|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-308 |
0e+00 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 710.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 6 QCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKL 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 86 WCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGV 165
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 166 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALA 245
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453543 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTL 308
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-319 |
0e+00 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 505.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 13 GHFMPVLGFGTYA-PAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSHR 91
Cdd:cd19109 1 GNSIPIIGLGTYSePKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 92 PELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 172 QLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALAKKHKRT 251
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 252 PALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPF 319
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-305 |
2.25e-138 |
|
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: 394.06 E-value: 2.25e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 10 LNDGHFMPVLGFGTY--APAEVPkskalEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKI-ADGSVKREDIFYTSKLW 86
Cdd:cd19106 1 LHTGQKMPLIGLGTWksKPGQVK-----AAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19106 76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNRRQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShREEPWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGS-PDRPWAKPDEPVLLEEPKVKALAK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 5453543 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19106 233 KYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-323 |
1.31e-137 |
|
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: 392.17 E-value: 1.31e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELV 95
Cdd:cd19107 4 MPILGLGTW---KSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 96 RPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEM 175
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 176 ILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShREEPWVDPNSPVLLEDPVLCALAKKHKRTPALI 255
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGS-PDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 256 ALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY 323
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-305 |
1.03e-131 |
|
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: 376.62 E-value: 1.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 7 CVKLNDGHFMPVLGFGTYApaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWK--LKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKpgeEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFK---ENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNRRQLEMILNkpGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPwvDPNSPVLLEDPVLCALAK 246
Cdd:cd19116 157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRG--QTNPPPRLDDPTLVAIAK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 5453543 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19116 233 KYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-297 |
1.52e-125 |
|
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: 359.10 E-value: 1.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIadgsVKREDIFYTSKLWCNSHRPELV 95
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 96 RPALERSLKNLQLDYVDLYLIHFPVSVKPGEevipkdengkilfDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEM 175
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGG-------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 176 ILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREepwvdpnspVLLEDPVLCALAKKHKRTPALI 255
Cdd:cd19071 141 LLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR---------PLLDDPVLKEIAKKYGKTPAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 5453543 256 ALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 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 |
7.87e-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: 351.95 E-value: 7.87e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTY--APAEVPkskalEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSHRPE 93
Cdd:cd19110 4 IPAVGLGTWkaSPGEVT-----EAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 94 LVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQL 173
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 174 EMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEpwVDpnspvLLEDPVLCALAKKHKRTPA 253
Cdd:cd19110 159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEG--VD-----LIDDPVIQRIAKKHGKSPA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 254 LIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY 323
Cdd:cd19110 232 QILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-305 |
4.07e-119 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 343.19 E-value: 4.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 12 DGHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWCNSHR 91
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 92 PELVRPALERSLKNLQLDYVDLYLIHFPVSVkpgeevipkdengkilfdtvDLCATWEAVEKCKDAGLAKSIGVSNFNRR 171
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGPG--------------------PYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 172 QLEMILNKPGlkYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRT 251
Cdd:COG0656 134 HLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKT 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5453543 252 PALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:COG0656 201 PAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-306 |
1.18e-117 |
|
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: 340.93 E-value: 1.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYAPAevpKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSK---PGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGeEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSN 167
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 168 FNRRQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-HREEPWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19123 160 FSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKIAE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYL 306
Cdd:cd19123 238 KHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
7-304 |
3.75e-117 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 340.16 E-value: 3.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 7 CVKLNDGHFMPVLGFGTY--APAEVpkskaLEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSK 84
Cdd:cd19154 3 SITLSNGVKMPLIGLGTWqsKGAEG-----ITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 LWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIG 164
Cdd:cd19154 78 LWTHEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 165 VSNFNRRQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-----HREEPWVDPnSPVLLEDP 239
Cdd:cd19154 158 VSNFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranFTKSTGVSP-APNLLQDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5453543 240 VLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVR 304
Cdd:cd19154 235 IVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
6-299 |
9.04e-113 |
|
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: 328.15 E-value: 9.04e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 6 QCVKLNDGHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKL 85
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTW---QADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 86 WCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEeviPKDENGKILfdTVDLCATWEAVEKCKDAGLAKSIGV 165
Cdd:cd19125 78 WCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 166 SNFNRRQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShREEPWVDPNspvLLEDPVLCALA 245
Cdd:cd19125 153 SNFSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGS-PGTTWVKKN---VLKDPIVTKVA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5453543 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19125 227 EKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-299 |
4.97e-106 |
|
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: 311.12 E-value: 4.97e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 12 DGHFMPVLGFGTYAPAEVPKsKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVK-REDIFYTSKLWCNSH 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE-DIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 91 RPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENgkiLFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNR 170
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEE---DFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 171 RQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReEPWvdpNSPVLLEDPVLCALAKKHKR 250
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPG-TKW---GSNAVMESDVLKEIAAAKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 5453543 251 TPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
7-304 |
1.13e-100 |
|
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: 298.29 E-value: 1.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 7 CVKLNDGHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTW---QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV-SVKPGEEVIPKDENGKILFD-TVDLCATWEAVEKCKDAGLAKSIG 164
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVgSLSKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 165 VSNFNRRQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS----HREEPWVDP--NSPVLLED 238
Cdd:cd19155 160 LSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaaHFSPGTGSPsgSSPDLLQD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453543 239 PVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVR 304
Cdd:cd19155 238 PVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-305 |
7.35e-98 |
|
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: 290.55 E-value: 7.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 13 GHFMPVLGFGTY--APAEVpkskaLEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSH 90
Cdd:cd19111 1 GFPMPVIGLGTYqsPPEEV-----RAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 91 RPELVRPALERSLKNLQLDYVDLYLIHFPVSVkpgeeVIPKDENGKILFDTvDLCATWEAVEKCKDAGLAKSIGVSNFNR 170
Cdd:cd19111 76 EFKDTEKSLEKSLENLKLPYVDLYLIHHPCGF-----VNKKDKGERELASS-DVTSVWRAMEALVSEGKVKSIGLSNFNP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 171 RQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-HREEPWVDPNSPVLLEDPVLCALAKKHK 249
Cdd:cd19111 150 RQINKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELD 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 5453543 250 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19111 228 KTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-299 |
2.93e-96 |
|
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: 286.23 E-value: 2.93e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 10 LNDGHFMPVLGFGTY--APAEVPKskaleATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIAD-GSVKREDIFYTSKLW 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaEPGEVGA-----AVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPK----DENGKILFDT-VDLCATWEAVEKCKDAGLAK 161
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavpTNGGEVDLDLsVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 162 SIGVSNFNRRQLEMILNKPGLkyKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREepwvdpNSPVLLEDPVL 241
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLA------GLPLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTSEEMKAIDGL 299
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-305 |
2.60e-93 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 278.96 E-value: 2.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 11 NDGHFMPVLGFGTYAPaevPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSH 90
Cdd:cd19129 1 NGSGAIPALGFGTLIP---DPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 91 RPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDT-VDLCATWEAVEKCKDAGLAKSIGVSNFN 169
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 170 RRQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGsHREEpwvdpnsPVLLEDPVLCALAKKHK 249
Cdd:cd19129 158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG-HGME-------PKLLEDPVITAIARRVN 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 5453543 250 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVfeFQLTSEEMKAI-DGLNRNVRY 305
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREInEGIKTRYRF 282
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-301 |
5.92e-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: 275.15 E-value: 5.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 9 KLNDGHFMPVLGFGTYAPAEVPKSKALEAtklAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWCN 88
Cdd:cd19117 7 KLNTGAEIPAVGLGTWQSKPNEVAKAVEA---ALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLWCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 89 SHRPelVRPALERSLKNLQLDYVDLYLIHFPVSVKP-GEEVIPKDENG-KILFDTVDLCATWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19117 80 WHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPdGNDFLFKKDDGtKDHEPDWDFIKTWELMQKLPATGKVKAIGVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNRRQLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShreepwvdPNSPvLLEDPVLCALAK 246
Cdd:cd19117 158 NFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS--------TNAP-LLKEPVIIKIAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5453543 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTSEEMKAIDGLNR 301
Cdd:cd19117 229 KHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHK 281
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-297 |
8.73e-92 |
|
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: 274.11 E-value: 8.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 13 GHFMPVLGFGT----YAPAEVPKSKAL-EATKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWC 87
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLvDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPelvRPALERSLKNLQLDYVDLYLIHFPVSVKPGeevipkdengkilfdTVDLCATWEAVEKCKDAGLAKSIGVSN 167
Cdd:cd19120 77 GIKDP---REALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 168 FNRRQLEMILNKPglKYKPVCNQVECHPYFN--QRKLLDFCKSKDIVLVAYSALGSHreepWVDPNSPVlleDPVLCALA 245
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPL----TRDAGGPL---DPVLEKIA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 5453543 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-297 |
1.02e-91 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 272.99 E-value: 1.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWCNSHRPELV 95
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 96 RPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAVEKCKDAGLAKSIGVSNFNRRQLEM 175
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEE-------------------TLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 176 ILNKPGLkyKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGsHREepwvdpnspvLLEDPVLCALAKKHKRTPALI 255
Cdd:cd19073 135 ALDISPL--PIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA-RGE----------VLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 5453543 256 ALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-300 |
1.69e-91 |
|
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: 273.09 E-value: 1.69e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWC 87
Cdd:cd19131 2 ITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVsvkPGEevipkdenGKIlfdtVDlcaTWEAVEKCKDAGLAKSIGVSN 167
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PAQ--------DKY----VE---TWKALIELKKEGRVKSIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 168 FNRRQLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19131 137 FTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEK 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 5453543 248 HKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 300
Cdd:cd19131 204 HGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-305 |
5.55e-90 |
|
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: 271.28 E-value: 5.55e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTY-APAEVPKSKALEAtklaIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWrMEPGEIKELILNA----IKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHrpELVRPALERSLKNLQLDYVDLYLIHFPVSVKP---GEEVIPKDENGKILFD-TVDLCATWEAVEKCKDAGLAKS 162
Cdd:cd19112 79 NSDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLDIDvTISLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 163 IGVSNFnrrqlEMILNKPGLKY---KPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALG-SHREEPWVDPNSPvlLED 238
Cdd:cd19112 157 IGISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5453543 239 PVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-300 |
1.65e-89 |
|
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: 268.15 E-value: 1.65e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYapaEVPK-SKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSkiadGSVKREDIFYTSKLW 86
Cdd:cd19126 1 VTLNNGTRMPWLGLGVF---QTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgeevipkdenGKILfdtvdlcATWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGK-------------DKFI-------DTWKALEKLYASGKVKAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNRRQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAK 246
Cdd:cd19126 134 NFQEHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGE 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5453543 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 300
Cdd:cd19126 201 KYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-317 |
2.46e-89 |
|
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: 269.68 E-value: 2.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19115 5 VKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK---PGEEVIP--KDENGKILFDTVDLCATWEAVEKCKDAGLAKS 162
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 163 IGVSNFNrRQLEMILnkpgLKY---KPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALG--SHREEPWVDP-NSPVLL 236
Cdd:cd19115 162 IGVSNFS-AQLLMDL----LRYariRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqSFLELDLPGAkDTPPLF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 237 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRyltldiFAGPPN 316
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR------FNNPLN 310
|
.
gi 5453543 317 Y 317
Cdd:cd19115 311 Y 311
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-305 |
2.31e-88 |
|
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: 265.41 E-value: 2.31e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 7 CVKLNDGHFMPVLGFGTYapaEVPK-SKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKL 85
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVF---KVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 86 WCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEevipkdengkilfdtvdlcaTWEAVEKCKDAGLAKSIGV 165
Cdd:cd19157 74 WNADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKE--------------------TWKALEKLYKDGRVRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 166 SNFNRRQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALA 245
Cdd:cd19157 134 SNFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIA 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19157 201 EKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-305 |
3.21e-88 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 266.62 E-value: 3.21e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19113 3 IKLNSGYKMPSVGFGCW---KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK--PGEEVIPK-----DENgKILFDTVDLCATWEAVEKCKDAGLA 160
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPgfycgDGD-NFVYEDVPILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 161 KSIGVSNFNRRQLEMILNkpGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHR----EEPWVdPNSPVLL 236
Cdd:cd19113 159 KSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSfvelNQGRA-LNTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5453543 237 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-299 |
7.01e-88 |
|
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: 264.11 E-value: 7.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTY---APAEVpkSKALEAtklAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSHRP 92
Cdd:cd19136 1 MPILGLGTFrlrGEEEV--RQAVDA---ALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 93 ELVRPALERSLKNLQLDYVDLYLIHFP-VSVKPgeeviPKDENGKILfdtvdLCATWEAVEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19136 76 EKARAACLGSLERLGTDYLDLYLIHWPgVQGLK-----PSDPRNAEL-----RRESWRALEDLYKEGKLRAIGVSNYTVR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 172 QLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShreepwvdpNSPVLLEDPVLCALAKKHKRT 251
Cdd:cd19136 146 HLEELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS---------GDLRLLEDPTVLAIAKKYGRT 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 5453543 252 PALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19136 215 PAQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-300 |
9.92e-87 |
|
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: 260.97 E-value: 9.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYapaEVP-KSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPdPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgeevipkdengkilfdtvDLCATWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNRRQLEMILnkPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEpwvdpnspvLLEDPVLCALAK 246
Cdd:cd19133 133 NFYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN---------LFENPVLTEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5453543 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 300
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-301 |
6.37e-86 |
|
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: 258.74 E-value: 6.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 10 LNDGHFMPVLGFGTYApaeVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWCNS 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYP---LKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 90 HRPELVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeeviPKdeNGKILfdtvdlcATWEAVEKCKDAGLAKSIGVSNFN 169
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWPN---------PS--RDLYV-------EAWQALIEAREEGLVRSIGVSNFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 170 RRQLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREepwvdpnspvLLEDPVLCALAKKHK 249
Cdd:cd19132 136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG----------LLDEPVIKAIAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 5453543 250 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNR 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 |
3.83e-84 |
|
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: 255.14 E-value: 3.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELVR 96
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 97 PALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMI 176
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 177 LNKpgLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPwvdpnSPVLLEDPVLCALAKKHKRTPALIA 256
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDG-----NLTFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 5453543 257 LRYQLQR---GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19128 232 IAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-299 |
2.63e-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: 252.18 E-value: 2.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 13 GHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWCNSHRP 92
Cdd:cd19140 5 GVRIPALGLGTY---PLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 93 ELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeeviPKDengkilfdtVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWP----------NKD---------VPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 173 LEMILNKPGLKYkpVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTP 252
Cdd:cd19140 139 LREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 5453543 253 ALIALRYQLQR-GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19140 206 AQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-299 |
8.69e-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: 251.68 E-value: 8.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 9 KLNDGHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGsVKREDIFYTSKLWCN 88
Cdd:cd19121 5 KLNTGASIPAVGLGTW---QAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 89 SH-RPELvrpALERSLKNLQLDYVDLYLIHFPVSVKP--GEEVIPKDENGKILFD-TVDLCATWEAVEKCKDAGLAKSIG 164
Cdd:cd19121 81 YHrRVEL---CLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 165 VSNFNRRQLEMILnkPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShreepwvdPNSPVLLEDPVLcAL 244
Cdd:cd19121 158 VSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS--------TGSPLISDEPVV-EI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5453543 245 AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFqlTSEEMKAIDGL 299
Cdd:cd19121 227 AKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-305 |
1.62e-82 |
|
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: 250.51 E-value: 1.62e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYapaEVPK-SKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKiadgSVKREDIFYTSKLW 86
Cdd:cd19156 1 VKLANGVEMPRLGLGVW---RVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPgeevipKDengkilfdtvdlcaTWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19156 74 NSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKF------KD--------------TWKAFEKLYKEKKVRAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNRRQLEMILNKpgLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAK 246
Cdd:cd19156 134 NFHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGK 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 5453543 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19156 201 KYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-300 |
2.56e-82 |
|
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: 250.02 E-value: 2.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYApaeVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWC 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQ---TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeevipkdengKILFDtvDLCATWEAVEKCKDAGLAKSIGVSN 167
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPV---------------PNDFD--RTIQAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 168 FNRRQLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-HREEPWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19127 137 FTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvMRYGASGPTGPGDVLQDPTITGLAE 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5453543 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 300
Cdd:cd19127 215 KYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-301 |
4.59e-78 |
|
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: 240.09 E-value: 4.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYAPAEvPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWC 87
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPelVRPALERSLKNLQLDYVDLYLIHFPVSVK-----PGEEVIPKDENGKILF-DTVDLCATWEAVEKCKDAGLAK 161
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYaASGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 162 SIGVSNFNRRQLEMILNKpgLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEpwvdpnspvLLEDPVL 241
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPLV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVfeFQLTSEEMKAIDGLNR 301
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-299 |
5.32e-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: 5.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 7 CVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKlaiEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSGGYSHEAVVYALK---ECGYRHIDTAKRYGCEELLGKAIK----ESGVPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGeevipkDENGKILFDTvdlcatWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19135 77 PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSG------KNVKETRAET------WRALEELYDEGLCRAIGVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNRRQLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAK 246
Cdd:cd19135 145 NFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEPTVTELAK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 5453543 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19135 212 KYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-311 |
1.28e-76 |
|
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: 236.69 E-value: 1.28e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 13 GHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSHRP 92
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 93 ELVRPALERSLKNLQLDYVDLYLIHFPVS---VKPGEEVIP---KDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPaayVDPAENYPFlwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNrrqLEMILNKpgLKY---KPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPV--LLEDPVL 241
Cdd:cd19114 158 NFN---VQLILDL--LTYakiKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVV 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIF 311
Cdd:cd19114 233 KKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPVVY 302
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-300 |
4.21e-75 |
|
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: 231.34 E-value: 4.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 10 LNDGHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWCNS 89
Cdd:cd19130 4 LNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 90 HRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPgeevipkdengkilfdtvDLCATWEAVEKCKDAGLAKSIGVSNFN 169
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAG------------------NYVHTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 170 RRQLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHK 249
Cdd:cd19130 139 PPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAAAHG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 5453543 250 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 300
Cdd:cd19130 206 KTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-305 |
5.44e-74 |
|
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: 228.59 E-value: 5.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTyapAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWC 87
Cdd:cd19134 3 VTLNDDNTMPVIGLGV---GELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgeevipkdENGKIlfdtVDlcaTWEAVEKCKDAGLAKSIGVSN 167
Cdd:cd19134 76 PDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKY----VD---SWGGLMKLREEGLARSIGVSN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 168 FNRRQLEMILNKPGlkYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19134 138 FTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAA 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 248 HKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19134 205 HGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-300 |
1.95e-69 |
|
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: 217.95 E-value: 1.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 19 LGFGTYA----PAEVPKSKALEATKLAIEAGFRHIDSAHLYN---NEEQVGLAIrskiADGSVKREDIFYTSKL------ 85
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 86 WCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkdengkilFDTVDLCATWEAVEKCKDAGLAKSIGV 165
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP-------------------DPDTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 166 SNFNRRQLEMILNKPglKYKPVCNQVECHPYF--NQRKLLDFCKSKDIVLVAYSALGS----------------HREEPW 227
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5453543 228 VDPNSPVLLEDPVLCALAKKHKRTPALIALRY--QLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 300
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-299 |
2.41e-69 |
|
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: 216.45 E-value: 2.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTY--APAEVPKSkaleaTKLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWCNSHRPE 93
Cdd:cd19139 1 IPAFGLGTFrlKDDVVIDS-----VRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 94 LVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeeviPKDEngkilfdtVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQL 173
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVDLTLIHWPS---------PNDE--------VPVEEYIGALAEAKEQGLTRHIGVSNFTIALL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 174 EMILNKPGlKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPA 253
Cdd:cd19139 135 DEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPA 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 5453543 254 LIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19139 203 QIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-297 |
2.24e-66 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 210.17 E-value: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 9 KLNDGHFMPVLGFGTYApAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADG-SVKREDIFYTSKLWC 87
Cdd:cd19122 2 TLNNGVKIPAVGFGTFA-NEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPK-DENGK--ILFD-TVDLCATWEAVEKCKDAGLAKSI 163
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKyvILKDlTENPEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 164 GVSNFNRRQLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPwvdPNSPVLLEDPVLCA 243
Cdd:cd19122 161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVP---STGERVSENPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5453543 244 LAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTSEEMKAID 297
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAIN 287
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-304 |
4.86e-65 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 206.08 E-value: 4.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWC 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVW---QASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPelVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeeviPKDENgkilfdTVDlcaTWEAVEKCKDAGLAKSIGVSN 167
Cdd:PRK11565 80 DDHKR--PREALEESLKKLQLDYVDLYLMHWPV---------PAIDH------YVE---AWKGMIELQKEGLIKSIGVCN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 168 FNRRQLEMILNKPGLKykPVCNQVECHPYFNQRKLLdfckskdivlvAYSALGSHREEPWvdpnSPV------LLEDPVL 241
Cdd:PRK11565 140 FQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLH-----------AWNATHKIQTESW----SPLaqggkgVFDQKVI 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453543 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVR 304
Cdd:PRK11565 203 RDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
16-297 |
1.72e-63 |
|
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: 201.69 E-value: 1.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTYA---PAEVPKS---KALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSkiadgsVKREDIFYTSKLW 86
Cdd:cd19072 4 VPVLGLGTWGiggGMSKDYSddkKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeevipkdengkilfDTVDLCATWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPN-------------------PSIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNRRQLEMILNKPGlKYKPVCNQVECHpYFNQR---KLLDFCKSKDIVLVAYSALGshREEPWVDPNSPVLLEdpvlca 243
Cdd:cd19072 139 NFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLE--KGKLSNAKGSPLLDE------ 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 5453543 244 LAKKHKRTPALIALRYQLQR-GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19072 209 IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-312 |
4.55e-58 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 187.92 E-value: 4.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTYapaEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWCNSHRPELV 95
Cdd:PRK11172 3 IPAFGLGTF---RLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 96 RPALERSLKNLQLDYVDLYLIHFPVsvkpgeeviPKDEngkilfdtVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEM 175
Cdd:PRK11172 76 IPSLKESLQKLRTDYVDLTLIHWPS---------PNDE--------VSVEEFMQALLEAKKQGLTREIGISNFTIALMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 176 ILNKPGlKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALI 255
Cdd:PRK11172 139 AIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATPAQV 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 5453543 256 ALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFA 312
Cdd:PRK11172 207 ILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSPEGLA 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-297 |
5.00e-56 |
|
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: 182.83 E-value: 5.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 6 QCVKLNDGHFMPVLGFGTYAPAEVPKSKA--LEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIF 80
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAqeIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 81 YTSKLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVkPGEEVIpkdengkilfdtvdlcatwEAVEKCKDAGLA 160
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGV-PLAETV-------------------AAMEELKKEGKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 161 KSIGVSNFNRRQLEMILNKPGLKyKPVCNQVECHpyFNQR----KLLDFCKSKDIVLVAYSALGSHREEPwvdpnsPVLL 236
Cdd:cd19138 134 RAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLR------RGLL 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5453543 237 EDPVLCALAKKHKRTPALIALRYQL-QRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19138 205 ENPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-297 |
5.19e-46 |
|
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: 156.58 E-value: 5.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 13 GHFMPVLGFGTYA------PAEVPKSKALEATKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSkiadgsVKREDIFYTS 83
Cdd:cd19137 1 GEKIPALGLGTWGiggfltPDYSRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 84 KLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgEEVIPKDEngkilfdtvdlcaTWEAVEKCKDAGLAKSI 163
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP------NPNIPLEE-------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 164 GVSNFNRRQLEMILNKpgLKYKPVCNQVECHPY---FNQRKLLDFCKSKDIVLVAYSALgshreepwvdpNSPVLLEDPV 240
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-----------RRGLEKTNRT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 241 LCALAKKHKRTPALIALRYQLQR-GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19137 203 LEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-297 |
3.21e-43 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 150.37 E-value: 3.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 13 GHFMPVLGFGTYA-----PAEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSK 84
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 ---LWCNSH------RPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDENgkilfdtVDLCATWEAVEKCK 155
Cdd:cd19084 74 cglRWDGGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 156 DAGLAKSIGVSNFNRRQLEMIlnkpgLKY-KPVCNQVechPY--FNQ---RKLLDFCKSKDIVLVAYSAL------GSHR 223
Cdd:cd19084 135 KEGKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLaqglltGKYK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 224 EEPWVDPN-----SPVLLED---------PVLCALAKKHKRTPALIALRYQLQR-GV-VVLAKSYNEQRIRQNVQVFEFQ 287
Cdd:cd19084 207 KEPTFPPDdrrsrFPFFRGEnfeknleivDKLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWE 286
|
330
....*....|
gi 5453543 288 LTSEEMKAID 297
Cdd:cd19084 287 LTEEELKEID 296
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
17-297 |
1.86e-41 |
|
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: 146.48 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGT----YAPAEVPKSKALEATKLAIEAGFRHIDSAHLYN---NEEQVGLAIRSKiadgsvKREDIFYTSKL---- 85
Cdd:COG0667 14 SRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR------PRDDVVIATKVgrrm 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 86 ----WCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDENgkilfdtVDLCATWEAVEKCKDAGLAK 161
Cdd:COG0667 88 gpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP------------DPD-------TPIEETLGALDELVREGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 162 SIGVSNFNRRQLEMILNKPGLKYKPVCNQVEchpY--FNQR---KLLDFCKSKDIVLVAYSALGS------HREEPWVDP 230
Cdd:COG0667 149 YIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAARELGVGVLAYSPLAGglltgkYRRGATFPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 231 NS--------PVLLED-----PVLCALAKKHKRTPALIALRYQLQRGVVVL----AKSynEQRIRQNVQVFEFQLTSEEM 293
Cdd:COG0667 226 GDraatnfvqGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENLAAADLELSAEDL 303
|
....
gi 5453543 294 KAID 297
Cdd:COG0667 304 AALD 307
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-297 |
4.58e-41 |
|
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: 144.68 E-value: 4.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTYA---------PAEVPKSkALEATKLAIEAGFRHIDSAHLY---NNEEQVGLAIRskiadGSVKREDIFYTSK 84
Cdd:cd19093 3 SPLGLGTWQwgdrlwwgyGEYGDED-LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 LWC--NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGeevipkdengkilfdtvdLCATWEAVEKCKDAGLAKS 162
Cdd:cd19093 77 FAPlpWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQ------------------IEALMDGLADAVEEGLVRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 163 IGVSNFNRRQLEMI---LNKPGlkYKPVCNQVE---CHPYFNQRKLLDFCKSKDIVLVAYSALG----------SHR-EE 225
Cdd:cd19093 139 VGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspENPpPG 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5453543 226 PWVDPNSPVLLE--DPVLCAL---AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19093 217 GRRRLFGRKNLEkvQPLLDALeeiAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-303 |
1.78e-40 |
|
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: 143.11 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTYAPA------EVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLWC 87
Cdd:cd19085 2 SRLGLGCWQFGggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgeevipkdengkilfdTVDLCATWEAVEKCKDAGLAKSIGVSN 167
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSS-------------------DVPLEETMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 168 FNRRQLEMILnKPGlkyKPVCNQVECHPYFNQ--RKLLDFCKSKDIVLVAYSAL------GSHREEPWVDPN-----SPV 234
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQLPYNLLWRAieYEILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrLFR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 235 LLEDPV----------LCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRN 302
Cdd:cd19085 212 HFEPGAeeetfealekLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
.
gi 5453543 303 V 303
Cdd:cd19085 292 L 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-282 |
3.33e-33 |
|
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: 122.24 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTYA-PAEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRskiadGSVKREDIFYTSKL------- 85
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLK-----GRGNRDDVVIATKGghppggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 86 -WCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAVEKCKDAGLAKSIG 164
Cdd:cd06660 76 pSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEE-------------------TLEALNELVREGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 165 VSNFNRRQLEMILN--KPGLKYKPVCNQVE---CHPYFNQRKLLDFCKSKDIVLVAYSALGshreepwvdpnspvlledp 239
Cdd:cd06660 137 VSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA------------------- 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 5453543 240 vlcalakkhkRTPALIALRYQLQR--GVVVLAKSYNEQRIRQNVQ 282
Cdd:cd06660 198 ----------RGPAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-299 |
9.24e-29 |
|
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: 112.38 E-value: 9.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFGTYA---------PAEVPKSKALEATKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvkREDIFYTSK- 84
Cdd:cd19102 3 TIGLGTWAiggggwgggWGPQDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 --LW------CNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAVEKCKD 156
Cdd:cd19102 76 glLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEE-------------------AWGALAELKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 157 AGLAKSIGVSNFNRRQLEMIL-------NKPGlkYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALGS-------H 222
Cdd:cd19102 137 EGKVRAIGVSNFSVDQMKRCQaihpiasLQPP--YSLLRRGIE-------AEILPFCAEHGIGVIVYSPMQSglltgkmT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 223 REE----PWVD--PNSPVLLED---------PVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFE 285
Cdd:cd19102 208 PERvaslPADDwrRRSPFFQEPnlarnlalvDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAAD 287
|
330
....*....|....
gi 5453543 286 FQLTSEEMKAIDGL 299
Cdd:cd19102 288 LRLTPEELAEIEAL 301
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-281 |
4.87e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 103.33 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNN-EEQVGLAIRSKiadgsvkREDIFYTSKLWcnSHRPELV 95
Cdd:cd19100 12 SRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTG--ARDYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 96 RPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIpkDENGkilfdtvdlcaTWEAVEKCKDAGLAKSIGVSNFNRRQLEM 175
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVF--GPGG-----------ALEALLEAKEEGKIRFIGISGHSPEVLLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 176 ILNKPglkykpvcnqvechpyfnqrkllDFckskDIVLVAYSALGSHREEPwvdpnspvllEDPVLCALAKKHK------ 249
Cdd:cd19100 150 ALETG-----------------------EF----DVVLFPINPAGDHIDSF----------REELLPLAREKGVgviamk 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 5453543 250 -----------RTPALIALRYQLQRGVVVLA----KSYNEqrIRQNV 281
Cdd:cd19100 193 vlaggrllsgdPLDPEQALRYALSLPPVDVVivgmDSPEE--LDENL 237
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
18-292 |
5.44e-26 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 104.85 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKlwC-----NS 89
Cdd:COG4989 17 VLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLS----PSLREKIELQTK--CgirlpSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 90 HRPELV----------RPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkdengkilfDT-VDLCATWEAVEKCKDAG 158
Cdd:COG4989 91 ARDNRVkhydtskehiIASVEGSLRRLGTDYLDLLLLHRP--------------------DPlMDPEEVAEAFDELKASG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 159 LAKSIGVSNFNRRQLEMiLNKpGLKYKPVCNQVECHPYFNQ---RKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVL 235
Cdd:COG4989 151 KVRHFGVSNFTPSQFEL-LQS-ALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 236 LEdpVLCALAKKHKRTPALIALRYqLQR---GVVVLAKSYNEQRIRQNVQVFEFQLTSEE 292
Cdd:COG4989 229 RA--ALDELAEKYGVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-292 |
4.19e-25 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 102.25 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSK----LWCNSH 90
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKcgirLGDDPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 91 R---------PELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkdengkilfDT-VDLCATWEAVEKCKDAGLA 160
Cdd:cd19092 86 PgrikhydtsKEHILASVEGSLKRLGTDYLDLLLLHRP--------------------DPlMDPEEVAEAFDELVKSGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 161 KSIGVSNFNRRQLEMiLNKpGLKYKPVCNQVEC---HPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLE 237
Cdd:cd19092 146 RYFGVSNFTPSQIEL-LQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 238 dpVLCALAKKHKRTPALIALRYQLQ---RGVVVLAkSYNEQRIRQNVQVFEFQLTSEE 292
Cdd:cd19092 224 --ALEELAEEYGVTIEAIALAWLLRhpaRIQPILG-TTNPERIRSAVKALDIELTREE 278
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-299 |
4.73e-25 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 103.36 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLY-NNEEQVGLAIRSKiadgsvkREDIFYTSKL--WCNShrP 92
Cdd:COG1453 13 VSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLppWVRD--P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 93 ELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIpkDENGkilfdtvdlcaTWEAVEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:COG1453 84 EDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVL--KPGG-----------ALEALEKAKAEGKIRHIGFSTHGSLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 173 L----------EMILnkpgLKYkpvcNqvechpYFNQR-----KLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLE 237
Cdd:COG1453 151 VikeaidtgdfDFVQ----LQY----N------YLDQDnqageEALEAAAEKGIGVIIMKPLKGGR-----------LAN 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453543 238 DPVLCALAKKHKRTPALIALRYQLQR-GV-VVLAKSYNEQRIRQNVQVFE--FQLTSEEMKAIDGL 299
Cdd:COG1453 206 PPEKLVELLCPPLSPAEWALRFLLSHpEVtTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
39-299 |
2.51e-24 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 100.57 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 39 KLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvKREDIFYTSKlwcNSHR-----------PELVRPALERSLK 104
Cdd:cd19083 40 REALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATK---GAHKfggdgsvlnnsPEFLRSAVEKSLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 105 NLQLDYVDLYLIHFPvsvkpgEEVIPKDEngkilfdtvdlcaTWEAVEKCKDAGLAKSIGVSNFNRRQLEMiLNKPGL-- 182
Cdd:cd19083 111 RLNTDYIDLYYIHFP------DGETPKAE-------------AVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDGYvd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 183 ----KYKPVCNQVECHpyfnqrkLLDFCKSKDIVLVAYSAL------GSHREEPWVDPN--------------SPVLLED 238
Cdd:cd19083 171 vlqgEYNLLQREAEED-------ILPYCVENNISFIPYFPLasgllaGKYTKDTKFPDNdlrndkplfkgerfSENLDKV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453543 239 PVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19083 244 DKLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-297 |
2.78e-24 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 100.38 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 11 NDGHFMPVLGFG--TYAPAEVPKSK-----ALEATKL---AIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkRE 77
Cdd:cd19091 8 RSGLKVSELALGtmTFGGGGGFFGAwggvdQEEADRLvdiALDAGINFFDTADVYSEgesEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 78 DIFYTSKLW------CN---SHRPELVRpALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTW 148
Cdd:cd19091 81 DVLIATKVRgrmgegPNdvgLSRHHIIR-AVEASLKRLGTDYIDLYQLHGFDALTPLEE-------------------TL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 149 EAVEKCKDAGLAKSIGVSNFNRRQLEMIL---NKPGLKyKPVCNQVechpYFN------QRKLLDFCKSKDIVLVAYSAL 219
Cdd:cd19091 141 RALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 220 GS-------HREEPWVD------------PNSPVLLEDPV--LCALAKKHKRTPALIALRYQLQR----GVVVLAKsyNE 274
Cdd:cd19091 216 AGgllsgkyRRGQPAPEgsrlrrtgfdfpPVDRERGYDVVdaLREIAKETGATPAQVALAWLLSRptvsSVIIGAR--NE 293
|
330 340
....*....|....*....|...
gi 5453543 275 QRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19091 294 EQLEDNLGAAGLSLTPEEIARLD 316
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-297 |
2.21e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 97.67 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 31 KSKALEATKLAIEAGFRHIDSAHLYNN-EEQVGLAIRSKIADGSVKREDIFYTsKLWCNSHR----PELVRPALERSLKN 105
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDAADDVQIHT-KWVPDPGEltmtRAYVEAAIDRSLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 106 LQLDYVDLYLIHFpvsvkpgeevipKDENGKILFDTVdlcatwEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKPglkYK 185
Cdd:cd19101 101 LGVDRLDLVQFHW------------WDYSDPGYLDAA------KHLAELQEEGKIRHLGLTNFDTERLREILDAG---VP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 186 PVCNQVEcHPYFNQR---KLLDFCKSKDIVLVAYSALGS---------HREEPWVDPNSPV------------------- 234
Cdd:cd19101 160 IVSNQVQ-YSLLDRRpenGMAALCEDHGIKLLAYGTLAGgllsekylgVPEPTGPALETRSlqkyklmidewggwdlfqe 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5453543 235 LLEdpVLCALAKKHKRTPALIALRYQLQR----GVVVLAKsyNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19101 239 LLR--TLKAIADKHGVSIANVAVRWVLDQpgvaGVIVGAR--NSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-288 |
8.03e-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: 95.70 E-value: 8.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTY----APAEVPKSKALEATKLAIEAGFRHIDSAHLYNN-EEQVGLAIRSkiadgsVKREDIFYTSKLWCNSHR 91
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVGRLPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 92 -----PELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPkdenGKILfdtvdlcatwEAVEKCKDAGLAKSIGVS 166
Cdd:cd19090 75 tadysADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP----GGAL----------EALLELKEEGLIKHIGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 ----NFNRR-----QLEMILnkPGLKYKPvCNQVechpyfNQRKLLDFCKSKDIVLVAYSALG----SHREEPWVDPNSP 233
Cdd:cd19090 141 ggppDLLRRaietgDFDVVL--TANRYTL-LDQS------AADELLPAAARHGVGVINASPLGmgllAGRPPERVRYTYR 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5453543 234 VLLEDPV-----LCALAKKHKRTPALIALRYQLQ----RGVVVLAKsyNEQRIRQNVQVFEFQL 288
Cdd:cd19090 212 WLSPELLdrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNVAAAEGPL 273
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-169 |
1.52e-22 |
|
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: 94.22 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTY----APAEVPKSKALEATKLAIEAGFRHIDSAHLY-NNEEQVGLAIRSkiadgsVKREDIFYTSKLWCNS-- 89
Cdd:cd19095 1 SVLGLGTSgigrVWGVPSEAEAARLLNTALDLGINLIDTAPAYgRSEERLGRALAG------LRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 90 ------HRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIpkdengkilfdtvdlcatwEAVEKCKDAGLAKSI 163
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVL-------------------ETLEDLKAAGKVRYI 135
|
....*.
gi 5453543 164 GVSNFN 169
Cdd:cd19095 136 GVSGDG 141
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-297 |
1.80e-22 |
|
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: 95.42 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTYA--------PAEVPKS-KALEAtklAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSK 84
Cdd:cd19149 12 SVIGLGTWAigggpwwgGSDDNESiRTIHA---ALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 --LWCNSH-----------------RPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlc 145
Cdd:cd19149 82 cgLRWDREggsfffvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEE------------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 146 aTWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKPGL-----KYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSAL- 219
Cdd:cd19149 144 -TMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLdiiqeKYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLe 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 220 ----------------GSHRE-EPWVDPNS--PVLLEDPVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIR 278
Cdd:cd19149 216 qglltgkitpdrefdaGDARSgIPWFSPENreKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAE 295
|
330
....*....|....*....
gi 5453543 279 QNVQVFEFQLTSEEMKAID 297
Cdd:cd19149 296 ENAKAGDIRLSAEDIATMR 314
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-289 |
4.99e-22 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 93.05 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 15 FMPVLGFGTYAPAEvPKSKALEATKLAIEAGFRHIDSAHLYN---NEEQVGLAIRSKIAD-------GSVKREDifytsK 84
Cdd:cd19088 8 AMRLTGPGIWGPPA-DREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYPDDvviatkgGLVRTGP-----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 LWCNSHRPELVRPALERSLKNLQLDYVDLYLIHfpvsvkpgeevipkdengkILFDTVDLCATWEAVEKCKDAGLAKSIG 164
Cdd:cd19088 82 WWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLH-------------------RIDPKVPFEEQLGALAELQDEGLIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 165 VSNFNRRQLEMILNKPGLkykpVCNQVECHPYFNQ-RKLLDFCKSKDIVLVAYSALGSHreepwvdpnsPVLLEDPVLCA 243
Cdd:cd19088 143 LSNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGGG----------DLAQPGGLLAE 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 5453543 244 LAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLT 289
Cdd:cd19088 209 VAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-296 |
6.70e-22 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 94.05 E-value: 6.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 11 NDGHFMPVLGFGT------YAPAEvPKSKALEATKLAIEAGFRHIDSAHLY-NNEEQVGLAIrsKIADGsvKREDIFYTS 83
Cdd:cd19144 8 RNGPSVPALGFGAmglsafYGPPK-PDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWF--KQNPG--KREKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 84 K-----------LWCNShRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAVE 152
Cdd:cd19144 83 KfgieknvetgeYSVDG-SPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEK-------------------TVAAMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 153 KCKDAGLAKSIGVSNFNRRQLemilnKPGLKYKPVCN-QVECHPYF-----NQRKLLDFCKSKDIVLVAYSALGS----- 221
Cdd:cd19144 143 ELVQEGKIKHIGLSECSAETL-----RRAHAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRgfltg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 222 -------------HREEPWVDP-NSPVLLE--DPvLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQV 283
Cdd:cd19144 218 airspddfeegdfRRMAPRFQAeNFPKNLElvDK-IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGA 296
|
330
....*....|...
gi 5453543 284 FEFQLTSEEMKAI 296
Cdd:cd19144 297 LKVKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-230 |
8.59e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 89.57 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 13 GHFMPVLGFGTYAPAevpkSKALEATKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSkiadgsVKREDIFYTSKLWC-- 87
Cdd:cd19105 10 GLKVSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALKG------LRRDKVFLATKASPrl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHfpvSVKPGEEVIPKDEngkILfdtvdlcatwEAVEKCKDAGLAKSIGVS- 166
Cdd:cd19105 80 DKKDKAELLKSVEESLKRLQTDYIDIYQLH---GVDTPEERLLNEE---LL----------EALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5453543 167 NFNrrQLEMILnkpglkykpvcNQVECHPY------FN-------QRKLLDFCKSKDIVLVAYSALGSHREEPWVDP 230
Cdd:cd19105 144 HDN--MAEVLQ-----------AAIESGWFdvimvaYNflnqpaeLEEALAAAAEKGIGVVAMKTLAGGYLQPALLS 207
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-285 |
1.05e-19 |
|
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: 86.46 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTY-APAEVPKSKALEAT----KLAIEAGFRHIDSAHLYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WC 87
Cdd:cd19096 1 SVLGFGTMrLPESDDDSIDEEKAiemiRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgEEVIPKDENGKIlfdtvdlcatWEAVEKCKDAGLAKSIGVSn 167
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNS----PEWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 168 F--NRRQLEMILNkpglkykpvCNQVEC----HPYFNQ-----RKLLDFCKSKDIVLVAYSAL--GSHREEPwvdpnspv 234
Cdd:cd19096 140 FhdSPELLKEILD---------SYDFDFvqlqYNYLDQenqagRPGIEYAAKKGMGVIIMEPLkgGGLANNP-------- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 5453543 235 lledPVLCALAKKHKRTPALIALRYQL-QRGV-VVLAKSYNEQRIRQNVQVFE 285
Cdd:cd19096 203 ----PEALAILCGAPLSPAEWALRFLLsHPEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
33-297 |
1.08e-19 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 87.36 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 33 KALEATKLAIEAGFRHIDSAHLYN---NEEQVGLAIRskiadGSVKREDIFYTSKL---WCNSH------RPELVRPALE 100
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALK-----EYGKRDRVVIATKVgleWDEGGevvrnsSPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 101 RSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAVEKCKDAGLAKSIGVSNFNRRQLEmilnkp 180
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWPDPLVPIEE-------------------TAEALKELLDEGKIRAIGVSNFSPEQME------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 181 glKYKPVCNQVECHPYFN------QRKLLDFCKSKDIVLVAYSAL---------GSHREEPWVD----------PNSPVL 235
Cdd:cd19148 156 --TFRKVAPLHTVQPPYNlfereiEKDVLPYARKHNIVTLAYGALcrgllsgkmTKDTKFEGDDlrrtdpkfqePRFSQY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 236 LEdPV--LCALAKKH--KRTPALiALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19148 234 LA-AVeeLDKLAQERygKSVIHL-AVRWLLDQPgvSIALWGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
29-297 |
1.54e-19 |
|
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: 87.25 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 29 VPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKIadgsvKREDIFYTSKLwCNSHRPEL---------VR 96
Cdd:cd19079 32 LDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKV-YFPMGDGPngrglsrkhIM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 97 PALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDENgkilfdtVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMI 176
Cdd:cd19079 106 AEVDASLKRLGTDYIDLYQIHRW------------DYE-------TPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 177 LN---KPGLKyKPVCNQvechPYFN------QRKLLDFCKSKDIVLVAYSALGSHR---------EEPWVDPNSPVLLED 238
Cdd:cd19079 167 LHlaeKNGWT-KFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLARGRlarpwgdttERRRSTTDTAKLKYD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5453543 239 -------PVLCA---LAKKHKRTPALIALRYQLQRGVVV-----LAKSYneqRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19079 242 yfteadkEIVDRveeVAKERGVSMAQVALAWLLSKPGVTapivgATKLE---HLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-297 |
3.48e-19 |
|
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: 86.11 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 42 IEAGFRHIDSAHLYNN----------EEQVGLAIRSkiadgSVKREDIFYTSKL--WCNSHRPEL----VRPALERSLKN 105
Cdd:cd19081 36 VDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKS-----RGKRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 106 LQLDYVDLYLIHFPvsvkpgeevipkDENgkilfdtVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMILN---KPGL 182
Cdd:cd19081 111 LQTDYIDLYQAHWD------------DPA-------TPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 183 KyKPVCNQvechPYFN-------QRKLLDFCKSKDIVLVAYSALGS-------HREEP--------------WVDPNSPV 234
Cdd:cd19081 172 P-RYVSLQ----PEYNlvdresfEGELLPLCREEGIGVIPYSPLAGgfltgkyRSEADlpgstrrgeaakryLNERGLRI 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5453543 235 LledPVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19081 247 L---DALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-221 |
6.94e-18 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 81.37 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFGTYA-----PAEVPKSKALEATKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvkREDIFYTSK----L 85
Cdd:cd19086 5 EIGFGTWGlggdwWGDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVVIATKfgnrF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 86 WCNSHR-----PELVRPALERSLKNLQLDYVDLYLIHfpvsvKPGEEVIPKDEngkilfdtvdlcaTWEAVEKCKDAGLA 160
Cdd:cd19086 78 DGGPERpqdfsPEYIREAVEASLKRLGTDYIDLYQLH-----NPPDEVLDNDE-------------LFEALEKLKQEGKI 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 161 KSIGVSnfnrrqlemiLNKP--GLKY--KPVCNQVEcHPY--FNQR---KLLDFCKSKDIVLVAYSALGS 221
Cdd:cd19086 140 RAYGVS----------VGDPeeALAAlrRGGIDVVQ-VIYnlLDQRpeeELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
17-296 |
1.03e-17 |
|
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: 81.88 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGT------YAPAEVPKSKALeaTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvkREDIFYTSK--- 84
Cdd:cd19076 13 SALGLGCmgmsafYGPADEEESIAT--LHRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RDEVVIATKfgi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 LWC-------NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAVEKCKDA 157
Cdd:cd19076 84 VRDpgsgfrgVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEE-------------------TVGAMAELVEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 158 GLAKSIGVSNFN----RR----------QLEmilnkpglkYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALG--- 220
Cdd:cd19076 145 GKVRYIGLSEASadtiRRahavhpitavQSE---------YSLWTRDIE-------DEVLPTCRELGIGFVAYSPLGrgf 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 221 --------SHREEPWVDPNSP-----------VLLEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQ 279
Cdd:cd19076 209 ltgaikspEDLPEDDFRRNNPrfqgenfdknlKLVE--KLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEE 286
|
330
....*....|....*..
gi 5453543 280 NVQVFEFQLTSEEMKAI 296
Cdd:cd19076 287 NVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-259 |
2.01e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 81.21 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 19 LGFGTY--APAEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKIADGSVKREDIFYTSK--------- 84
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 ------LWC----------------NSH--RPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgEEVIPKDeNGKILFD 140
Cdd:cd19099 86 eplrplKYLeeklgrglidvadsagLRHciSPAYLEDQIERSLKRLGLDTIDLYLLHNP------EEQLLEL-GEEEFYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 141 TVDlcATWEAVEKCKDAGLAKSIGVSNFN------------------RRQLEMILNKPGLK-----YKPVCNQVECHPYF 197
Cdd:cd19099 159 RLE--EAFEALEEAVAEGKIRYYGISTWDgfrappalpghlsleklvAAAEEVGGDNHHFKviqlpLNLLEPEALTEKNT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5453543 198 NQRK---LLDFCKSKDIVLVAYSALGShreepwVDPNSPVLLEDPvlcaLAKKHKRTPALIALRY 259
Cdd:cd19099 237 VKGEalsLLEAAKELGLGVIASRPLNQ------GQLLGELRLADL----LALPGGATLAQRALQF 291
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-299 |
2.01e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 78.14 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 41 AIEAGFRHIDSAHLYnneeqvGLAIRSKIAdGSV----KREDIFYTSKL--WCNSHRPELVRPALERSLKNLQLDYVDLY 114
Cdd:cd19103 41 AMAAGLNLWDTAAVY------GMGASEKIL-GEFlkryPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 115 LIHFPVSV-KPGEEVIPKDENGKIlfdtvdlcatweavekckdaglaKSIGVSNFNRRQLEM---ILNKPGLKYKPVCNQ 190
Cdd:cd19103 114 WIHNPADVeRWTPELIPLLKSGKV-----------------------KHVGVSNHNLAEIKRaneILAKAGVSLSAVQNH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 191 VE-CHPYFNQRKLLDFCKSKDIVLVAYSAL-----------------GSHREEPWvdpnSPVL--LED--PVLCALAKKH 248
Cdd:cd19103 171 YSlLYRSSEEAGILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGRAETY----NPLLpqLEEltAVMAEIGAKH 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 5453543 249 KRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19103 247 GASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-297 |
2.20e-16 |
|
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: 78.03 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 42 IEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKL----------WCNSHRPELVRpALERSLKNLQL 108
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKYtmnrrpgdpnAGGNHRKNLRR-SVEASLRRLQT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 109 DYVDLYLIHFPVSVKPGEEVIPK-DE---NGKILFdtVDLCAT--WEAVekcKDAGLAKSIGVSNFNRRQLEmilnkpgl 182
Cdd:cd19080 113 DYIDLLYVHAWDFTTPVEEVMRAlDDlvrAGKVLY--VGISDTpaWVVA---RANTLAELRGWSPFVALQIE-------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 183 kYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALG-------------SHREEPWVDPNSPVLLED------PVLCA 243
Cdd:cd19080 180 -YSLLERTPE-------RELLPMARALGLGVTPWSPLGgglltgkyqrgeeGRAGEAKGVTVGFGKLTErnwaivDVVAA 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 5453543 244 LAKKHKRTPALIALRYQLQR---GVVVLAKSYNEQrIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19080 252 VAEELGRSAAQVALAWVRQKpgvVIPIIGARTLEQ-LKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
40-297 |
3.20e-15 |
|
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: 74.91 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 40 LAIEAGFRHIDSAHLY----------NNEEQVGLAIRSKiadgsVKREDIF-------YTSKLWCNSHRP-----ELVRP 97
Cdd:cd19094 26 YAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKK-----GNRDKVVlatkvagPGEGITWPRGGGtrldrENIRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 98 ALERSLKNLQLDYVDLYLIHFPVSVKP----GEEVIPKDENgkilfDTVDLCATWEAVEKCKDAGLAKSIGVSN------ 167
Cdd:cd19094 101 AVEGSLKRLGTDYIDLYQLHWPDRYTPlfggGYYTEPSEEE-----DSVSFEEQLEALGELVKAGKIRHIGLSNetpwgv 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 168 --FNR--RQLemilnkpGLKyKPVCNQvecHPY--FNQRKLLDF---CKSKDIVLVAYSAL------GSHREEPWVDPNS 232
Cdd:cd19094 176 mkFLElaEQL-------GLP-RIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLaggvltGKYLDGAARPEGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 233 PVLL--------EDP-------VLCALAKKHKRTPALIALRYQLQR---GVVVLAKSYNEQrIRQNVQVFEFQLTSEEMK 294
Cdd:cd19094 245 RLNLfpgymaryRSPqaleavaEYVKLARKHGLSPAQLALAWVRSRpfvTSTIIGATTLEQ-LKENIDAFDVPLSDELLA 323
|
...
gi 5453543 295 AID 297
Cdd:cd19094 324 EID 326
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
18-291 |
5.01e-15 |
|
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: 74.17 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFGTYAP--AEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WCNSHR 91
Cdd:cd19074 6 ELSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 92 PE---LVRP----ALERSLKNLQLDYVDLYLIH-FPVSVKPGE------EVIpkdENGKILFDTVdlcATWEAVEKCKDA 157
Cdd:cd19074 80 PNdrgLSRKhifeSIHASLKRLQLDYVDIYYCHrYDPETPLEEtvramdDLI---RQGKILYWGT---SEWSAEQIAEAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 158 GLAKSIGVsnfnrrqlemilnkpglkYKPVCNQVECHpYFNQRK---LLDFCKSKDIVLVAYSAL--------------- 219
Cdd:cd19074 154 DLARQFGL------------------IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltgkyrdgipp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 220 --GSHREEPWVDPNSPVLLEDPV------LCALAKKHKRTPALIALRYQLQR-GV--VVLAKSYNEQrIRQNVQVFEFQL 288
Cdd:cd19074 215 psRSRATDEDNRDKKRRLLTDENlekvkkLKPIADELGLTLAQLALAWCLRNpAVssAIIGASRPEQ-LEENVKASGVKL 293
|
...
gi 5453543 289 TSE 291
Cdd:cd19074 294 SPE 296
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-259 |
7.22e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 73.33 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 29 VPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVglairskIADGSVKREDIFYTSKL----WCNSHRPELVRPALERSLK 104
Cdd:cd19097 23 PSEKEAKKILEYALKAGINTLDTAPAYGDSEKV-------LGKFLKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 105 NLQLDYVDLYLIHfpvsvkpGEEVIPKDeNGKIlfdtvdlcatWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKY 184
Cdd:cd19097 96 RLKVDSLDGLLLH-------NPDDLLKH-GGKL----------VEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 185 kpVcnQVechPY--FNQR----KLLDFCKSKDIVLVAYSA-----LGSHREEP--WVDPNSPVLLEdpvLCALAKKHKRT 251
Cdd:cd19097 158 --I--QL---PFniLDQRflksGLLAKLKKKGIEIHARSVflqglLLMEPDKLpaKFAPAKPLLKK---LHELAKKLGLS 227
|
....*...
gi 5453543 252 PALIALRY 259
Cdd:cd19097 228 PLELALGF 235
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-294 |
1.42e-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: 72.58 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 16 MPVLGFGTyAPA-----EVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSkiadgsVKREDIFYTSK--- 84
Cdd:cd19163 13 VSKLGFGA-SPLggvfgPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALKG------IPRDSYYLATKvgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 ---LWCNS--HRPELVRPALERSLKNLQLDYVDLYLIHfPVSVKPGEEVIpkdengkilfdtvdLCATWEAVEKCKDAGL 159
Cdd:cd19163 86 yglDPDKMfdFSAERITKSVEESLKRLGLDYIDIIQVH-DIEFAPSLDQI--------------LNETLPALQKLKEEGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 160 AKSIGVSNFNRRQLEMILNKPG------LKYkpvcnqveCHpY--FNQR--KLLDFCKSKDIVLVAYSALG----SHREE 225
Cdd:cd19163 151 VRFIGITGYPLDVLKEVLERSPvkidtvLSY--------CH-YtlNDTSllELLPFFKEKGVGVINASPLSmgllTERGP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5453543 226 PwvdPNSPVLLEDPVLCALAKKHKRTP----ALIALRYQLQ--RGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMK 294
Cdd:cd19163 222 P---DWHPASPEIKEACAKAAAYCKSRgvdiSKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-299 |
4.24e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 71.53 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 34 ALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLwcnSHRPEL-------VRPALERSL 103
Cdd:cd19104 34 QIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL-------PAGPYITTKV---RLDPDDlgdiggqIERSVEKSL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 104 KNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTvdlcATWEAVEKCKDAGLAKSIGVSNF-NRRQLEMIL--NKP 180
Cdd:cd19104 104 KRLKRDSVDLLQLHNRIGDERDKPVGGTLSTTDVLGLG----GVADAFERLRSEGKIRFIGITGLgNPPAIRELLdsGKF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 181 G--------LKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS---------HREEPwVDPNSPVLLE----DP 239
Cdd:cd19104 180 DavqvyynlLNPSAAEARPRGWSAQDYGGIIDAAAEHGVGVMGIRVLAAgalttsldrGREAP-PTSDSDVAIDfrraAA 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5453543 240 VLcALAKKHKRTPALIALRYQL-QRGV--VVLAKSyNEQRIRQNVQVFEF-QLTSEEMKAIDGL 299
Cdd:cd19104 259 FR-ALAREWGETLAQLAHRFALsNPGVstVLVGVK-NREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-299 |
7.85e-14 |
|
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: 70.66 E-value: 7.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLG---FGTYA-PAEVPKSKALEATKLaiEAGFRHIDSAHLYNN---EEQVGlAIRSKIADGSV--KredifyTSKLWCN 88
Cdd:cd19075 4 ILGtmtFGSQGrFTTAEAAAELLDAFL--ERGHTEIDTARVYPDgtsEELLG-ELGLGERGFKIdtK------ANPGVGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 89 SHRPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDEngkilfdTVDLCATWEAVEKCKDAGLAKSIGVSNF 168
Cdd:cd19075 75 GLSPENVRKQLETSLKRLKVDKVDVFYLHAP------------DR-------STPLEETLAAIDELYKEGKFKEFGLSNY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 169 NRRQLEMILN--------KP----GLkYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSAL------GSHREEPWV-- 228
Cdd:cd19075 136 SAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLaggfltGKYKYSEDKag 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 229 ----DPNSPVL---------------LEdpVLCALAKKHKRTPALIALRY-----QLQRG---VVVLAKSyNEQRIRQNV 281
Cdd:cd19075 208 ggrfDPNNALGklyrdrywkpsyfeaLE--KVEEAAEKEGISLAEAALRWlyhhsALDGEkgdGVILGAS-SLEQLEENL 284
|
330
....*....|....*....
gi 5453543 282 Q-VFEFQLTSEEMKAIDGL 299
Cdd:cd19075 285 AaLEKGPLPEEVVKAIDEA 303
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-282 |
3.72e-13 |
|
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: 68.73 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGT-YAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLA-------IRSKIadgsvKREDIFYTSK---- 84
Cdd:cd19082 1 SRIVLGTaDFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGAServigewLKSRG-----NRDKVVIATKgghp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 -LWCNS-HR--PELVRPALERSLKNLQLDYVDLYLIH-----FPVsvkpgEEVIpkdengkilfdtvdlcatwEAVEKCK 155
Cdd:cd19082 76 dLEDMSrSRlsPEDIRADLEESLERLGTDYIDLYFLHrddpsVPV-----GEIV-------------------DTLNELV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 156 DAGLAKSIGVSNFNrrqLEMIL---------NKPGlkykPVCNQvechPYFN-----------------QRKLLDFCKSK 209
Cdd:cd19082 132 RAGKIRAFGASNWS---TERIAeanayakahGLPG----FAASS----PQWSlarpneppwpgptlvamDEEMRAWHEEN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 210 DIVLVAYSALG----SHREEPWVDPNSPVL-----------LEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSY 272
Cdd:cd19082 201 QLPVFAYSSQArgffSKRAAGGAEDDSELRrvyyseenferLE--RAKELAEEKGVSPTQIALAYVLNQPfpTVPIIGPR 278
|
330
....*....|
gi 5453543 273 NEQRIRQNVQ 282
Cdd:cd19082 279 TPEQLRDSLA 288
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
41-299 |
4.98e-13 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 68.37 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 41 AIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKL------WCNSH---RPELVRpALERSLKNLQL 108
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVfgpmgdDPNDRglsRRHIRR-AVEASLRRLQT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 109 DYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAVEKCKDAGLAKSIGVSNF-------------NRRQLEM 175
Cdd:cd19087 111 DYIDLYQMHHFDRDTPLEE-------------------TLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaaRRGLLRF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 176 ILNKPglKYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALG---------------SHR--------EEPWVDPNS 232
Cdd:cd19087 172 VSEQP--MYNLLKRQAE-------LEILPAARAYGLGVIPYSPLAgglltgkygkgkrpeSGRlveraryqARYGLEEYR 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5453543 233 PVLLEdpvLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19087 243 DIAER---FEALAAEAGLTPASLALAWVLSHPAVtsPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-297 |
1.04e-12 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 67.26 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 19 LGFG------TYAPaevPKSKAlEATKL---AIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvkREDIFYTSK-- 84
Cdd:cd19078 7 IGLGcmgmshGYGP---PPDKE-EMIELirkAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKfg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 ----------LWCNShRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIpkdengkilfdtvdlcatwEAVEKC 154
Cdd:cd19078 76 fkidggkpgpLGLDS-RPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVA-------------------GTMKEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 155 KDAGLAKSIGVS----NFNRRqlemilnkpGLKYKPVCN-QVECHPYFN--QRKLLDFCKSKDIVLVAYSALGSHREEPW 227
Cdd:cd19078 136 IKEGKIRHWGLSeagvETIRR---------AHAVCPVTAvQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLGKGFLTGK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 228 VDPNSP----------------------VLLEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQV 283
Cdd:cd19078 207 IDENTKfdegddraslprftpealeanqALVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGA 284
|
330
....*....|....
gi 5453543 284 FEFQLTSEEMKAID 297
Cdd:cd19078 285 ADIELTPEELREIE 298
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
20-297 |
8.98e-12 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 64.57 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 20 GFG----TYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVG--LAIRSKIADGSVKREDIFYTSKLWCNSH--- 90
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKGGLDPDtlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 91 ---RPELVRPALERSLKNL-QLDYVDLYlihfpvsvkpgeEVIPKDENgkilfdtVDLCATWEAVEKCKDAGLAKSIGVS 166
Cdd:cd19077 89 pdgSPEAVRKSIENILRALgGTKKIDIF------------EPARVDPN-------VPIEETIKALKELVKEGKIRGIGLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 167 NFNRRQLEMILnkpglKYKPV-CNQVECHPYFN---QRKLLDFCKSKDIVLVAYSALGS-----HREEPWVDPNSPVLLE 237
Cdd:cd19077 150 EVSAETIRRAH-----AVHPIaAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRglltgRIKSLADIPEGDFRRH 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 238 DP---------------VLCALAKKHKRTPALIAL---RYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19077 225 LDrfngenfeknlklvdALQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-282 |
1.45e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 63.89 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 42 IEAGFRHIDSAHLYN----------NEEQVG--LAIRSKiadgsvkREDIFYTSKL---------WCNSHR---PELVRP 97
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGrwLKDRGN-------RDDVVIATKVgagprdpdgGPESPEglsAETIEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 98 ALERSLKNLQLDYVDLYLIHfpvsvkpgeevipkdengkILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEM-- 175
Cdd:cd19752 100 EIDKSLRRLGTDYIDLYYAH-------------------VDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERar 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 176 -ILNKPGLKyKPVCNQVEcHPYF---------NQR----KLLDFCKS-KDIVLVAYSAL--GSH------REEPWVDPNS 232
Cdd:cd19752 161 qIARQQGWA-EFSAIQQR-HSYLrprpgadfgVQRivtdELLDYASSrPDLTLLAYSPLlsGAYtrpdrpLPEQYDGPDS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 5453543 233 PVLLEdpVLCALAKKHKRTPALIALRYQLQR--GVV-VLAKSYNEQrIRQNVQ 282
Cdd:cd19752 239 DARLA--VLEEVAGELGATPNQVVLAWLLHRtpAIIpLLGASTVEQ-LEENLA 288
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
19-296 |
2.79e-11 |
|
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: 63.22 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 19 LGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKIadgsvkREDIFYTSKLWCNSHR---- 91
Cdd:cd19145 20 MGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKFGIHEIGgsgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 92 -----PELVRPALERSLKNLQLDYVDLYLIH-----FPVSVKPGE--EVIpkdENGKIlfdtvdlcatweavekckdagl 159
Cdd:cd19145 94 evrgdPAYVRAACEASLKRLDVDYIDLYYQHridttVPIEITMGElkKLV---EEGKI---------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 160 aKSIGVSNFN----RR----------QLEMILnkpglkykpVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALGshREE 225
Cdd:cd19145 149 -KYIGLSEASadtiRRahavhpitavQLEWSL---------WTRDIE-------EEIIPTCRELGIGIVPYSPLG--RGF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 226 PWvdpNSPVLLEDPV-------------------------LCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIR 278
Cdd:cd19145 210 FA---GKAKLEELLEnsdvrkshprfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLN 286
|
330
....*....|....*...
gi 5453543 279 QNVQVFEFQLTSEEMKAI 296
Cdd:cd19145 287 QNIGALSVKLTKEDLKEI 304
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
18-167 |
4.45e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 56.79 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFGTYAPAEV-PKSKALEATKLAIEAGFRHIDSAHLYN----------NEEQVG-----------LAIRSKIAdGSVK 75
Cdd:PRK10625 15 TLGLGTMTFGEQnSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGnwlakrgsrekLIIASKVS-GPSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 76 REDifytsklwcNSHRPEL------VRPALERSLKNLQLDYVDLYLIHFPVSvkpgeeviPKDENGKILFD------TVD 143
Cdd:PRK10625 94 NND---------KGIRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWPQR--------PTNCFGKLGYSwtdsapAVS 156
|
170 180
....*....|....*....|....
gi 5453543 144 LCATWEAVEKCKDAGLAKSIGVSN 167
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-166 |
5.73e-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: 56.21 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTYAPAEVPKSKALEATKL---AIEAGFRHIDSAHLYN---NEEQVGLAIRSKiadgsvKREDIFYTSKL----- 85
Cdd:cd19162 1 PRLGLGAASLGNLARAGEDEAAATldaAWDAGIRYFDTAPLYGlglSERRLGAALARH------PRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 86 -----WCNSHRPEL------VRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDENgkilfDTVDLCATWEAVEKC 154
Cdd:cd19162 75 pgaagRPAGADRRFdfsadgIRRSIEASLERLGLDRLDLVFLHDP------------DRH-----LLQALTDAFPALEEL 137
|
170
....*....|..
gi 5453543 155 KDAGLAKSIGVS 166
Cdd:cd19162 138 RAEGVVGAIGVG 149
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-165 |
6.53e-08 |
|
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: 53.00 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTyAP-----AEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvKREDIFYTSKL--- 85
Cdd:cd19152 1 PKLGFGT-APlgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgrl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 86 ---------------WCNS-HRPEL------VRPALERSLKNLQLDYVDLYLIHFPvsvkpgEEVIPKDENgKILFDTVD 143
Cdd:cd19152 74 lvplqeveptfepgfWNPLpFDAVFdysydgILRSIEDSLQRLGLSRIDLLSIHDP------DEDLAGAES-DEHFAQAI 146
|
170 180
....*....|....*....|..
gi 5453543 144 LCAtWEAVEKCKDAGLAKSIGV 165
Cdd:cd19152 147 KGA-FRALEELREEGVIKAIGL 167
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
17-209 |
8.76e-08 |
|
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: 52.85 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGTYA--PAEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKL-WcnSH 90
Cdd:cd19142 14 SNVGLGTWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIyW--SY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 91 RPE---LVRP----ALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKD----ENGKILFDTvdlCATWEAVEkckdagl 159
Cdd:cd19142 88 GSEergLSRKhiieSVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMsyliDNGLIMYWG---TSRWSPVE------- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5453543 160 aksIGVSNFNRRQLEMILnkpglkykPVCNQVECHPyfnqrklldFCKSK 209
Cdd:cd19142 158 ---IMEAFSIARQFNCPT--------PICEQSEYHM---------FCREK 187
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-129 |
1.04e-07 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 52.60 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFG---TYApAEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRskiaDGSVKREDIFYTSKL-W---- 86
Cdd:cd19143 15 ALSFGswvTFG-NQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKIfWgggg 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 5453543 87 --CNSH---RPELVRpALERSLKNLQLDYVDLYLIHFPVSVKPGEEVI 129
Cdd:cd19143 90 ppPNDRglsRKHIVE-GTKASLKRLQLDYVDLVFCHRPDPATPIEETV 136
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-266 |
1.89e-07 |
|
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: 51.87 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 20 GFGTYAPAEVPKSKALEAtklaIEAGFRHIDsahLYNN--------EEQVGLAIRSkiaDGSVKREDIFYTSK----LW- 86
Cdd:cd19089 21 NFGDYTSPEEARELLRTA----FDLGITHFD---LANNygpppgsaEENFGRILKR---DLRPYRDELVISTKagygMWp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 87 ----CNSHRPELVRpALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAVEKCKDAGLAKS 162
Cdd:cd19089 91 gpygDGGSRKYLLA-SLDQSLKRMGLDYVDIFYHHRYDPDTPLEE-------------------TMTALADAVRSGKALY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 163 IGVSNFNRRQLEM---ILNKpgLKYKPVCNQVechPY--FNQ---RKLLDFCKSKDIVLVAYSAL--------------- 219
Cdd:cd19089 151 VGISNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIGFIAFSPLaqglltdkylngipp 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 5453543 220 GSHREEPWVDPNSPVLLEDPV-----LCALAKKHKRTPALIALRYQLQRGVV 266
Cdd:cd19089 226 DSRRAAESKFLTEEALTPEKLeqlrkLNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-166 |
7.86e-07 |
|
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: 49.97 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFGTYAPA---EVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQV-GLAIrSKIADgSVKREDIFYTSK-----LWCN 88
Cdd:cd19164 17 IFGAATFSYQyttDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL-KALRD-EFPRDTYFIITKvgrygPDDF 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 89 SHRPELVRPALERSLKNLQLDYVDLYLIHfPVSVKPGEEVIpkdENGKILFdtvdlcatweaveKCKDAGLAKSIGVS 166
Cdd:cd19164 95 DYSPEWIRASVERSLRRLHTDYLDLVYLH-DVEFVADEEVL---EALKELF-------------KLKDEGKIRNVGIS 155
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
19-285 |
3.13e-06 |
|
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: 47.92 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 19 LGFGTYAPAEV----PKSKALEAT-KLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKlwCNSH 90
Cdd:cd19153 15 VGLGTAALGGVygdgLEQDEAVAIvAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATK--VGRY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 91 RP-------ELVRPALERSLKNLQLDYVDLYLIH-------FPVSvkpgEEVIPkdengkilfdtvdlcatweAVEKCKD 156
Cdd:cd19153 89 RDsefdysaERVRASVATSLERLHTTYLDVVYLHdiefvdyDTLV----DEALP-------------------ALRTLKD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 157 AGLAKSIGVSNFNRRQLEMILNK--PGlkyKPVCNQVECHPYFNQRKLLD----FCKSKDIVLVAYSALG----SHREEP 226
Cdd:cd19153 146 EGVIKRIGIAGYPLDTLTRATRRcsPG---SLDAVLSYCHLTLQDARLESdapgLVRGAGPHVINASPLSmgllTSQGPP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453543 227 WVDPNSPVLLEdpvLCALAKKH-----KRTPALiALRYQL----QRGVVVLAKSYNEQrIRQNVQVFE 285
Cdd:cd19153 223 PWHPASGELRH---YAAAADAVcasveASLPDL-ALQYSLaahaGVGTVLLGPSSLAQ-LRSMLAAVD 285
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
18-281 |
4.08e-06 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 47.85 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFGTyAP-----AEVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKlwCNS 89
Cdd:PLN02587 13 SVGFGA-SPlgsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTK--CGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 90 HR------PELVRPALERSLKNLQLDYVDLYLIHfpvsvkpgeevipkdengKILFDTVD--LCATWEAVEKCKDAGLAK 161
Cdd:PLN02587 86 YGegfdfsAERVTKSVDESLARLQLDYVDILHCH------------------DIEFGSLDqiVNETIPALQKLKESGKVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 162 SIGVSNFNRRQLEMILNK--PG-----LKYkpvcnqveCHPYFNQRKLLD---FCKSKDIVLVAYSALG----SHREEPW 227
Cdd:PLN02587 148 FIGITGLPLAIFTYVLDRvpPGtvdviLSY--------CHYSLNDSSLEDllpYLKSKGVGVISASPLAmgllTENGPPE 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 228 VDPNSPVLLEdpvLCALAKKH----KRTPALIALRYQL--QRGVVVLAKSYNEQRIRQNV 281
Cdd:PLN02587 220 WHPAPPELKS---ACAAAATHckekGKNISKLALQYSLsnKDISTTLVGMNSVQQVEENV 276
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
19-202 |
6.21e-05 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 44.26 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 19 LGFGTYAP--AEVPKSKALEATKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgSVKREDIFYTSKL-WCNSHRP 92
Cdd:cd19159 16 LGLGTWVTfgGQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAET 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 93 E--LVRP----ALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPK-----DENGKILFDTvdlcATWEAVEKCKDAGLAk 161
Cdd:cd19159 92 ErgLSRKhiieGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAmthviNQGMAMYWGT----SRWSAMEIMEAYSVA- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 5453543 162 sigvsnfnrRQLEMIlnkpglkyKPVCNQVECHpYFNQRKL 202
Cdd:cd19159 167 ---------RQFNMI--------PPVCEQAEYH-LFQREKV 189
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
18-202 |
2.71e-04 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); 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.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 42.05 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 18 VLGFGTYAP--AEVPKSKALEATKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgSVKREDIFYTSKL-WCNSHR 91
Cdd:cd19141 14 CLGLGTWVTfgSQISDEVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKK----GWRRSSYVITTKIfWGGKAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 92 PE--LVRP----ALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIpkdengkilfdtvdlcatwEAVEKCKDAGLAKSIGV 165
Cdd:cd19141 90 TErgLSRKhiieGLKASLERLQLEYVDIVFANRPDPNTPMEEIV-------------------RAFTHVINQGMAMYWGT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5453543 166 SNFNR----------RQLEMIlnkpglkyKPVCNQVECHpYFNQRKL 202
Cdd:cd19141 151 SRWSAmeimeaysvaRQFNLI--------PPIVEQAEYH-LFQREKV 188
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
17-295 |
4.66e-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: 41.16 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 17 PVLGFGT------YAPaeVPKSKALEATKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvKREDIFYTSK--- 84
Cdd:cd19161 1 SELGLGTaglgnlYTA--VSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREK------PRDEFVLSTKvgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 85 LWCNSHRPELVRP----------------------ALERSLKNLQLDYVDLYLIHfpvsvkPGEEVIPKDENGKILFDTv 142
Cdd:cd19161 73 LLKPAREGSVPDPngfvdplpfeivydysydgimrSFEDSLQRLGLNRIDILYVH------DIGVYTHGDRKERHHFAQ- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 143 dLCAT-WEAVEKCKDAGLAKSIGVsnfnrrqlemilnkpGLKYKPVCNQVechpyfnqRKLLDFckskDIVLVA--YSAL 219
Cdd:cd19161 146 -LMSGgFKALEELKKAGVIKAFGL---------------GVNEVQICLEA--------LDEADL----DCFLLAgrYSLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453543 220 GSHREEPWVDP--------------NSPVLLEDPV-----------------LCALAK---KHKRTPALIALRYQLQRGV 265
Cdd:cd19161 198 DQSAEEEFLPRceqrgtslviggvfNSGILATGTKsgakfnygdapaeiisrVMEIEKicdAYNVPLAAAALQFPLRHPA 277
|
330 340 350
....*....|....*....|....*....|..
gi 5453543 266 V--VLAKSYNEQRIRQNVQVFEFQLTSEEMKA 295
Cdd:cd19161 278 VasVLTGARNPAQLRQNVEAFQTDIPEELWQA 309
|
|
| |
