|
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) ... |
6-306 |
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: 697.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 6 QRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKL 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 86 WCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGV 165
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 166 SNFNCRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPVLCALA 245
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083905 246 KKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYV 306
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-319 |
3.99e-176 |
|
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: 489.70 E-value: 3.99e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 13 GHFMPVLGFGTYAPPE-VPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQ 91
Cdd:cd19109 1 GNSIPIIGLGTYSEPKtTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 92 PQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCR 171
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 172 QLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPVLCALAKKHKQT 251
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 252 PALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYVVMDFLMDHPDYPF 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 |
1.90e-138 |
|
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: 394.09 E-value: 1.90e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGTY-APPevprNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQM 94
Cdd:cd19107 4 MPILGLGTWkSPP----GQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 95 VQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLE 174
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 175 MILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQrHKLWVDPNSPVLLEDPVLCALAKKHKQTPAL 254
Cdd:cd19107 160 RILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP-DRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQ 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083905 255 IALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYVVMDFLMDHPDYPFSDEY 323
Cdd:cd19107 239 VLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-307 |
1.98e-129 |
|
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: 371.33 E-value: 1.98e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 10 LNDGHFMPVLGFGTY--APPEVprNRAVEVtklAIEAGFRHIDSAYLYNNEEQVGLAIRSKI-ADGSVKREDIFYTSKLW 86
Cdd:cd19106 1 LHTGQKMPLIGLGTWksKPGQV--KAAVKY---ALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 CTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVS 166
Cdd:cd19106 76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 NFNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQrHKLWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSP-DRPWAKPDEPVLLEEPKVKALAK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083905 247 KHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYVV 307
Cdd:cd19106 233 KYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIV 293
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-306 |
7.32e-125 |
|
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: 359.29 E-value: 7.32e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 7 RVELNDGHFMPVLGFGTYAppEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWK--LKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 CTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETplpKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVS 166
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENND---SESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 NFNCRQLEMILNkpGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGtqRHKLWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19116 157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFG--RLVPRGQTNPPPRLDDPTLVAIAK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 247 KHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYV 306
Cdd:cd19116 233 KYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 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 |
1.18e-123 |
|
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: 354.48 E-value: 1.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIadgsVKREDIFYTSKLWCTFFQPQMV 95
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 96 QPALESSLKKLQLDYVDLYLLHFPMALKPGETPlpkdengkvifdtVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEM 175
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGGSK-------------EARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 176 ILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLwvdpnspvlLEDPVLCALAKKHKQTPALI 255
Cdd:cd19071 141 LLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRPL---------LDDPVLKEIAKKYGKTPAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1844083905 256 ALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLD 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 |
1.55e-122 |
|
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: 353.88 E-value: 1.55e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGTY--APPEVprnraVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQ 93
Cdd:cd19110 4 IPAVGLGTWkaSPGEV-----TEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 94 MVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQL 173
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 174 EMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLwvdpnspVLLEDPVLCALAKKHKQTPA 253
Cdd:cd19110 159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGV-------DLIDDPVIQRIAKKHGKSPA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 254 LIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYVVMDFLMDHPDYPFSDEY 323
Cdd:cd19110 232 QILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-304 |
1.13e-116 |
|
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: 339.00 E-value: 1.13e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19154 4 ITLSNGVKMPLIGLGTW---QSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPN----SPVLLEDPVLCA 243
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspAPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083905 244 LAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYR 304
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
10-306 |
9.97e-114 |
|
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: 331.30 E-value: 9.97e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 10 LNDGHFMPVLGFGTY--APPEVprNRAVevtKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19123 6 LSNGDLIPALGLGTWksKPGEV--GQAV---KQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGeTPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGT-QRHKLWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19123 160 FSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKIAE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 247 KHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYV 306
Cdd:cd19123 238 KHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-305 |
9.72e-112 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 324.70 E-value: 9.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 12 DGHFMPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWCTFFQ 91
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 92 PQMVQPALESSLKKLQLDYVDLYLLHFPMAlkpgetplpkdengkvifdtVDLSATWEVMEKCKDAGLAKSIGVSNFNCR 171
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 172 QLEMILNKPGlkYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAKKHKQT 251
Cdd:COG0656 134 HLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKT 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1844083905 252 PALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRY 305
Cdd:COG0656 201 PAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-299 |
2.05e-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: 319.68 E-value: 2.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 9 ELNDGHFMPVLGFGTY-APPEVPRNrAVEVtklAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19125 4 KLNTGAKIPAVGLGTWqADPGVVGN-AVKT---AIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGEtplPKDENGKVIfdTVDLSATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19125 80 TDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQrHKLWVDPNspvLLEDPVLCALAKK 247
Cdd:cd19125 155 FSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSP-GTTWVKKN---VLKDPIVTKVAEK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1844083905 248 HKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGL 299
Cdd:cd19125 229 LGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-299 |
8.89e-102 |
|
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: 299.95 E-value: 8.89e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 12 DGHFMPVLGFGTYAPPEVPrnravEVTKL----AIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVK-REDIFYTSKLW 86
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSP-----EDIKAavleAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 CTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENgkvIFDTVDLSATWEVMEKCKDAGLAKSIGVS 166
Cdd:cd19124 76 CSDAHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEE---DFLPFDIKGVWEAMEECQRLGLTKAIGVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 NFNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKlWvdpNSPVLLEDPVLCALAK 246
Cdd:cd19124 153 NFSCKKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK-W---GSNAVMESDVLKEIAA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1844083905 247 KHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGL 299
Cdd:cd19124 227 AKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
8-304 |
4.05e-95 |
|
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: 284.03 E-value: 4.05e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTY-APPEVPRnRAVEVtklAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWqSSPEEIE-TAVDT---ALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 CTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALK-PGETPLPKDENGKVIFD-TVDLSATWEVMEKCKDAGLAKSIG 164
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 165 VSNFNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQ-RHKLWVDPNSPV-----LLED 238
Cdd:cd19155 160 LSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPgAAHFSPGTGSPSgsspdLLQD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844083905 239 PVLCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYR 304
Cdd:cd19155 238 PVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-307 |
4.74e-93 |
|
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: 278.23 E-value: 4.74e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 13 GHFMPVLGFGTY-APPEVPRnravEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQ 91
Cdd:cd19111 1 GFPMPVIGLGTYqSPPEEVR----AAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 92 PQMVQPALESSLKKLQLDYVDLYLLHFPMALKpgetplPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCR 171
Cdd:cd19111 77 FKDTEKSLEKSLENLKLPYVDLYLIHHPCGFV------NKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 172 QLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGT-QRHKLWVDPNSPVLLEDPVLCALAKKHKQ 250
Cdd:cd19111 151 QINKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELDK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083905 251 TPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYVV 307
Cdd:cd19111 229 TPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFD 285
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
10-303 |
2.27e-92 |
|
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: 276.30 E-value: 2.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 10 LNDGHFMPVLGFGTY--APPEVprNRAVEVtklAIEAGFRHIDSAYLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWC 87
Cdd:cd19117 8 LNTGAEIPAVGLGTWqsKPNEV--AKAVEA---ALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLWC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQpqMVQPALESSLKKLQLDYVDLYLLHFPMALKP-GETPLPKDENG-KVIFDTVDLSATWEVMEKCKDAGLAKSIGV 165
Cdd:cd19117 79 TWHR--RVEEALDQSLKKLGLDYVDLYLMHWPVPLDPdGNDFLFKKDDGtKDHEPDWDFIKTWELMQKLPATGKVKAIGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 166 SNFNCRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQrhklwvdpNSPvLLEDPVLCALA 245
Cdd:cd19117 157 SNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGST--------NAP-LLKEPVIIKIA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 246 KKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEfqLTSEDMKVLDGLNRNY 303
Cdd:cd19117 228 KKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHKEY 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-305 |
3.35e-92 |
|
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: 276.26 E-value: 3.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 11 NDGHFMPVLGFGTYAP-PEVPRNraveVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTF 89
Cdd:cd19129 1 NGSGAIPALGFGTLIPdPSATRN----AVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 90 FQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDT-VDLSATWEVMEKCKDAGLAKSIGVSNF 168
Cdd:cd19129 77 HRPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 169 NCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGtqrHKLwvdpnSPVLLEDPVLCALAKKH 248
Cdd:cd19129 157 SLEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG---HGM-----EPKLLEDPVITAIARRV 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083905 249 KQTPALIALRYQLQRGVVVLAKSYNEQRIRENiqvFEFQLTSEDM--KVLDGLNRNYRY 305
Cdd:cd19129 227 NKTPAQVLLAWAIQRGTALLTTSKTPSRIREN---FDISTLPEDAmrEINEGIKTRYRF 282
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-305 |
1.03e-91 |
|
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: 275.52 E-value: 1.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTY-APPEVPRNRAVEvtklAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWrMEPGEIKELILN----AIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 CTffQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKP---GETPLPKDENGKV-IFDTVDLSATWEVMEKCKDAGLAKS 162
Cdd:cd19112 79 NS--DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLdIDVTISLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 163 IGVSNFncrqlEMILNKPGLKY---KPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALG-TQRHKLWVDPNSPvlLED 238
Cdd:cd19112 157 IGISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083905 239 PVLCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRY 305
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-305 |
6.68e-89 |
|
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: 266.79 E-value: 6.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 13 GHFMPVLGFGT----YAPPEVPRNR-AVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWC 87
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRdLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TffqPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGetplpkdengkvifdTVDLSATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19120 77 G---IKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPglKYKPVCNQVECHPYLN--QSKLLDFCKSKDIVLVAHSALGTqrhkLWVDPNSPVlleDPVLCALA 245
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSP----LTRDAGGPL---DPVLEKIA 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 246 KKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRY 305
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-299 |
1.15e-88 |
|
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: 266.97 E-value: 1.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 10 LNDGHFMPVLGFGTY--APPEVprNRAVevtKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIAD-GSVKREDIFYTSKLW 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaEPGEV--GAAV---KIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 CTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPG--ETPLP--KDENGKVIFDT-VDLSATWEVMEKCKDAGLAK 161
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTgdLNPLTavPTNGGEVDLDLsVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 162 SIGVSNFNCRQLEMILNKPGLkyKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLwvdpnsPVLLEDPVL 241
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLAGL------PLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 242 CALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEfqLTSEDMKVLDGL 299
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-300 |
1.10e-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: 260.83 E-value: 1.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYAPPEvpRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWC 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPD--GDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMAlkpgetplpkdenGKVIfdtvdlsATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19126 75 DDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGK-------------DKFI-------DTWKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGtQRHklwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19126 135 FQEHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLG-QGG----------LLSNPVLAAIGEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1844083905 248 HKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN 300
Cdd:cd19126 202 YGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-299 |
7.46e-86 |
|
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: 258.72 E-value: 7.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGTYappevpRNRAVE----VTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQ 91
Cdd:cd19136 1 MPILGLGTF------RLRGEEevrqAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 92 PQMVQPALESSLKKLQLDYVDLYLLHFPmalkpGETPLPKDENGKVIFDtvdlSATWEVMEKCKDAGLAKSIGVSNFNCR 171
Cdd:cd19136 75 YEKARAACLGSLERLGTDYLDLYLIHWP-----GVQGLKPSDPRNAELR----RESWRALEDLYKEGKLRAIGVSNYTVR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 172 QLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnsPVLLEDPVLCALAKKHKQT 251
Cdd:cd19136 146 HLEELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD---------LRLLEDPTVLAIAKKYGRT 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1844083905 252 PALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGL 299
Cdd:cd19136 215 PAQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-297 |
3.62e-85 |
|
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: 256.43 E-value: 3.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWCTFFQPQMV 95
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 96 QPALESSLKKLQLDYVDLYLLHFPMAlkpgetplpkdengkvifdTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEM 175
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNP-------------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 176 ILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGtqRHKLwvdpnspvlLEDPVLCALAKKHKQTPALI 255
Cdd:cd19073 135 ALDISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA--RGEV---------LRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1844083905 256 ALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-305 |
4.88e-85 |
|
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: 258.50 E-value: 4.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19115 5 VKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALK---PgETPLP---KDENGKVIFDTVDLSATWEVMEKCKDAGLAK 161
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdP-AVRYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 162 SIGVSNFnCRQLEMILnkpgLKY---KPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPN---SPVL 235
Cdd:cd19115 161 SIGVSNF-SAQLLMDL----LRYariRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDLPGakdTPPL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 236 LEDPVLCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRY 305
Cdd:cd19115 236 FEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-300 |
9.10e-85 |
|
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: 255.76 E-value: 9.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWC 87
Cdd:cd19131 2 ITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMalkPGEtplpkdenGKVIfdtvdlsATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PAQ--------DKYV-------ETWKALIELKKEGRVKSIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19131 137 FTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEK 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1844083905 248 HKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN 300
Cdd:cd19131 204 HGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-305 |
7.65e-84 |
|
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: 253.85 E-value: 7.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYAPPEvpRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWC 87
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEE--GSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKVWN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETplpkdengkvifdtvdlsatWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19157 76 ADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKET--------------------WKALEKLYKDGRVRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19157 136 FQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAEK 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 248 HKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRY 305
Cdd:cd19157 203 YNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
10-299 |
3.61e-83 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 252.84 E-value: 3.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 10 LNDGHFMPVLGFGTY--APPEVPrnravEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGsVKREDIFYTSKLWC 87
Cdd:cd19121 6 LNTGASIPAVGLGTWqaKAGEVK-----AAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQpqMVQPALESSLKKLQLDYVDLYLLHFPMALKP-GETPL-PKDENGKVIFD-TVDLSATWEVMEKCKDAGLAKSIG 164
Cdd:cd19121 80 TYHR--RVELCLDRSLKSLGLDYVDLYLVHWPVLLNPnGNHDLfPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 165 VSNFNCRQLEMILnkPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQrhklwvdpNSPVLLEDPVLcAL 244
Cdd:cd19121 158 VSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGST--------GSPLISDEPVV-EI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1844083905 245 AKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFqlTSEDMKVLDGL 299
Cdd:cd19121 227 AKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-299 |
4.89e-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: 251.41 E-value: 4.89e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 13 GHFMPVLGFGTYapPEVPRnRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWCTFFQP 92
Cdd:cd19140 5 GVRIPALGLGTY--PLTGE-ECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 93 QMVQPALESSLKKLQLDYVDLYLLHFPmalkpgetplPKDengkvifdtVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQ 172
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWP----------NKD---------VPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 173 LEMILNKPGLKYkpVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAKKHKQTP 252
Cdd:cd19140 139 LREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1844083905 253 ALIALRYQLQR-GVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGL 299
Cdd:cd19140 206 AQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-305 |
1.46e-82 |
|
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: 252.37 E-value: 1.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19113 3 IKLNSGYKMPSVGFGCW---KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALK--PGETPLPK-----DENgKVIFDTVDLSATWEVMEKCKDAGLA 160
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPgfycgDGD-NFVYEDVPILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 161 KSIGVSNFNCRQLEMILNkpGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQ-----RHKLWVdpNSPVL 235
Cdd:cd19113 159 KSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL--NTPTL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 236 LEDPVLCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRY 305
Cdd:cd19113 235 FEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-300 |
1.34e-81 |
|
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: 247.87 E-value: 1.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTY-APPEVPRNRAVevtKLAIEAGFRHIDSAYLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVFqIPDPEECERAV---LEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 CTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMAlkpgetplpkdengkvifdtvDLSATWEVMEKCKDAGLAKSIGVS 166
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 NFNCRQLEMILnkPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnsPVLLEDPVLCALAK 246
Cdd:cd19133 133 NFYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGR---------NNLFENPVLTEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1844083905 247 KHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN 300
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-303 |
5.21e-80 |
|
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: 245.10 E-value: 5.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYAPPEvPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPqmVQPALESSLKKLQLDYVDLYLLHFPMALK-----PGETPLPKDENGKVIF-DTVDLSATWEVMEKCKDAGLAK 161
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYaASGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 162 SIGVSNFNCRQLEMILNKpgLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKlwvdpnspvLLEDPVL 241
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPLV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083905 242 CALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVfeFQLTSEDMKVLDGLNRNY 303
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGEKY 289
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-305 |
9.75e-80 |
|
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: 243.58 E-value: 9.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYAPPEvpRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWC 87
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQD--GAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMAlkpgetplpkdenGKVIfdtvdlsATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19156 75 SDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVK-------------GKFK-------DTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKpgLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 248 HKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRY 305
Cdd:cd19156 202 YGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-301 |
4.33e-78 |
|
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: 238.71 E-value: 4.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 10 LNDGHFMPVLGFGTYAppeVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWCTF 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYP---LKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 90 FQPQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgetpLPKdeNGKVIfdtvdlsATWEVMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWP---------NPS--RDLYV-------EAWQALIEAREEGLVRSIGVSNFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 170 CRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGtqrhklwvdPNSPvLLEDPVLCALAKKHK 249
Cdd:cd19132 136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG---------RGSG-LLDEPVIKAIAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1844083905 250 QTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNR 301
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-299 |
6.37e-78 |
|
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: 239.35 E-value: 6.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQ 96
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 97 PALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMI 176
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 177 LNKpgLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGtqrhKLWVDPNSpVLLEDPVLCALAKKHKQTPALIA 256
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLG----GSYGDGNL-TFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1844083905 257 LRYQLQR---GVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGL 299
Cdd:cd19128 232 IAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-300 |
1.38e-77 |
|
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: 238.08 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYAppeVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWC 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQ---TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMalkpgetplPKDENgkvifDTVdlsATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPV---------PNDFD-----RTI---QAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPV-LLEDPVLCALAK 246
Cdd:cd19127 137 FTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGPTGPGdVLQDPTITGLAE 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1844083905 247 KHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN 300
Cdd:cd19127 215 KYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-299 |
5.68e-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: 236.45 E-value: 5.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKlaiEAGFRHIDSAYLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWC 87
Cdd:cd19135 5 VRLSNGVEMPILGLGTSHSGGYSHEAVVYALK---ECGYRHIDTAKRYGCEELLGKAIK----ESGVPREDLFLTTKLWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgETPLPKDENGKVifdtvdLSATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19135 78 SDYGYESTKQAFEASLKRLGVDYLDLYLLHWP------DCPSSGKNVKET------RAETWRALEELYDEGLCRAIGVSN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19135 146 FLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEPTVTELAKK 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1844083905 248 HKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGL 299
Cdd:cd19135 213 YQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-305 |
6.60e-75 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 232.45 E-value: 6.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 13 GHFMPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQP 92
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 93 QMVQPALESSLKKLQLDYVDLYLLHFPMALK---PGE--TPLPKD-ENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVS 166
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAEnyPFLWKDkELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 NFNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPV--LLEDPVLCAL 244
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083905 245 AKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRY 305
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-305 |
5.30e-69 |
|
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: 215.88 E-value: 5.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYAPPEVPRNRAVEVtklAIEAGFRHIDSAYLYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWC 87
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSA---ALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMAlkpgetplpkdENGKVifdtVDlsaTWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19134 76 PDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKY----VD---SWGGLMKLREEGLARSIGVSN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILNKPGlkYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19134 138 FTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAA 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 248 HKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRY 305
Cdd:cd19134 205 HGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
7-300 |
5.90e-67 |
|
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: 210.54 E-value: 5.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 7 RVELNDGHFMPVLGFGTYAPPEVPRNRAVEVtklAIEAGFRHIDSAYLYNNEEQVGLAIrskiADGSVKREDIFYTSKLW 86
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVAT---ALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 CTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPgetplpkdengkvifdtvDLSATWEVMEKCKDAGLAKSIGVS 166
Cdd:cd19130 74 NDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAG------------------NYVHTWEAMIELRAAGRTRSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 NFNCRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAK 246
Cdd:cd19130 136 NFLPPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAA 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1844083905 247 KHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN 300
Cdd:cd19130 203 AHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-299 |
7.69e-65 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 204.89 E-value: 7.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGTYA-PPEVprnrAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWCTFFQPQM 94
Cdd:cd19139 1 IPAFGLGTFRlKDDV----VIDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 95 VQPALESSLKKLQLDYVDLYLLHFPMalkpgetplPKDEngkvifdtVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLE 174
Cdd:cd19139 73 LLPSLEESLEKLRTDYVDLTLIHWPS---------PNDE--------VPVEEYIGALAEAKEQGLTRHIGVSNFTIALLD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 175 MILNKPGlKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAKKHKQTPAL 254
Cdd:cd19139 136 EAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPAQ 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1844083905 255 IALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGL 299
Cdd:cd19139 204 IALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-300 |
4.95e-64 |
|
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: 204.08 E-value: 4.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 19 LGFGTYA----PPEVPRNRAVEVTKLAIEAGFRHIDSAYLYN---NEEQVGLAIrskiADGSVKREDIFYTSKL------ 85
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 86 WCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgetplpkdengkviFDTVDLSATWEVMEKCKDAGLAKSIGV 165
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP-------------------DPDTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 166 SNFNCRQLEMILNKPglKYKPVCNQVECHPY--LNQSKLLDFCKSKDIVLVAHSALG----------------TQRHKLW 227
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGgglltgkytrdpdkgpGERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083905 228 VDPNSPVLLEDPVLCALAKKHKQTPALIALRY--QLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN 300
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
16-297 |
8.71e-64 |
|
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: 202.46 E-value: 8.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGTYA------PPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSkiadgsVKREDIFYTSKLW 86
Cdd:cd19072 4 VPVLGLGTWGigggmsKDYSDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 CTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgetplpkdeNgkvifDTVDLSATWEVMEKCKDAGLAKSIGVS 166
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP--------------N-----PSIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 NFNCRQLEMILNKPGlKYKPVCNQVECHpYLNQ---SKLLDFCKSKDIVLVAHSALgtQRHKLWVDPNSPVLLEdpvlca 243
Cdd:cd19072 139 NFSLEELEEAQSYLK-KGPIVANQVEYN-LFDReeeSGLLPYCQKNGIAIIAYSPL--EKGKLSNAKGSPLLDE------ 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1844083905 244 LAKKHKQTPALIALRYQLQR-GVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19072 209 IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-297 |
6.93e-63 |
|
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: 201.31 E-value: 6.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 10 LNDGHFMPVLGFGTYAPPEVPRNRAVEVTKlAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADG-SVKREDIFYTSKLWCT 88
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEGAKGETYAAVTK-ALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 89 FFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPK-DENGKVIFD---TVDLSATWEVMEKCKDAGLAKSIG 164
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILkdlTENPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 165 VSNFNCRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHklwVDPNSPVLLEDPVLCAL 244
Cdd:cd19122 162 VSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ---VPSTGERVSENPTLNEV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1844083905 245 AKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEfqLTSEDMKVLD 297
Cdd:cd19122 237 AEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAIN 287
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-293 |
1.87e-61 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 196.83 E-value: 1.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWC 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVW---QASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TffQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKpgetplpkdengkvifDT-VDlsaTWEVMEKCKDAGLAKSIGVS 166
Cdd:PRK11565 80 D--DHKRPREALEESLKKLQLDYVDLYLMHWPVPAI----------------DHyVE---AWKGMIELQKEGLIKSIGVC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 NFNCRQLEMILNKPGLKykPVCNQVECHPYLNQSKLldfckskdivlvaHSALGTqrHKLWVDPNSPV------LLEDPV 240
Cdd:PRK11565 139 NFQIHHLQRLIDETGVT--PVINQIELHPLMQQRQL-------------HAWNAT--HKIQTESWSPLaqggkgVFDQKV 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1844083905 241 LCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDM 293
Cdd:PRK11565 202 IRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDEL 254
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-306 |
1.07e-55 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 181.76 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGTYappEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWCTFFQPQMV 95
Cdd:PRK11172 3 IPAFGLGTF---RLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 96 QPALESSLKKLQLDYVDLYLLHFPMalkpgetplPKDEngkvifdtVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEM 175
Cdd:PRK11172 76 IPSLKESLQKLRTDYVDLTLIHWPS---------PNDE--------VSVEEFMQALLEAKKQGLTREIGISNFTIALMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 176 ILNKPGlKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPVLCALAKKHKQTPALI 255
Cdd:PRK11172 139 AIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATPAQV 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1844083905 256 ALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYV 306
Cdd:PRK11172 207 ILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLV 257
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-297 |
2.11e-52 |
|
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: 173.20 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 8 VELNDGHFMPVLGFGTYAPPEVPRNRAVEVT--KLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgsvkREDIFYT 82
Cdd:cd19138 3 VTLPDGTKVPALGQGTWYMGEDPAKRAQEIEalRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 83 SKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFpmalkPGETPLPkdengkvifDTVdlsatwEVMEKCKDAGLAKS 162
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHW-----RGGVPLA---------ETV------AAMEELKKEGKIRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 163 IGVSNFNCRQLEMILNKPGLKyKPVCNQVECHpyLNQS----KLLDFCKSKDIVLVAHSALGTQRhklwvdPNSPVLLED 238
Cdd:cd19138 136 WGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGG------LLRRGLLEN 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 239 PVLCALAKKHKQTPALIALRYQL-QRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19138 207 PTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-297 |
7.01e-44 |
|
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: 151.18 E-value: 7.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 13 GHFMPVLGFGT-----YAPPEVPRN-RAVEVTKLAIEAGFRHIDSAYLY---NNEEQVGLAIRSkiadgsVKREDIFYTS 83
Cdd:cd19137 1 GEKIPALGLGTwgiggFLTPDYSRDeEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 84 KLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgETPLPKDEngkvifdtvdlsaTWEVMEKCKDAGLAKSI 163
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP------NPNIPLEE-------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 164 GVSNFNCRQLEMILNKpgLKYKPVCNQVECHPY---LNQSKLLDFCKSKDIVLVAHSALgtqrhklwvdpNSPVLLEDPV 240
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-----------RRGLEKTNRT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 241 LCALAKKHKQTPALIALRYQLQR-GVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19137 203 LEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-297 |
2.38e-37 |
|
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: 135.05 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGT-------------YAPPEvprnrAVEVTKLAIEAGFRHIDSAYLY---NNEEQVGLAIRskiadGSVKREDIF 80
Cdd:cd19093 3 SPLGLGTwqwgdrlwwgygeYGDED-----LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 81 YTSKLWCTF--FQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGetplpkdengkvifdtvdLSATWEVMEKCKDAG 158
Cdd:cd19093 73 IATKFAPLPwrLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQ------------------IEALMDGLADAVEEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 159 LAKSIGVSNFNCRQLEMI---LNKPGlkYKPVCNQVE---CHPYLNQSKLLDFCKSKDIVLVAHSALG-----------T 221
Cdd:cd19093 135 LVRAVGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspeN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 222 QRHKLWVDPNSPVLLE--DPVLCAL---AKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVL 296
Cdd:cd19093 213 PPPGGRRRLFGRKNLEkvQPLLDALeeiAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
.
gi 1844083905 297 D 297
Cdd:cd19093 293 D 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
17-297 |
3.64e-36 |
|
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: 132.22 E-value: 3.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGT----YAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYN---NEEQVGLAIRSKiadgsvKREDIFYTSKLWCTF 89
Cdd:COG0667 14 SRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR------PRDDVVIATKVGRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 90 FQPQMVQP--------ALESSLKKLQLDYVDLYLLHFPmalkPGETPLpkDEngkvifdtvdlsaTWEVMEKCKDAGLAK 161
Cdd:COG0667 88 GPGPNGRGlsrehirrAVEASLRRLGTDYIDLYQLHRP----DPDTPI--EE-------------TLGALDELVREGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 162 SIGVSNFNCRQLEMILNKPGLKYKPVCNQVEchpY--LNQS---KLLDFCKSKDIVLVAHSAL----------------- 219
Cdd:COG0667 149 YIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAARELGVGVLAYSPLagglltgkyrrgatfpe 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 220 GTQRHKLWVDPNSPVLLEDPV--LCALAKKHKQTPALIALRYQLQRGVVVL----AKSynEQRIRENIQVFEFQLTSEDM 293
Cdd:COG0667 226 GDRAATNFVQGYLTERNLALVdaLRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENLAAADLELSAEDL 303
|
....
gi 1844083905 294 KVLD 297
Cdd:COG0667 304 AALD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-297 |
4.00e-36 |
|
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: 131.55 E-value: 4.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGT------YAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLWC 87
Cdd:cd19085 2 SRLGLGCwqfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMalkpgetplpkdengkvifDTVDLSATWEVMEKCKDAGLAKSIGVSN 167
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPS-------------------SDVPLEETMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 FNCRQLEMILnKPGlkyKPVCNQVechPY--LNQSK---LLDFCKSKDIVLVAHSAL-----------------GTQRHK 225
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQL---PYnlLWRAIeyeILPFCREHGIGVLAYSPLaqglltgkfssaedfppGDARTR 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 226 LWV---DPNSPVLLED-PVLCALAKKHKQTPALIALRYQLQRGVV--VLAKSYNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19085 209 LFRhfePGAEEETFEAlEKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLD 286
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-297 |
1.61e-34 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 127.64 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 13 GHFMPVLGFGTYA-----PPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAI---RSK--IAD--GSVKRE 77
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALkgrRDDvvIATkcGLRWDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 78 DIFYTSKLwctffQPQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgetplpkDENgkvifdtVDLSATWEVMEKCKDA 157
Cdd:cd19084 81 GKGVTKDL-----SPESIRKEVEQSLRRLQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLKKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 158 GLAKSIGVSNFNCRQLEMIlnkpgLKY-KPVCNQVechPY--LNQ---SKLLDFCKSKDIVLVAHSALGT---------- 221
Cdd:cd19084 137 GKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAQglltgkykke 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 222 ---------QRHKLWVDPNSPVLLE--DpVLCALAKKHKQTPALIALRYQLQR-GV-VVLAKSYNEQRIRENIQVFEFQL 288
Cdd:cd19084 209 ptfppddrrSRFPFFRGENFEKNLEivD-KLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWEL 287
|
....*....
gi 1844083905 289 TSEDMKVLD 297
Cdd:cd19084 288 TEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-282 |
1.07e-31 |
|
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: 118.39 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGTYA-PPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRskiadGSVKREDIFYTSKLWCTFFQ- 91
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLK-----GRGNRDDVVIATKGGHPPGGd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 92 -------PQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgetplpkDEngkvifdTVDLSATWEVMEKCKDAGLAKSIG 164
Cdd:cd06660 76 psrsrlsPEHIRRDLEESLRRLGTDYIDLYYLHRD------------DP-------STPVEETLEALNELVREGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 165 VSNFNCRQLEMILN--KPGLKYKPVCNQVE---CHPYLNQSKLLDFCKSKDIVLVAHSALGtqrhklwvdpnspvlledp 239
Cdd:cd06660 137 VSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA------------------- 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1844083905 240 vlcalakkhkQTPALIALRYQLQR--GVVVLAKSYNEQRIRENIQ 282
Cdd:cd06660 198 ----------RGPAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-304 |
8.46e-24 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 99.89 E-value: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLY-NNEEQVGLAIRSkiadgsvKREDIFYTSKLWCTFFQPQM 94
Cdd:COG1453 13 VSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKG-------PRDKVILATKLPPWVRDPED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 95 VQPALESSLKKLQLDYVDLYLLHFPMalKPGETPLPKDENGkvifdtvdlsaTWEVMEKCKDAGLAKSIGVSNFNcrQLE 174
Cdd:COG1453 86 MRKDLEESLKRLQTDYIDLYLIHGLN--TEEDLEKVLKPGG-----------ALEALEKAKAEGKIRHIGFSTHG--SLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 175 MILnkpglkykpvcNQVECHP---------YLNQS-----KLLDFCKSKDIVLVAHSALGTQRhklwvdpnspvLLEDPV 240
Cdd:COG1453 151 VIK-----------EAIDTGDfdfvqlqynYLDQDnqageEALEAAAEKGIGVIIMKPLKGGR-----------LANPPE 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 241 LCALAKKHKQTPALIALRYQLQR-GV-VVLAKSYNEQRIRENIQVFE--FQLTSEDMKVLDGLNRNYR 304
Cdd:COG1453 209 KLVELLCPPLSPAEWALRFLLSHpEVtTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERLAEELG 276
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-288 |
2.00e-23 |
|
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: 97.24 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGTY----APPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN-EEQVGLAIRSkiadgsVKREDIFYTSKLWC---- 87
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVGRlped 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 -TFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPkdengkvifdtvdlSATWEVMEKCKDAGLAKSIGVS 166
Cdd:cd19090 75 tADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP--------------GGALEALLELKEEGLIKHIGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 nfnCRQLEMIlnkpglkyKPVCNQVEC------HPY--LNQS---KLLDFCKSKDIVLVAHSALG----TQRHKLWVDPN 231
Cdd:cd19090 141 ---GGPPDLL--------RRAIETGDFdvvltaNRYtlLDQSaadELLPAAARHGVGVINASPLGmgllAGRPPERVRYT 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844083905 232 SPVLLEDPV-----LCALAKKHKQTPALIALRYQLQ----RGVVVLAKsyNEQRIRENIQVFEFQL 288
Cdd:cd19090 210 YRWLSPELLdrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNVAAAEGPL 273
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-166 |
7.18e-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: 94.86 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN-EEQVGLAIRSKiadgsvkREDIFYTSKLWCTffQPQMV 95
Cdd:cd19100 12 SRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGAR--DYEGA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083905 96 QPALESSLKKLQLDYVDLYLLHFPMalKPGETPLPKDENGkvifdtvdlsaTWEVMEKCKDAGLAKSIGVS 166
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHAVD--TEEDLDQVFGPGG-----------ALEALLEAKEEGKIRFIGIS 140
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-289 |
1.22e-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: 94.59 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 15 FMPVLGFGTYAPPEvPRNRAVEVTKLAIEAGFRHIDSAYLYN---NEEQVGLAIRSKIAD-------GSVKREDifytsK 84
Cdd:cd19088 8 AMRLTGPGIWGPPA-DREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYPDDvviatkgGLVRTGP-----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 85 LWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHfpmalkpgetplpkdengkVIFDTVDLSATWEVMEKCKDAGLAKSIG 164
Cdd:cd19088 82 WWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLH-------------------RIDPKVPFEEQLGALAELQDEGLIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 165 VSNFNCRQLEMILNKPGLkykpVCNQVECHPYLNQS-KLLDFCKSKDIVLVAHSALGTqrhklwvdpnSPVLLEDPVLCA 243
Cdd:cd19088 143 LSNVTVAQIEEARAIVRI----VSVQNRYNLANRDDeGVLDYCEAAGIAFIPWFPLGG----------GDLAQPGGLLAE 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1844083905 244 LAKKHKQTPALIALRYQLQRG--VVVLAKSYNEQRIRENIQVFEFQLT 289
Cdd:cd19088 209 VAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
34-292 |
2.06e-22 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 94.83 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 34 AVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKlwCTFFQPQMVQP------------- 97
Cdd:COG4989 33 AAALIEAALELGITTFDHADIYGGytcEALFGEALKLS----PSLREKIELQTK--CGIRLPSEARDnrvkhydtskehi 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 98 --ALESSLKKLQLDYVDLYLLHFPMALkpgetplpkdengkvifdtVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEM 175
Cdd:COG4989 107 iaSVEGSLRRLGTDYLDLLLLHRPDPL-------------------MDPEEVAEAFDELKASGKVRHFGVSNFTPSQFEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 176 iLNKpGLKYKPVCNQVECHPyLNQSKL----LDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEdpVLCALAKKHKQT 251
Cdd:COG4989 168 -LQS-ALDQPLVTNQIELSL-LHTDAFddgtLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRA--ALDELAEKYGVS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1844083905 252 PALIALRYqLQR---GVVVLAKSYNEQRIRENIQVFEFQLTSED 292
Cdd:COG4989 243 PEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
19-299 |
5.93e-22 |
|
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: 94.02 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 19 LGFGTYAP------PEVPRNRAVEVTKLAIEAGFRHIDSAYLY---NNEEQVGLAIRSKiadgsvKREDIFYTSKLWCTF 89
Cdd:cd19083 14 IGLGTNAVgghnlyPNLDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 90 F--------QPQMVQPALESSLKKLQLDYVDLYLLHFPmalkPGETplPKDEngkvifdtvdlsaTWEVMEKCKDAGLAK 161
Cdd:cd19083 88 GgdgsvlnnSPEFLRSAVEKSLKRLNTDYIDLYYIHFP----DGET--PKAE-------------AVGALQELKDEGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 162 SIGVSNFNCRQLEMiLNKPGlkykpvcnQVEC--HPY--LNQ---SKLLDFCKSKDIVLV-----AHSALGTQRHKLWVD 229
Cdd:cd19083 149 AIGVSNFSLEQLKE-ANKDG--------YVDVlqGEYnlLQReaeEDILPYCVENNISFIpyfplASGLLAGKYTKDTKF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 230 PNSPVLLEDPV---------------LCALAKKHKQTPALIALRYQLQRGVV--VLAKSYNEQRIRENIQVFEFQLTSED 292
Cdd:cd19083 220 PDNDLRNDKPLfkgerfsenldkvdkLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEE 299
|
....*..
gi 1844083905 293 MKVLDGL 299
Cdd:cd19083 300 IAFIDAL 306
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-292 |
1.59e-21 |
|
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: 92.23 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 18 VLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKlwCTFFQPQM 94
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTK--CGIRLGDD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 95 VQP---------------ALESSLKKLQLDYVDLYLLHFPMALkpgetplpkdengkvifdtVDLSATWEVMEKCKDAGL 159
Cdd:cd19092 84 PRPgrikhydtskehilaSVEGSLKRLGTDYLDLLLLHRPDPL-------------------MDPEEVAEAFDELVKSGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 160 AKSIGVSNFNCRQLEMiLNKpGLKYKPVCNQVEC---HPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLL 236
Cdd:cd19092 145 VRYFGVSNFTPSQIEL-LQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLR 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083905 237 EdpVLCALAKKHKQTPALIALRYQLQ---RGVVVLAkSYNEQRIRENIQVFEFQLTSED 292
Cdd:cd19092 223 A--ALEELAEEYGVTIEAIALAWLLRhpaRIQPILG-TTNPERIRSAVKALDIELTREE 278
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-285 |
1.73e-21 |
|
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: 91.47 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGTY-----APPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WC 87
Cdd:cd19096 1 SVLGFGTMrlpesDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 88 TFFQPQMVQPALESSLKKLQLDYVDLYLLHfpmALKPGETPLPKDENGkvifdtvdlsaTWEVMEKCKDAGLAKSIGVSn 167
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLH---GLNSPEWLEKARKGG-----------LLEFLEKAKKEGLIRHIGFS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 168 F--NCRQLEMILNkpglkykpvCNQVEC----HPYLNQ-----SKLLDFCKSKDIVLVAHSALGTQRHklwvdPNSPvll 236
Cdd:cd19096 140 FhdSPELLKEILD---------SYDFDFvqlqYNYLDQenqagRPGIEYAAKKGMGVIIMEPLKGGGL-----ANNP--- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1844083905 237 edPVLCALAKKHKQTPALIALRYQL-QRGV-VVLAKSYNEQRIRENIQVFE 285
Cdd:cd19096 203 --PEALAILCGAPLSPAEWALRFLLsHPEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-299 |
3.33e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 91.58 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 18 VLGFGTYA---------PPEVPRNRAVEVTKLAIEAGFRHIDSAYLY---NNEEQVGLAIRSKiadgsvkREDIFYTSK- 84
Cdd:cd19102 3 TIGLGTWAiggggwgggWGPQDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 85 --LW------CTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgeTPlpkdengkvifdTVDLSATWEVMEKCKD 156
Cdd:cd19102 76 glLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWP-------DP------------DEPIEEAWGALAELKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 157 AGLAKSIGVSNFNCRQLEMIL-------NKPGlkYKPVCNQVEchpylnqSKLLDFCKSKDIVLVAHSALGT-------- 221
Cdd:cd19102 137 EGKVRAIGVSNFSVDQMKRCQaihpiasLQPP--YSLLRRGIE-------AEILPFCAEHGIGVIVYSPMQSglltgkmt 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 222 -QR-HKLWVD---PNSPVLLED---------PVLCALAKKHKQTPALIALRYQLQRGVV--VLAKSYNEQRIRENIQVFE 285
Cdd:cd19102 208 pERvASLPADdwrRRSPFFQEPnlarnlalvDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAAD 287
|
330
....*....|....
gi 1844083905 286 FQLTSEDMKVLDGL 299
Cdd:cd19102 288 LRLTPEELAEIEAL 301
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-169 |
9.50e-21 |
|
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: 89.60 E-value: 9.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGTY----APPEVPRNRAVEVTKLAIEAGFRHIDSAYLY-NNEEQVGLAIRSkiadgsVKREDIFYTSKLWCTF-- 89
Cdd:cd19095 1 SVLGLGTSgigrVWGVPSEAEAARLLNTALDLGINLIDTAPAYgRSEERLGRALAG------LRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 90 ------FQPQMVQPALESSLKKLQLDYVDLYLLHFpmalkpgetPLPKDENGKVIfdtvdlsatwEVMEKCKDAGLAKSI 163
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHG---------PSDDELTGEVL----------ETLEDLKAAGKVRYI 135
|
....*.
gi 1844083905 164 GVSNFN 169
Cdd:cd19095 136 GVSGDG 141
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-297 |
2.65e-20 |
|
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: 89.59 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 11 NDGHFMPVLGFGT----------YAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgsvkRE 77
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggffGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 78 DIFYTSKlwcTFFQP------------QMVQpALESSLKKLQLDYVDLYLLHFPMALkpgeTPLpkDEngkvifdtvdls 145
Cdd:cd19091 81 DVLIATK---VRGRMgegpndvglsrhHIIR-AVEASLKRLGTDYIDLYQLHGFDAL----TPL--EE------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 146 aTWEVMEKCKDAGLAKSIGVSNFNCRQLEMIL---NKPGLKyKPVCNQVechpYLN------QSKLLDFCKSKDIVLVAH 216
Cdd:cd19091 139 -TLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVW 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 217 SAL-----------------GTQRHKLWVD--PNSPVLLEDPV--LCALAKKHKQTPALIALRYQLQR----GVVVLAKs 271
Cdd:cd19091 213 SPLaggllsgkyrrgqpapeGSRLRRTGFDfpPVDRERGYDVVdaLREIAKETGATPAQVALAWLLSRptvsSVIIGAR- 291
|
330 340
....*....|....*....|....*.
gi 1844083905 272 yNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19091 292 -NEEQLEDNLGAAGLSLTPEEIARLD 316
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-294 |
5.85e-20 |
|
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: 88.65 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 11 NDGHFMPVLGFGT------YAPPEvPRNRAVEVTKLAIEAGFRHIDSAYLY-NNEEQVGLAIrsKIADGsvKREDIFYTS 83
Cdd:cd19144 8 RNGPSVPALGFGAmglsafYGPPK-PDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWF--KQNPG--KREKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 84 KL----------WCTFFQPQMVQPALESSLKKLQLDYVDLYLLHfpmaLKPGETPLPKdengkvifdtvdlsaTWEVMEK 153
Cdd:cd19144 83 KFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH----RVDGKTPIEK---------------TVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 154 CKDAGLAKSIGVSNFNCRQLemilnKPGLKYKPVCN-QVECHPYL-----NQSKLLDFCKSKDIVLVAHSALG----TQR 223
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETL-----RRAHAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGrgflTGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 224 HKLWVD---------------PNSPVLLE--DPvLCALAKKHKQTPALIALRYQLQRG--VVVLAKSYNEQRIRENIQVF 284
Cdd:cd19144 219 IRSPDDfeegdfrrmaprfqaENFPKNLElvDK-IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGAL 297
|
330
....*....|
gi 1844083905 285 EFQLTSEDMK 294
Cdd:cd19144 298 KVKLTEEEEK 307
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-166 |
6.86e-19 |
|
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: 84.17 E-value: 6.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 13 GHFMPVLGFGTYAPPEvprnRAVEVTKLAIEAGFRHIDSAYLY---NNEEQVGLAIRSkiadgsVKREDIFYTSKLWCTF 89
Cdd:cd19105 10 GLKVSRLGFGGGGLPR----ESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALKG------LRRDKVFLATKASPRL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083905 90 FQ--PQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETplpkdeNGKVIfdtvdlsatwEVMEKCKDAGLAKSIGVS 166
Cdd:cd19105 80 DKkdKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLL------NEELL----------EALEKLKKEGKVRFIGFS 142
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-297 |
1.44e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 84.18 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 31 RNRAVEVTKLAIEAGFRHIDSAYLYNN-EEQVGLAIRSKIADGSVKREDIFYTSklWCTFFQPQMVQPA-----LESSLK 104
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDAADDVQIHTK--WVPDPGELTMTRAyveaaIDRSLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 105 KLQLDYVDLYLLHFpmalkpgetplpKDENGKVIFDTvdlsATWevMEKCKDAGLAKSIGVSNFNCRQLEMILNKPglkY 184
Cdd:cd19101 100 RLGVDRLDLVQFHW------------WDYSDPGYLDA----AKH--LAELQEEGKIRHLGLTNFDTERLREILDAG---V 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 185 KPVCNQVEcHPYLNQ---SKLLDFCKSKDIVLVAHSALG----TQRhklWVDPNSPV----------------------- 234
Cdd:cd19101 159 PIVSNQVQ-YSLLDRrpeNGMAALCEDHGIKLLAYGTLAggllSEK---YLGVPEPTgpaletrslqkyklmidewggwd 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083905 235 ----LLEdpVLCALAKKHKQTPALIALRYQLQR----GVVVLAKsyNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19101 235 lfqeLLR--TLKAIADKHGVSIANVAVRWVLDQpgvaGVIVGAR--NSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-219 |
2.77e-17 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 79.44 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 18 VLGFGTYA-----PPEVPRNRAVEVTKLAIEAGFRHIDSAYLY---NNEEQVGLAIRSKiadgsvkREDIFYTSKLWCTF 89
Cdd:cd19086 5 EIGFGTWGlggdwWGDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 90 ---------FQPQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgetPLPKDENGKVifdtvdlsatWEVMEKCKDAGLA 160
Cdd:cd19086 78 dggperpqdFSPEYIREAVEASLKRLGTDYIDLYQLHNP--------PDEVLDNDEL----------FEALEKLKQEGKI 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083905 161 KSIGVS------------NFNCRQLEMILNkpglkykpVCNQvecHPYLnqsKLLDFCKSKDIVLVAHSAL 219
Cdd:cd19086 140 RAYGVSvgdpeealaalrRGGIDVVQVIYN--------LLDQ---RPEE---ELFPLAEEHGVGVIARVPL 196
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-297 |
4.86e-17 |
|
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: 80.01 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGTYA------PPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgsvkREDIFYTSK--- 84
Cdd:cd19149 12 SVIGLGTWAigggpwWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATKcgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 85 LWCT-----FFQPQMVQ------PA-----LESSLKKLQLDYVDLYLLHFPmalkPGETPlpkdengkvifdtvdLSATW 148
Cdd:cd19149 85 RWDReggsfFFVRDGVTvyknlsPEsireeVEQSLKRLGTDYIDLYQTHWQ----DVETP---------------IEETM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 149 EVMEKCKDAGLAKSIGVSNFNCRQLEMILNkpglkykpvCNQVEchpyLNQSK-----------LLDFCKSKDIVLVAHS 217
Cdd:cd19149 146 EALEELKRQGKIRAIGASNVSVEQIKEYVK---------AGQLD----IIQEKysmldrgiekeLLPYCKKNNIAFQAYS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 218 AL-----------------GTQR--HKLWVDPNSP---VLLED--PvlcaLAKKHKQTPALIALRYQLQRG--VVVLAKS 271
Cdd:cd19149 213 PLeqglltgkitpdrefdaGDARsgIPWFSPENREkvlALLEKwkP----LCEKYGCTLAQLVIAWTLAQPgiTSALCGA 288
|
330 340
....*....|....*....|....*.
gi 1844083905 272 YNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19149 289 RKPEQAEENAKAGDIRLSAEDIATMR 314
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-285 |
8.49e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 78.72 E-value: 8.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 29 VPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVglairskIADGSVKREDIFYTSKLWCTFFQPQMVQPA----LESSLK 104
Cdd:cd19097 23 PSEKEAKKILEYALKAGINTLDTAPAYGDSEKV-------LGKFLKRLDKFKIITKLPPLKEDKKEDEAAieasVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 105 KLQLDYVDLYLLHFPMALkpgetplpkDENGKVIfdtvdlsatWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKPGLKY 184
Cdd:cd19097 96 RLKVDSLDGLLLHNPDDL---------LKHGGKL---------VEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 185 kpVcnQVECHPY---LNQSKLLDFCKSKDIVLVAHSA-----LGTQRHKL--WVDPNSPVLLEdpvLCALAKKHKQTPAL 254
Cdd:cd19097 158 --I--QLPFNILdqrFLKSGLLAKLKKKGIEIHARSVflqglLLMEPDKLpaKFAPAKPLLKK---LHELAKKLGLSPLE 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1844083905 255 IALRYQLQR----GVVVLAKSYNEqrIRENIQVFE 285
Cdd:cd19097 231 LALGFVLSLpeidKIVVGVDSLEQ--LKEIIAAFK 263
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-259 |
7.98e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 76.59 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 19 LGFGTY--APPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKIADGSVKREDIFYTSKL-WCTFFQP 92
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgYIPGDGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 93 QMVQP--------------------------------ALESSLKKLQLDYVDLYLLHFPmalkpgETPLPKDeNGKVIFD 140
Cdd:cd19099 86 EPLRPlkyleeklgrglidvadsaglrhcispayledQIERSLKRLGLDTIDLYLLHNP------EEQLLEL-GEEEFYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 141 TvdLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMIL------------------NKPGLK-----YKPVCNQVECHPYL 197
Cdd:cd19099 159 R--LEEAFEALEEAVAEGKIRYYGISTWDGFRAPPALpghlsleklvaaaeevggDNHHFKviqlpLNLLEPEALTEKNT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083905 198 NQSK---LLDFCKSKDIVLVAHSALGTQRhklwvdpnspVLLEDPVLCALAKKHKQTPALIALRY 259
Cdd:cd19099 237 VKGEalsLLEAAKELGLGVIASRPLNQGQ----------LLGELRLADLLALPGGATLAQRALQF 291
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-299 |
1.10e-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: 76.22 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 41 AIEAGFRHIDSAYLYnneeqvGLAIRSKIAdGSV----KREDIFYTSKlwctfFQPQM-------VQPALESSLKKLQLD 109
Cdd:cd19103 41 AMAAGLNLWDTAAVY------GMGASEKIL-GEFlkryPREDYIISTK-----FTPQIagqsadpVADMLEGSLARLGTD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 110 YVDLYLLHFPMALK---PGETPLPKDenGKVifdtvdlsatwevmekckdaglaKSIGVSNFN---CRQLEMILNKPGLK 183
Cdd:cd19103 109 YIDIYWIHNPADVErwtPELIPLLKS--GKV-----------------------KHVGVSNHNlaeIKRANEILAKAGVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 184 YKPVCNqvecHPYL-----NQSKLLDFCKSKDIVLVAHSAL-----------------GTQRHKLWvdpnSPVL--LED- 238
Cdd:cd19103 164 LSAVQN----HYSLlyrssEEAGILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGRAETY----NPLLpqLEEl 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083905 239 -PVLCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGL 299
Cdd:cd19103 236 tAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
34-297 |
7.70e-15 |
|
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: 73.77 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 34 AVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKIadgsvKREDIFYTSKlwctFFQPQMVQP------------A 98
Cdd:cd19079 37 SRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATK----VYFPMGDGPngrglsrkhimaE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 99 LESSLKKLQLDYVDLYLLHFPMAlkpgETPLPkdengkvifdtvdlsatwEVMEKCKD---AGLAKSIGVSNFNCRQLEM 175
Cdd:cd19079 108 VDASLKRLGTDYIDLYQIHRWDY----ETPIE------------------ETLEALHDvvkSGKVRYIGASSMYAWQFAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 176 ILN---KPGLKyKPVCNQvechPYLN------QSKLLDFCKSKDIVLVAHSAL---------GTQRHKLWVDPNSPVLLE 237
Cdd:cd19079 166 ALHlaeKNGWT-KFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLargrlarpwGDTTERRRSTTDTAKLKY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083905 238 D-------PVLCA---LAKKHKQTPALIALRYQLQRGVVV-----LAKSYneqRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19079 241 DyfteadkEIVDRveeVAKERGVSMAQVALAWLLSKPGVTapivgATKLE---HLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
17-294 |
9.97e-15 |
|
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: 73.40 E-value: 9.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGT------YAPPevPRNRAVEVTKLAIEAGFRHIDSAYLY---NNEEQVGLAIRSKiadgsvkREDIFYTSK--- 84
Cdd:cd19076 13 SALGLGCmgmsafYGPA--DEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RDEVVIATKfgi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 85 LWCTFFQ-------PQMVQPALESSLKKLQLDYVDLYLLHFPmalkPGETPlpkdengkvIFDTVdlsatwEVMEKCKDA 157
Cdd:cd19076 84 VRDPGSGfrgvdgrPEYVRAACEASLKRLGTDVIDLYYQHRV----DPNVP---------IEETV------GAMAELVEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 158 GLAKSIGVSNFNCRQ------------LEMilnkpglKYKPVCNQVECHpylnqskLLDFCKSKDIVLVAHSALGtqRHK 225
Cdd:cd19076 145 GKVRYIGLSEASADTirrahavhpitaVQS-------EYSLWTRDIEDE-------VLPTCRELGIGFVAYSPLG--RGF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 226 LWVDPNSPVLLE-------DP---------------VLCALAKKHKQTPALIALRYQLQRG--VVVLAKSYNEQRIRENI 281
Cdd:cd19076 209 LTGAIKSPEDLPeddfrrnNPrfqgenfdknlklveKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENV 288
|
330
....*....|...
gi 1844083905 282 QVFEFQLTSEDMK 294
Cdd:cd19076 289 GALDVVLTPEELA 301
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
34-297 |
1.43e-14 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 72.72 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 34 AVEVTKLAIEAGFRHIDSAYLYN---NEEQVGLAIRskiadGSVKREDIFYTSKL---W---------CTffqPQMVQPA 98
Cdd:cd19148 27 AIETIHKALDLGINLIDTAPVYGfglSEEIVGKALK-----EYGKRDRVVIATKVgleWdeggevvrnSS---PARIRKE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 99 LESSLKKLQLDYVDLYLLHFPmalkpgetplpkDEngkvifdTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEmiln 178
Cdd:cd19148 99 VEDSLRRLQTDYIDLYQVHWP------------DP-------LVPIEETAEALKELLDEGKIRAIGVSNFSPEQME---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 179 kpglKYKPVCNQVECHPYLN------QSKLLDFCKSKDIVLVAHSAL--GTQRHKLWVD-----------------PNSP 233
Cdd:cd19148 156 ----TFRKVAPLHTVQPPYNlfereiEKDVLPYARKHNIVTLAYGALcrGLLSGKMTKDtkfegddlrrtdpkfqePRFS 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083905 234 VLLEdPV--LCALAKKHKQTPAL-IALRYQLQRG--VVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19148 232 QYLA-AVeeLDKLAQERYGKSVIhLAVRWLLDQPgvSIALWGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-291 |
2.36e-14 |
|
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: 72.20 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 16 MPVLGFGT------YAPpeVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSkiadgsVKREDIF------ 80
Cdd:cd19163 13 VSKLGFGAsplggvFGP--VDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALKG------IPRDSYYlatkvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 81 -YTSKLWCTF-FQPQMVQPALESSLKKLQLDYVDLYLLHfpmalkpgetplpkDengkVIF-DTVD--LSATWEVMEKCK 155
Cdd:cd19163 85 rYGLDPDKMFdFSAERITKSVEESLKRLGLDYIDIIQVH--------------D----IEFaPSLDqiLNETLPALQKLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 156 DAGLAKSIGVSNFNCRQLEMILNKPG------LKYkpvcnqveCHPYLNQS---KLLDFCKSKDIVLVAHSALG----TQ 222
Cdd:cd19163 147 EEGKVRFIGITGYPLDVLKEVLERSPvkidtvLSY--------CHYTLNDTsllELLPFFKEKGVGVINASPLSmgllTE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 223 R-----HklwvdPNSPVLLEdpvLCALAKKHKQTP----ALIALRYQLQ--RGVVVLAKSYNEQRIRENIQVFEFQLTSE 291
Cdd:cd19163 219 RgppdwH-----PASPEIKE---ACAKAAAYCKSRgvdiSKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLDAH 290
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-297 |
3.42e-14 |
|
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: 71.86 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 42 IEAGFRHIDSAYLYNN----------EEQVGLAIRSkiadgSVKREDIFYTSKLWCTFFQ------PQMVQPALESSLKK 105
Cdd:cd19081 36 VDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKS-----RGKRDRVVIATKVGFPMGPngpglsRKHIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 106 LQLDYVDLYLLHFPmalkpgetplpkDENgkvifdtVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILN---KPGL 182
Cdd:cd19081 111 LQTDYIDLYQAHWD------------DPA-------TPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 183 KyKPVCNQ-----VECHPYlnQSKLLDFCKSKDIVLVAHSAL---------------------GTQRHKLWVDPNSPVLl 236
Cdd:cd19081 172 P-RYVSLQpeynlVDRESF--EGELLPLCREEGIGVIPYSPLaggfltgkyrseadlpgstrrGEAAKRYLNERGLRIL- 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083905 237 edPVLCALAKKHKQTPALIALRYQLQRGVV--VLAKSYNEQRIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19081 248 --DALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
40-297 |
4.08e-14 |
|
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: 71.83 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 40 LAIEAGFRHIDSAYLY-----------------------NNEEQVGLAirSKIADGSVKREDIFYTSklwcTFFQPQMVQ 96
Cdd:cd19094 26 YAFDEGVNFIDTAEMYpvppspetqgrteeiigswlkkkGNRDKVVLA--TKVAGPGEGITWPRGGG----TRLDRENIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 97 PALESSLKKLQLDYVDLYLLHFP---MALKPGETPLPKDENGkvifDTVDLSATWEVMEKCKDAGLAKSIGVSNFN---- 169
Cdd:cd19094 100 EAVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEEE----DSVSFEEQLEALGELVKAGKIRHIGLSNETpwgv 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 170 CRQLEM--ILNKPglkyKPVCNQvecHPY--LNQSKLLDF---CKSKDIVLVAHSALG--------------TQRHKLWV 228
Cdd:cd19094 176 MKFLELaeQLGLP----RIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLAggvltgkyldgaarPEGGRLNL 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083905 229 DP-------NSPVLLEDPVLCALAKKHKQTPALIALRYQLQR---GVVVLAKSYNEQrIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19094 249 FPgymaryrSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRpfvTSTIIGATTLEQ-LKENIDAFDVPLSDELLAEID 326
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
18-291 |
1.22e-13 |
|
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: 69.93 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 18 VLGFGTYAP--PEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WCTFFQ 91
Cdd:cd19074 6 ELSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 92 P--------QMVQpALESSLKKLQLDYVDLYLLHFPmalKPgETPLpkDEngkvifdtvdlsaTWEVMEKCKDAGLAKSI 163
Cdd:cd19074 80 PndrglsrkHIFE-SIHASLKRLQLDYVDIYYCHRY---DP-ETPL--EE-------------TVRAMDDLIRQGKILYW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 164 GVSNF----------NCRQLEMIlnkpglkyKPVCNQVECHpYLNQSK---LLDFCKSKDIVLVAHSAL------GTQRH 224
Cdd:cd19074 140 GTSEWsaeqiaeahdLARQFGLI--------PPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltGKYRD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 225 KLWVDPNSPVLLEDP-----------------VLCALAKKHKQTPALIALRYQLQR-GV--VVLAKSYNEQrIRENIQVF 284
Cdd:cd19074 211 GIPPPSRSRATDEDNrdkkrrlltdenlekvkKLKPIADELGLTLAQLALAWCLRNpAVssAIIGASRPEQ-LEENVKAS 289
|
....*..
gi 1844083905 285 EFQLTSE 291
Cdd:cd19074 290 GVKLSPE 296
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-299 |
1.99e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 66.91 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 34 AVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKlwCTFFQPQM------VQPALESSLK 104
Cdd:cd19104 34 QIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL-------PAGPYITTK--VRLDPDDLgdiggqIERSVEKSLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 105 KLQLDYVDLYLLH---FPMALKPGETPLPKDengkvifDTVDLSATWEVMEKCKDAGLAKSIGVSNF-NCRQLEMIL--N 178
Cdd:cd19104 105 RLKRDSVDLLQLHnriGDERDKPVGGTLSTT-------DVLGLGGVADAFERLRSEGKIRFIGITGLgNPPAIRELLdsG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 179 KPG--------LKYKPVCNQVECHPYLNQSKLLDFCKSKD-----IVLVAHSALGTQ-RHKLWVDPNSPVLLEDPV---- 240
Cdd:cd19104 178 KFDavqvyynlLNPSAAEARPRGWSAQDYGGIIDAAAEHGvgvmgIRVLAAGALTTSlDRGREAPPTSDSDVAIDFrraa 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083905 241 -LCALAKKHKQTPALIALRYQL-QRGV--VVLAKSyNEQRIRENIQVFEF-QLTSEDMKVLDGL 299
Cdd:cd19104 258 aFRALAREWGETLAQLAHRFALsNPGVstVLVGVK-NREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
18-296 |
3.15e-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: 65.92 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 18 VLGFG------TYAPPeVPRNRAVEVTKLAIEAGFRHIDSAYLY---NNEEQVGLAIRSKIadgsvkREDIFYTSKLWCT 88
Cdd:cd19145 14 AQGLGcmglsgDYGAP-KPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKFGIH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 89 FFQ---------PQMVQPALESSLKKLQLDYVDLYLLH-----FPMALKPGEtpLPK-DENGKVIFdtVDLSatwevmEK 153
Cdd:cd19145 87 EIGgsgvevrgdPAYVRAACEASLKRLDVDYIDLYYQHridttVPIEITMGE--LKKlVEEGKIKY--IGLS------EA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 154 CKDAgLAKSIGVSNFNCRQLEMILnkpglkykpVCNQVEchpylnqSKLLDFCKSKDIVLVAHSALGtqRHKLWvdpNSP 233
Cdd:cd19145 157 SADT-IRRAHAVHPITAVQLEWSL---------WTRDIE-------EEIIPTCRELGIGIVPYSPLG--RGFFA---GKA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 234 VLLEDPV-------------------------LCALAKKHKQTPALIALRYQLQRG--VVVLAKSYNEQRIRENIQVFEF 286
Cdd:cd19145 215 KLEELLEnsdvrkshprfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSV 294
|
330
....*....|
gi 1844083905 287 QLTSEDMKVL 296
Cdd:cd19145 295 KLTKEDLKEI 304
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
41-168 |
1.95e-10 |
|
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: 60.66 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 41 AIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKlwctFFQPqM-------------VQPALESSLK 104
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATK----VFGP-MgddpndrglsrrhIRRAVEASLR 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083905 105 KLQLDYVDLYLLHFPMAlkpgETPLpkDEngkvifdtvdlsaTWEVMEKCKDAGLAKSIGVSNF 168
Cdd:cd19087 107 RLQTDYIDLYQMHHFDR----DTPL--EE-------------TLRALDDLVRQGKIRYIGVSNF 151
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-297 |
2.61e-10 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 60.31 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 42 IEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLwcTFFQPQ------------MVQpALESSLKKL 106
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKY--TMNRRPgdpnaggnhrknLRR-SVEASLRRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 107 QLDYVDLYLLHFPmalkPGETPLPK-----DE---NGKVIFdtVDLSAT--WEVmekCKDAGLAKSIGVSNFNCRQLEmi 176
Cdd:cd19080 111 QTDYIDLLYVHAW----DFTTPVEEvmralDDlvrAGKVLY--VGISDTpaWVV---ARANTLAELRGWSPFVALQIE-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 177 lnkpglkYKPVCNQVEchpylnqSKLLDFCKSKDIVLVAHSALG------------TQRHKLWVDPNSPVLLEDP----- 239
Cdd:cd19080 180 -------YSLLERTPE-------RELLPMARALGLGVTPWSPLGgglltgkyqrgeEGRAGEAKGVTVGFGKLTErnwai 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083905 240 --VLCALAKKHKQTPALIALRYQLQR---GVVVLAKSYNEQrIRENIQVFEFQLTSEDMKVLD 297
Cdd:cd19080 246 vdVVAAVAEELGRSAAQVALAWVRQKpgvVIPIIGARTLEQ-LKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-297 |
2.66e-10 |
|
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: 60.32 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 19 LGFG----TYAPPEVP-RNRAVEVTKLAIEAGFRHIDSAYLY---NNEEQVGLAIRSKiadgsvkREDIFYTSKLWCTFF 90
Cdd:cd19078 7 IGLGcmgmSHGYGPPPdKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKFGFKID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 91 QPQMVQP-----------ALESSLKKLQLDYVDLYLLHFPmalkpgetplpkDENgkvifdtVDLSATWEVMEKCKDAGL 159
Cdd:cd19078 80 GGKPGPLgldsrpehirkAVEGSLKRLQTDYIDLYYQHRV------------DPN-------VPIEEVAGTMKELIKEGK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 160 AKSIGVSNFNCRQLEmilnkpglKYKPVC---------NQVECHPylnQSKLLDFCKSKDIVLVAHSALG--------TQ 222
Cdd:cd19078 141 IRHWGLSEAGVETIR--------RAHAVCpvtavqseySMMWREP---EKEVLPTLEELGIGFVPFSPLGkgfltgkiDE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 223 RHKL-------WVDPNSP-------VLLEdpVLCALAKKHKQTPALIALRYQLQRG--VVVLAKSYNEQRIRENIQVFEF 286
Cdd:cd19078 210 NTKFdegddraSLPRFTPealeanqALVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADI 287
|
330
....*....|.
gi 1844083905 287 QLTSEDMKVLD 297
Cdd:cd19078 288 ELTPEELREIE 298
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-240 |
1.45e-09 |
|
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: 58.14 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGTYA---PPEVPRNRAVEVTKLAIEAGFRHIDSAYLYN---NEEQVGLAIRSKiadgsvKREDIFYTSKLWCTFF 90
Cdd:cd19162 1 PRLGLGAASlgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALARH------PRAEYVVSTKVGRLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 91 QPQMVQPA----------------LESSLKKLQLDYVDLYLLHfpmalkpgeTPLPKDENGkvifdtvdLSATWEVMEKC 154
Cdd:cd19162 75 PGAAGRPAgadrrfdfsadgirrsIEASLERLGLDRLDLVFLH---------DPDRHLLQA--------LTDAFPALEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 155 KDAGLAKSIGVSNFNCRQLEMILNKPGLKYKPVCNQvecHPYLNQS---KLLDFCKSKDIVLVAHSALgtqrhklwvdpN 231
Cdd:cd19162 138 RAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAGR---YTLLDRRaatELLPLCAAKGVAVVAAGVF-----------N 203
|
....*....
gi 1844083905 232 SPVLLEDPV 240
Cdd:cd19162 204 SGILATDDP 212
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-167 |
2.16e-09 |
|
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: 57.56 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGT-YAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLA-------IRSKIadgsvKREDIFYTSKLWCT 88
Cdd:cd19082 1 SRIVLGTaDFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGAServigewLKSRG-----NRDKVVIATKGGHP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 89 FFQ--------PQMVQPALESSLKKLQLDYVDLYLLHfpmalkpgetplpKDENgkvifdTVDLSATWEVMEKCKDAGLA 160
Cdd:cd19082 76 DLEdmsrsrlsPEDIRADLEESLERLGTDYIDLYFLH-------------RDDP------SVPVGEIVDTLNELVRAGKI 136
|
....*..
gi 1844083905 161 KSIGVSN 167
Cdd:cd19082 137 RAFGASN 143
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
20-297 |
2.23e-09 |
|
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: 57.63 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 20 GFG----TYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVG--------LAIRSKIADG---SVKREDIFYTSK 84
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkllarfFRKYPEYADKvvlSVKGGLDPDTLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 85 LWCTffqPQMVQPALESSLKKL-QLDYVDLYllhfpmalkpgeTPLPKDENgkvifdtVDLSATWEVMEKCKDAGLAKSI 163
Cdd:cd19077 89 PDGS---PEAVRKSIENILRALgGTKKIDIF------------EPARVDPN-------VPIEETIKALKELVKEGKIRGI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 164 GVSNFNCRQLEMILnkpglKYKPV-CNQVECHPYLN---QSKLLDFCKSKDIVLVAHSALG----TQRHK-LWVDPNSPV 234
Cdd:cd19077 147 GLSEVSAETIRRAH-----AVHPIaAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGrgllTGRIKsLADIPEGDF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 235 LLEDP---------------VLCALAKKHKQTPALIAL---RYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVL 296
Cdd:cd19077 222 RRHLDrfngenfeknlklvdALQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDEELKEI 301
|
.
gi 1844083905 297 D 297
Cdd:cd19077 302 N 302
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
40-305 |
2.72e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 57.56 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 40 LAIEAGFRHIDSAYLYN----------NEEQVG-----------LAIRSKIAdGSVKREDifytsklwcTFFQPQM---- 94
Cdd:PRK10625 38 YAVAQGINLIDVAEMYPvpprpetqglTETYIGnwlakrgsrekLIIASKVS-GPSRNND---------KGIRPNQaldr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 95 --VQPALESSLKKLQLDYVDLYLLHFPMAlkpgetplPKDENGKVIFD------TVDLSATWEVMEKCKDAGLAKSIGVS 166
Cdd:PRK10625 108 knIREALHDSLKRLQTDYLDLYQVHWPQR--------PTNCFGKLGYSwtdsapAVSLLETLDALAEQQRAGKIRYIGVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 167 N---FNCRQLEMILNKPGLKyKPVCNQvecHPY--LNQS---KLLDFCKSKDIVLVAHSAL--GT--------------- 221
Cdd:PRK10625 180 NetaFGVMRYLHLAEKHDLP-RIVTIQ---NPYslLNRSfevGLAEVSQYEGVELLAYSCLafGTltgkylngakpagar 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 222 ----QRHKLWVDPNSPVLLEDPVlcALAKKHKQTPALIALRYQLQRGVV---VLAKSYNEQrIRENIQVFEFQLTSEDMK 294
Cdd:PRK10625 256 ntlfSRFTRYSGEQTQKAVAAYV--DIAKRHGLDPAQMALAFVRRQPFVastLLGATTMEQ-LKTNIESLHLTLSEEVLA 332
|
330
....*....|.
gi 1844083905 295 VLDGLNRNYRY 305
Cdd:PRK10625 333 EIEAVHQVYTY 343
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-220 |
3.42e-09 |
|
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: 56.80 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 18 VLG---FGTYAPPEVPRNRAvEVTKLAIEAGFRHIDSAYLYNN---EEQVGLA--------IRSKIADGSVKRedifyts 83
Cdd:cd19075 4 ILGtmtFGSQGRFTTAEAAA-ELLDAFLERGHTEIDTARVYPDgtsEELLGELglgergfkIDTKANPGVGGG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 84 klwctfFQPQMVQPALESSLKKLQLDYVDLYLLHFPmalkpgetplpkDEngkvifdTVDLSATWEVMEKCKDAGLAKSI 163
Cdd:cd19075 76 ------LSPENVRKQLETSLKRLKVDKVDVFYLHAP------------DR-------STPLEETLAAIDELYKEGKFKEF 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083905 164 GVSNFNCRQLEMILN--------KP----GLkYKPVCNQVEchpylnqSKLLDFCKSKDIVLVAHSALG 220
Cdd:cd19075 131 GLSNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLA 191
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-266 |
2.81e-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: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 20 GFGTYAPPEVprnrAVEVTKLAIEAGFRHIDsayLYNN--------EEQVGLAIRSkiaDGSVKREDIFYTSKLWCTFFQ 91
Cdd:cd19089 21 NFGDYTSPEE----ARELLRTAFDLGITHFD---LANNygpppgsaEENFGRILKR---DLRPYRDELVISTKAGYGMWP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 92 P--------QMVQPALESSLKKLQLDYVDLYLLHFPmalKPgETPLPkdengkvifdtvdlsatwEVMEKCKDA---GLA 160
Cdd:cd19089 91 GpygdggsrKYLLASLDQSLKRMGLDYVDIFYHHRY---DP-DTPLE------------------ETMTALADAvrsGKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 161 KSIGVSNFNCRQLEM---ILNKpgLKYKPVCNQVechPY--LNQS---KLLDFCKSKDIVLVAHSALG----TQRHKLWV 228
Cdd:cd19089 149 LYVGISNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRWaedGLLEVLEEAGIGFIAFSPLAqgllTDKYLNGI 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1844083905 229 DPNSPVLLEDP----------------VLCALAKKHKQTPALIALRYQLQRGVV 266
Cdd:cd19089 224 PPDSRRAAESKflteealtpekleqlrKLNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
19-285 |
2.82e-08 |
|
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: 54.08 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 19 LGFGTYA-------PPEVprNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKLW-- 86
Cdd:cd19153 15 VGLGTAAlggvygdGLEQ--DEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVGry 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 --CTF-FQPQMVQPALESSLKKLQLDYVDLYLLHfpmalkpgetplpkD-ENGKviFDTvDLSATWEVMEKCKDAGLAKS 162
Cdd:cd19153 89 rdSEFdYSAERVRASVATSLERLHTTYLDVVYLH--------------DiEFVD--YDT-LVDEALPALRTLKDEGVIKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 163 IGVSNFNCRQLEMILNK--PGlkyKPVCNQVECHPYLNQSKLLD---FCKSKDIVLVAHSA------LGTQRHKLWvDPN 231
Cdd:cd19153 152 IGIAGYPLDTLTRATRRcsPG---SLDAVLSYCHLTLQDARLESdapGLVRGAGPHVINASplsmglLTSQGPPPW-HPA 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083905 232 SPVLLEdpvLCALAKKHKQTP----ALIALRYQL----QRGVVVLAKSYNEQrIRENIQVFE 285
Cdd:cd19153 228 SGELRH---YAAAADAVCASVeaslPDLALQYSLaahaGVGTVLLGPSSLAQ-LRSMLAAVD 285
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
18-297 |
4.89e-08 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 53.63 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 18 VLGFGtyAPP------EVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKlwCT 88
Cdd:PLN02587 13 SVGFG--ASPlgsvfgPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTK--CG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 89 -----F-FQPQMVQPALESSLKKLQLDYVDLYLLHfpmalkpgetplpkdengKVIFDTVD--LSATWEVMEKCKDAGLA 160
Cdd:PLN02587 85 rygegFdFSAERVTKSVDESLARLQLDYVDILHCH------------------DIEFGSLDqiVNETIPALQKLKESGKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 161 KSIGVSNFNCRQLEMILNK--PG-----LKYkpvcnqveCHPYLNQSKLLD---FCKSKDIVLVAHSALG----TQRHKL 226
Cdd:PLN02587 147 RFIGITGLPLAIFTYVLDRvpPGtvdviLSY--------CHYSLNDSSLEDllpYLKSKGVGVISASPLAmgllTENGPP 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083905 227 WVDPNSPVLLEdpvLCALAKKH----KQTPALIALRYQL--QRGVVVLAKSYNEQRIRENIQ-VFEFQLTSEDMKVLD 297
Cdd:PLN02587 219 EWHPAPPELKS---ACAAAATHckekGKNISKLALQYSLsnKDISTTLVGMNSVQQVEENVAaATELETSGIDEELLS 293
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-192 |
9.67e-08 |
|
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: 52.60 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 18 VLGFG---TYAPpEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRskiaDGSVKREDIFYTSKLwctFFQ 91
Cdd:cd19143 15 ALSFGswvTFGN-QVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKI---FWG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 92 PQMVQP------------ALESSLKKLQLDYVDLYLLHFPMAlkpgETPlpkdengkvIFDTVdlsatwEVMEKCKDAGL 159
Cdd:cd19143 87 GGGPPPndrglsrkhiveGTKASLKRLQLDYVDLVFCHRPDP----ATP---------IEETV------RAMNDLIDQGK 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 1844083905 160 AKSIGVSNFNCRQLE---MILNKPGLkYKPVCNQVE 192
Cdd:cd19143 148 AFYWGTSEWSAQQIEeahEIADRLGL-IPPVMEQPQ 182
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-282 |
4.48e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 50.41 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 42 IEAGFRHIDSAYLYN----------NEEQVG--LAIRSKiadgsvkREDIFYTSKL---------WCTFFQ---PQMVQP 97
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGrwLKDRGN-------RDDVVIATKVgagprdpdgGPESPEglsAETIEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 98 ALESSLKKLQLDYVDLYLLHfpmalkpgetplpkdengkVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEM-- 175
Cdd:cd19752 100 EIDKSLRRLGTDYIDLYYAH-------------------VDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERar 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 176 -ILNKPGLKyKPVCNQVEcHPYL---------NQS----KLLDFCKS-KDIVLVAHSAL--------GTQRHKLWVDPNS 232
Cdd:cd19752 161 qIARQQGWA-EFSAIQQR-HSYLrprpgadfgVQRivtdELLDYASSrPDLTLLAYSPLlsgaytrpDRPLPEQYDGPDS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1844083905 233 PVLLEdpVLCALAKKHKQTPALIALRYQLQR--GVV-VLAKSYNEQrIRENIQ 282
Cdd:cd19752 239 DARLA--VLEEVAGELGATPNQVVLAWLLHRtpAIIpLLGASTVEQ-LEENLA 288
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-165 |
1.72e-06 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 48.76 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGT------YAPpeVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgsvKREDIFYTSKL-W 86
Cdd:cd19152 1 PKLGFGTaplgnlYEA--VSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 87 ctFFQPQMVQPA--------------------------LESSLKKLQLDYVDLYLLHFPmalkpgETPLPKDENgKVIFD 140
Cdd:cd19152 73 --LLVPLQEVEPtfepgfwnplpfdavfdysydgilrsIEDSLQRLGLSRIDLLSIHDP------DEDLAGAES-DEHFA 143
|
170 180
....*....|....*....|....*
gi 1844083905 141 TVDLSAtWEVMEKCKDAGLAKSIGV 165
Cdd:cd19152 144 QAIKGA-FRALEELREEGVIKAIGL 167
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-166 |
2.41e-05 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 45.35 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 18 VLGFGTYAP---PEVPRNRAVEVTKLAIEAGFRHID-SAYLYNNEEQVGLAIrSKIADgSVKREDIFYTSKL----WCTF 89
Cdd:cd19164 17 IFGAATFSYqytTDPESIPPVDIVRRALELGIRAFDtSPYYGPSEIILGRAL-KALRD-EFPRDTYFIITKVgrygPDDF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 90 -FQPQMVQPALESSLKKLQLDYVDLYLLHfpmalkpgetplpkdengKVIFDTVDlsatwEVME------KCKDAGLAKS 162
Cdd:cd19164 95 dYSPEWIRASVERSLRRLHTDYLDLVYLH------------------DVEFVADE-----EVLEalkelfKLKDEGKIRN 151
|
....
gi 1844083905 163 IGVS 166
Cdd:cd19164 152 VGIS 155
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
17-209 |
5.26e-05 |
|
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: 44.38 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGTYA--PPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKL-WCTF- 89
Cdd:cd19142 14 SNVGLGTWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIyWSYGs 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 90 ----FQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGEtplpkdengkvifdtvdlsatwEV---MEKCKDAGLAKS 162
Cdd:cd19142 90 eergLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPME----------------------EVvraMSYLIDNGLIMY 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083905 163 IGVSNF----------NCRQLEMILnkpglkykPVCNQVECHPylnqsklldFCKSK 209
Cdd:cd19142 148 WGTSRWspveimeafsIARQFNCPT--------PICEQSEYHM---------FCREK 187
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
17-285 |
1.07e-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: 43.47 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 17 PVLGFGT------YAPpeVPRNRAVEVTKLAIEAGFRHIDSAYLYNN---EEQVGLAIRSKIADG---SVKREDIFYTSK 84
Cdd:cd19161 1 SELGLGTaglgnlYTA--VSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREKPRDEfvlSTKVGRLLKPAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 85 LWCTFFQPQMVQP----------------ALESSLKKLQLDYVDLYLLHFPMALKPGetplpkDENGKVIFDTVdLSATW 148
Cdd:cd19161 79 EGSVPDPNGFVDPlpfeivydysydgimrSFEDSLQRLGLNRIDILYVHDIGVYTHG------DRKERHHFAQL-MSGGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 149 EVMEKCKDAGLAKSIGVsnfncrqlemilnkpGLKYKPVCNQ------VEC------HPYLNQS---KLLDFCKSKDIVL 213
Cdd:cd19161 152 KALEELKKAGVIKAFGL---------------GVNEVQICLEaldeadLDCfllagrYSLLDQSaeeEFLPRCEQRGTSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083905 214 VA----HSAL-----GTQRHKLWVDPNSPVLLEDPVLCALAKKHKQTPALIALRYQLQRGVV--VLAKSYNEQRIRENIQ 282
Cdd:cd19161 217 VIggvfNSGIlatgtKSGAKFNYGDAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVasVLTGARNPAQLRQNVE 296
|
...
gi 1844083905 283 VFE 285
Cdd:cd19161 297 AFQ 299
|
|
| |
