTFHRP-ELVRV----------CLEQSLKQLQLDYVDLYLIH---------------FPMAMKPGENYLP 130
Cdd:cd19161 76 paregsvpdPNGFVDPlPFEIVydysydgimrSFEDSLQRLGLNRIDILYVHdigvythgdrkerhhFAQLMSGGFKALE 155
|
170 180
....*....|....*....|....*...
gi 13487925 131 KDENGKLI------YDAVDICDtwEAME 152
Cdd:cd19161 156 ELKKAGVIkafglgVNEVQICL--EALD 181
|
|
| |
