|
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: 703.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 6 QCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKL 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 86 WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGV 165
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 166 SNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALA 245
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20532374 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 |
7.51e-180 |
|
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: 498.94 E-value: 7.51e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 13 GHFMPVLGFGTYA-PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHR 91
Cdd:cd19109 1 GNSIPIIGLGTYSePKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 92 PELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHR 171
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 172 LLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALAKKHKRT 251
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 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 |
6.41e-139 |
|
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: 395.21 E-value: 6.41e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 10 LNDGHFMPVLGFGTY--APAEVPkskalEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKI-ADGSVKREDIFYTSKLW 86
Cdd:cd19106 1 LHTGQKMPLIGLGTWksKPGQVK-----AAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19106 76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShREEPWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGS-PDRPWAKPDEPVLLEEPKVKALAK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 20532374 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 |
4.04e-138 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 393.32 E-value: 4.04e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELV 95
Cdd:cd19107 4 MPILGLGTW---KSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 96 RPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEM 175
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 176 ILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShREEPWVDPNSPVLLEDPVLCALAKKHKRTPALI 255
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGS-PDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 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 |
1.79e-130 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 373.54 E-value: 1.79e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 7 CVKLNDGHFMPVLGFGTYApaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWK--LKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKpgeEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFK---ENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFNHRLLEMILNkpGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPwvDPNSPVLLEDPVLCALAK 246
Cdd:cd19116 157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRG--QTNPPPRLDDPTLVAIAK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 20532374 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 |
2.80e-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: 358.72 E-value: 2.80e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIadgsVKREDIFYTSKLWSNSHRPELV 95
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 96 RPALERSLKNLQLDYVDLYLIHFPVSVKPGEevipkdengkilfDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEM 175
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGG-------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 176 ILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREepwvdpnspVLLEDPVLCALAKKHKRTPALI 255
Cdd:cd19071 141 LLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR---------PLLDDPVLKEIAKKYGKTPAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 20532374 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 |
2.43e-120 |
|
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: 348.10 E-value: 2.43e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTY--APAEVPkskalEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPE 93
Cdd:cd19110 4 IPAVGLGTWkaSPGEVT-----EAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 94 LVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLL 173
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 174 EMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEpwVDpnspvLLEDPVLCALAKKHKRTPA 253
Cdd:cd19110 159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEG--VD-----LIDDPVIQRIAKKHGKSPA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 254 LIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY 323
Cdd:cd19110 232 QILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-305 |
9.62e-120 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 344.73 E-value: 9.62e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 12 DGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWSNSHR 91
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 92 PELVRPALERSLKNLQLDYVDLYLIHFPVSVkpgeevipkdengkilfdtvDLCATWEAMEKCKDAGLAKSIGVSNFNHR 171
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGPG--------------------PYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 172 LLEMILNKPGlkYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRT 251
Cdd:COG0656 134 HLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKT 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 20532374 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 |
1.00e-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: 341.31 E-value: 1.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYAPAevpKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSK---PGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGeEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 168 FNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-HREEPWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19123 160 FSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKIAE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 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 |
3.56e-115 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 335.15 E-value: 3.56e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 7 CVKLNDGHFMPVLGFGTY--APAEVpkskaLEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSK 84
Cdd:cd19154 3 SITLSNGVKMPLIGLGTWqsKGAEG-----ITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 LWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIG 164
Cdd:cd19154 78 LWTHEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 165 VSNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-----HREEPWVDPnSPVLLEDP 239
Cdd:cd19154 158 VSNFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranFTKSTGVSP-APNLLQDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20532374 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 |
2.36e-111 |
|
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: 324.68 E-value: 2.36e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 6 QCVKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKL 85
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTW---QADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 86 WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEeviPKDENGKILfdTVDLCATWEAMEKCKDAGLAKSIGV 165
Cdd:cd19125 78 WCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 166 SNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShREEPWVDPNspvLLEDPVLCALA 245
Cdd:cd19125 153 SNFSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGS-PGTTWVKKN---VLKDPIVTKVA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 20532374 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 |
3.39e-105 |
|
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: 308.81 E-value: 3.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 12 DGHFMPVLGFGTYAPAEVPKsKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVK-REDIFYTSKLWSNSH 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE-DIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 91 RPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENgkiLFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNH 170
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEE---DFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 171 RLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReEPWvdpNSPVLLEDPVLCALAKKHKR 250
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPG-TKW---GSNAVMESDVLKEIAAAKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 20532374 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 |
5.46e-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: 296.74 E-value: 5.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 7 CVKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTW---QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV-SVKPGEEVIPKDENGKILFD-TVDLCATWEAMEKCKDAGLAKSIG 164
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVgSLSKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 165 VSNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS----HREEPWVDP--NSPVLLED 238
Cdd:cd19155 160 LSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaaHFSPGTGSPsgSSPDLLQD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20532374 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 |
1.07e-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: 292.48 E-value: 1.07e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 13 GHFMPVLGFGTY--APAEVpkskaLEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSH 90
Cdd:cd19111 1 GFPMPVIGLGTYqsPPEEV-----RAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 91 RPELVRPALERSLKNLQLDYVDLYLIHFPVSVkpgeeVIPKDENGKILFDTvDLCATWEAMEKCKDAGLAKSIGVSNFNH 170
Cdd:cd19111 76 EFKDTEKSLEKSLENLKLPYVDLYLIHHPCGF-----VNKKDKGERELASS-DVTSVWRAMEALVSEGKVKSIGLSNFNP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 171 RLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-HREEPWVDPNSPVLLEDPVLCALAKKHK 249
Cdd:cd19111 150 RQINKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELD 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 20532374 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 |
6.07e-98 |
|
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: 290.47 E-value: 6.07e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 10 LNDGHFMPVLGFGTY--APAEVPKskaleAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIAD-GSVKREDIFYTSKLW 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaEPGEVGA-----AVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPK----DENGKILFDT-VDLCATWEAMEKCKDAGLAK 161
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavpTNGGEVDLDLsVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 162 SIGVSNFNHRLLEMILNKPGLkyKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREepwvdpNSPVLLEDPVL 241
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLA------GLPLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTSEEMKAIDGL 299
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-305 |
4.62e-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: 278.57 E-value: 4.62e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 11 NDGHFMPVLGFGTYAPaevPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSH 90
Cdd:cd19129 1 NGSGAIPALGFGTLIP---DPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 91 RPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDT-VDLCATWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 170 HRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGsHREEpwvdpnsPVLLEDPVLCALAKKHK 249
Cdd:cd19129 158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG-HGME-------PKLLEDPVITAIARRVN 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 20532374 250 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVfeFQLTSEEMKAI-DGLNRNVRY 305
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREInEGIKTRYRF 282
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-297 |
1.84e-92 |
|
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: 274.92 E-value: 1.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNSHRPELV 95
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 96 RPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAMEKCKDAGLAKSIGVSNFNHRLLEM 175
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEE-------------------TLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 176 ILNKPGLkyKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGsHREepwvdpnspvLLEDPVLCALAKKHKRTPALI 255
Cdd:cd19073 135 ALDISPL--PIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA-RGE----------VLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 20532374 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 |
6.76e-92 |
|
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: 274.25 E-value: 6.76e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWS 87
Cdd:cd19131 2 ITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVsvkPGEevipkdenGKIlfdtVDlcaTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PAQ--------DKY----VE---TWKALIELKKEGRVKSIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 168 FNHRLLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19131 137 FTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEK 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 20532374 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 |
1.66e-91 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 275.13 E-value: 1.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19112 3 ITLNSGHKMPVIGLGVW---RMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHrpELVRPALERSLKNLQLDYVDLYLIHFPVSVKP---GEEVIPKDENGKILFD-TVDLCATWEAMEKCKDAGLAKSI 163
Cdd:cd19112 80 SDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLDIDvTISLETTWHAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 164 GVSNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALG-SHREEPWVDPNSPvlLEDPVLC 242
Cdd:cd19112 158 GISNYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDDPVLK 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20532374 243 ALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19112 234 DLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-317 |
3.32e-91 |
|
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: 274.30 E-value: 3.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19115 5 VKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK---PGEEVIP--KDENGKILFDTVDLCATWEAMEKCKDAGLAKS 162
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 163 IGVSNFNHRLLeMILnkpgLKY---KPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALG--SHREEPWVDP-NSPVLL 236
Cdd:cd19115 162 IGVSNFSAQLL-MDL----LRYariRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqSFLELDLPGAkDTPPLF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 237 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRyltldiFAGPPN 316
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR------FNNPLN 310
|
.
gi 20532374 317 Y 317
Cdd:cd19115 311 Y 311
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-297 |
3.37e-91 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 272.95 E-value: 3.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 13 GHFMPVLGFGT----YAPAEVPKSKAL-EAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWS 87
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLvDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPelvRPALERSLKNLQLDYVDLYLIHFPVSVKPGeevipkdengkilfdTVDLCATWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19120 77 GIKDP---REALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 168 FNHRLLEMILNKPglKYKPVCNQVECHPYFN--QRKLLDFCKSKDIVLVAYSALGSHreepWVDPNSPVlleDPVLCALA 245
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPL----TRDAGGPL---DPVLEKIA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 20532374 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-301 |
2.76e-90 |
|
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: 270.91 E-value: 2.76e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 9 KLNDGHFMPVLGFGTY--APAEVPKskaleAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19117 7 KLNTGAEIPAVGLGTWqsKPNEVAK-----AVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPelVRPALERSLKNLQLDYVDLYLIHFPVSVKP-GEEVIPKDENG-KILFDTVDLCATWEAMEKCKDAGLAKSIG 164
Cdd:cd19117 78 CTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPdGNDFLFKKDDGtKDHEPDWDFIKTWELMQKLPATGKVKAIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 165 VSNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShreepwvdPNSPvLLEDPVLCAL 244
Cdd:cd19117 156 VSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS--------TNAP-LLKEPVIIKI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 20532374 245 AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTSEEMKAIDGLNR 301
Cdd:cd19117 227 AKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHK 281
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-305 |
2.93e-90 |
|
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: 272.01 E-value: 2.93e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19113 3 IKLNSGYKMPSVGFGCW---KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVK--PGEEVIPK-----DENgKILFDTVDLCATWEAMEKCKDAGLA 160
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPgfycgDGD-NFVYEDVPILDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 161 KSIGVSNFNHRLLEMILNkpGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHR----EEPWVdPNSPVLL 236
Cdd:cd19113 159 KSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSfvelNQGRA-LNTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20532374 237 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-300 |
3.31e-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: 267.38 E-value: 3.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYapaEVPK-SKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSkiadGSVKREDIFYTSKLW 86
Cdd:cd19126 1 VTLNNGTRMPWLGLGVF---QTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgeevipkdenGKILfdtvdlcATWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGK-------------DKFI-------DTWKALEKLYASGKVKAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAK 246
Cdd:cd19126 134 NFQEHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGE 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 20532374 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 300
Cdd:cd19126 201 KYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-305 |
6.45e-89 |
|
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: 266.95 E-value: 6.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 7 CVKLNDGHFMPVLGFGTYapaEVPK-SKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKL 85
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVF---KVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 86 WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEevipkdengkilfdtvdlcaTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19157 74 WNADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKE--------------------TWKALEKLYKDGRVRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 166 SNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALA 245
Cdd:cd19157 134 SNFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIA 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRY 305
Cdd:cd19157 201 EKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-300 |
1.16e-88 |
|
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: 265.98 E-value: 1.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYapaEVP-KSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPdPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgeevipkdengkilfdtvDLCATWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFN-HRLLEMILNKpglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEpwvdpnspvLLEDPVLCALA 245
Cdd:cd19133 133 NFYpDRLVDLILHN---EVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN---------LFENPVLTEIA 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 20532374 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN 300
Cdd:cd19133 201 EKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-299 |
7.48e-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: 7.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTY---APAEVpkSKALEAvklAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRP 92
Cdd:cd19136 1 MPILGLGTFrlrGEEEV--RQAVDA---ALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 93 ELVRPALERSLKNLQLDYVDLYLIHFP-VSVKPgeeviPKDENGKILfdtvdLCATWEAMEKCKDAGLAKSIGVSNFNHR 171
Cdd:cd19136 76 EKARAACLGSLERLGTDYLDLYLIHWPgVQGLK-----PSDPRNAEL-----RRESWRALEDLYKEGKLRAIGVSNYTVR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 172 LLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShreepwvdpNSPVLLEDPVLCALAKKHKRT 251
Cdd:cd19136 146 HLEELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS---------GDLRLLEDPTVLAIAKKYGRT 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 20532374 252 PALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19136 215 PAQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-299 |
4.57e-87 |
|
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: 262.46 E-value: 4.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVR 96
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 97 PALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMI 176
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 177 LNKpgLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPwvdpnSPVLLEDPVLCALAKKHKRTPALIA 256
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDG-----NLTFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 20532374 257 LRYQLQR---GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19128 232 IAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-301 |
3.58e-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: 259.51 E-value: 3.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 10 LNDGHFMPVLGFGTYApaeVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWSNS 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYP---LKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 90 HRPELVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeeviPKdeNGKILfdtvdlcATWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWPN---------PS--RDLYV-------EAWQALIEAREEGLVRSIGVSNFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 170 HRLLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREepwvdpnspvLLEDPVLCALAKKHK 249
Cdd:cd19132 136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG----------LLDEPVIKAIAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 20532374 250 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNR 301
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-299 |
1.76e-84 |
|
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: 255.92 E-value: 1.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 9 KLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGsVKREDIFYTSKLWSN 88
Cdd:cd19121 5 KLNTGASIPAVGLGTW---QAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 89 SH-RPELvrpALERSLKNLQLDYVDLYLIHFPVSVKP--GEEVIPKDENGKILFD-TVDLCATWEAMEKCKDAGLAKSIG 164
Cdd:cd19121 81 YHrRVEL---CLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 165 VSNFNHRLLEMILnkPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGShreepwvdPNSPVLLEDPVLcAL 244
Cdd:cd19121 158 VSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS--------TGSPLISDEPVV-EI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 20532374 245 AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFqlTSEEMKAIDGL 299
Cdd:cd19121 227 AKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-299 |
5.21e-83 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 251.41 E-value: 5.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 13 GHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNSHRP 92
Cdd:cd19140 5 GVRIPALGLGTY---PLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 93 ELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeeviPKDengkilfdtVDLCATWEAMEKCKDAGLAKSIGVSNFNHRL 172
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWP----------NKD---------VPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 173 LEMILNKPGLKYkpVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTP 252
Cdd:cd19140 139 LREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 20532374 253 ALIALRYQLQR-GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19140 206 AQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-305 |
1.73e-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: 1.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYapaEVPK-SKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKiadgSVKREDIFYTSKLW 86
Cdd:cd19156 1 VKLANGVEMPRLGLGVW---RVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPgeevipKDengkilfdtvdlcaTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19156 74 NSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKF------KD--------------TWKAFEKLYKEKKVRAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFNHRLLEMILNKpgLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAK 246
Cdd:cd19156 134 NFHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGK 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 20532374 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 |
5.53e-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: 249.25 E-value: 5.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYApaeVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWS 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQ---TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeevipkdengKILFDtvDLCATWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPV---------------PNDFD--RTIQAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 168 FNHRLLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS-HREEPWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19127 137 FTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvMRYGASGPTGPGDVLQDPTITGLAE 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 20532374 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 |
3.82e-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: 240.48 E-value: 3.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYAPAEvPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPelVRPALERSLKNLQLDYVDLYLIHFPVSVK-----PGEEVIPKDENGKILF-DTVDLCATWEAMEKCKDAGLAK 161
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYaASGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 162 SIGVSNFNHRLLEMILNKpgLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEpwvdpnspvLLEDPVL 241
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPLV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVfeFQLTSEEMKAIDGLNR 301
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-311 |
1.01e-77 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 239.77 E-value: 1.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 13 GHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRP 92
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 93 ELVRPALERSLKNLQLDYVDLYLIHFPVS---VKPGEEVIP---KDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPaayVDPAENYPFlwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPV--LLEDPVLCAL 244
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20532374 245 AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIF 311
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPVVY 302
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-299 |
1.09e-76 |
|
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: 235.68 E-value: 1.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 7 CVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKlaiEAGFHHIDSAHVYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSGGYSHEAVVYALK---ECGYRHIDTAKRYGCEELLGKAIK----ESGVPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGeevipkDENGKILFDTvdlcatWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19135 77 PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSG------KNVKETRAET------WRALEELYDEGLCRAIGVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFNHRLLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAK 246
Cdd:cd19135 145 NFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEPTVTELAK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 20532374 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19135 212 KYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-300 |
3.50e-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: 231.72 E-value: 3.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 10 LNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNS 89
Cdd:cd19130 4 LNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 90 HRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPgeevipkdengkilfdtvDLCATWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAG------------------NYVHTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 170 HRLLEMILNKPGLKykPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHK 249
Cdd:cd19130 139 PPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAAAHG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 20532374 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 |
4.99e-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: 228.97 E-value: 4.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTyapAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWS 87
Cdd:cd19134 3 VTLNDDNTMPVIGLGV---GELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgeevipkdENGKIlfdtVDlcaTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19134 76 PDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKY----VD---SWGGLMKLREEGLARSIGVSN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 168 FNHRLLEMILNKPGlkYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19134 138 FTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAA 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 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 |
1.71e-70 |
|
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: 220.65 E-value: 1.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 19 LGFGTYA----PAEVPKSKALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIrskiADGSVKREDIFYTSKL------ 85
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 86 WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkdengkilFDTVDLCATWEAMEKCKDAGLAKSIGV 165
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP-------------------DPDTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 166 SNFNHRLLEMILNKPglKYKPVCNQVECHPYF--NQRKLLDFCKSKDIVLVAYSALGS----------------HREEPW 227
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20532374 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 |
2.38e-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: 2.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTY--APAEVPKSkaleaVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNSHRPE 93
Cdd:cd19139 1 IPAFGLGTFrlKDDVVIDS-----VRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 94 LVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeeviPKDEngkilfdtVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLL 173
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVDLTLIHWPS---------PNDE--------VPVEEYIGALAEAKEQGLTRHIGVSNFTIALL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 174 EMILNKPGlKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPA 253
Cdd:cd19139 135 DEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPA 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 20532374 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 |
8.02e-67 |
|
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: 211.33 E-value: 8.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 9 KLNDGHFMPVLGFGTYApAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADG-SVKREDIFYTSKLWS 87
Cdd:cd19122 2 TLNNGVKIPAVGFGTFA-NEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPK-DENGK--ILFD-TVDLCATWEAMEKCKDAGLAKSI 163
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKyvILKDlTENPEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 164 GVSNFNHRLLEMILNKPglKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPwvdPNSPVLLEDPVLCA 243
Cdd:cd19122 161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVP---STGERVSENPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 20532374 244 LAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTSEEMKAID 297
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAIN 287
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-304 |
8.45e-66 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 208.00 E-value: 8.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 8 VKLNDGHFMPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWS 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVW---QASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPelVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeeviPKDENgkilfdTVDlcaTWEAMEKCKDAGLAKSIGVSN 167
Cdd:PRK11565 80 DDHKR--PREALEESLKKLQLDYVDLYLMHWPV---------PAIDH------YVE---AWKGMIELQKEGLIKSIGVCN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 168 FNHRLLEMILNKPGLKykPVCNQVECHPYFNQRKLLdfckskdivlvAYSALGSHREEPWvdpnSPV------LLEDPVL 241
Cdd:PRK11565 140 FQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLH-----------AWNATHKIQTESW----SPLaqggkgVFDQKVI 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20532374 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 |
5.42e-65 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 205.54 E-value: 5.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTYA---PAEVPKS---KALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSkiadgsVKREDIFYTSKLW 86
Cdd:cd19072 4 VPVLGLGTWGiggGMSKDYSddkKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVsvkpgeevipkdengkilfDTVDLCATWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPN-------------------PSIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFNHRLLEMILNKPGlKYKPVCNQVECHpYFNQR---KLLDFCKSKDIVLVAYSALGshREEPWVDPNSPVLLEdpvlca 243
Cdd:cd19072 139 NFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLE--KGKLSNAKGSPLLDE------ 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 20532374 244 LAKKHKRTPALIALRYQLQR-GVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19072 209 IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-312 |
1.03e-58 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 189.85 E-value: 1.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTYapaEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSNSHRPELV 95
Cdd:PRK11172 3 IPAFGLGTF---RLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 96 RPALERSLKNLQLDYVDLYLIHFPVsvkpgeeviPKDEngkilfdtVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEM 175
Cdd:PRK11172 76 IPSLKESLQKLRTDYVDLTLIHWPS---------PNDE--------VSVEEFMQALLEAKKQGLTREIGISNFTIALMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 176 ILNKPGlKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPVLCALAKKHKRTPALI 255
Cdd:PRK11172 139 AIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATPAQV 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 20532374 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 |
1.02e-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: 184.37 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 6 QCVKLNDGHFMPVLGFGTYAPAEVPKSKA--LEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIF 80
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAqeIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 81 YTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVkPGEEVIpkdengkilfdtvdlcatwEAMEKCKDAGLA 160
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGV-PLAETV-------------------AAMEELKKEGKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 161 KSIGVSNFNHRLLEMILNKPGLKyKPVCNQVECHpyFNQR----KLLDFCKSKDIVLVAYSALGSHREEPwvdpnsPVLL 236
Cdd:cd19138 134 RAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLR------RGLL 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20532374 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 |
1.64e-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: 158.12 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 13 GHFMPVLGFGTYA------PAEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSkiadgsVKREDIFYTS 83
Cdd:cd19137 1 GEKIPALGLGTWGiggfltPDYSRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 84 KLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgEEVIPKDEngkilfdtvdlcaTWEAMEKCKDAGLAKSI 163
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP------NPNIPLEE-------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 164 GVSNFNHRLLEMILNKpgLKYKPVCNQVECHPY---FNQRKLLDFCKSKDIVLVAYSALgshreepwvdpNSPVLLEDPV 240
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-----------RRGLEKTNRT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 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 |
3.80e-46 |
|
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: 158.07 E-value: 3.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 13 GHFMPVLGFGTYA-----PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSK 84
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 ---LWSNSH------RPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDENgkilfdtVDLCATWEAMEKCK 155
Cdd:cd19084 74 cglRWDGGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 156 DAGLAKSIGVSNFNhrlLEMIlnKPGLKY-KPVCNQVechPY--FNQ---RKLLDFCKSKDIVLVAYSAL------GSHR 223
Cdd:cd19084 135 KEGKIRYIGVSNFS---VEQL--EEARKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLaqglltGKYK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 224 EEPWVDPN-----SPVLLED---------PVLCALAKKHKRTPALIALRYQLQR-GV-VVLAKSYNEQRIRQNVQVFEFQ 287
Cdd:cd19084 207 KEPTFPPDdrrsrFPFFRGEnfeknleivDKLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWE 286
|
330
....*....|
gi 20532374 288 LTSEEMKAID 297
Cdd:cd19084 287 LTEEELKEID 296
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-297 |
1.03e-42 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 148.92 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTYA---------PAEVPKSkALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRskiadGSVKREDIFYTSK 84
Cdd:cd19093 3 SPLGLGTWQwgdrlwwgyGEYGDED-LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 L----WSNSHRPeLVRpALERSLKNLQLDYVDLYLIHFPVSVKPGeevipkdengkilfdtvdLCATWEAMEKCKDAGLA 160
Cdd:cd19093 77 FaplpWRLTRRS-VVK-ALKASLERLGLDSIDLYQLHWPGPWYSQ------------------IEALMDGLADAVEEGLV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 161 KSIGVSNFNHRLLEMI---LNKPGlkYKPVCNQVE---CHPYFNQRKLLDFCKSKDIVLVAYSALG----------SHR- 223
Cdd:cd19093 137 RAVGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspENPp 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20532374 224 EEPWVDPNSPVLLE--DPVLCAL---AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19093 215 PGGRRRLFGRKNLEkvQPLLDALeeiAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
17-297 |
1.98e-42 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 148.79 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGT----YAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIRSKiadgsvKREDIFYTSKL---- 85
Cdd:COG0667 14 SRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR------PRDDVVIATKVgrrm 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 86 ----WSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDENgkilfdtVDLCATWEAMEKCKDAGLAK 161
Cdd:COG0667 88 gpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP------------DPD-------TPIEETLGALDELVREGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 162 SIGVSNFN-HRLLEMILNKPGLkYKPVCNQVEchpY--FNQR---KLLDFCKSKDIVLVAYSALGS------HREEPWVD 229
Cdd:COG0667 149 YIGVSNYSaEQLRRALAIAEGL-PPIVAVQNE---YslLDRSaeeELLPAARELGVGVLAYSPLAGglltgkYRRGATFP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 230 PNS--------PVLLED-----PVLCALAKKHKRTPALIALRYQLQRGVVVL----AKSynEQRIRQNVQVFEFQLTSEE 292
Cdd:COG0667 225 EGDraatnfvqGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENLAAADLELSAED 302
|
....*
gi 20532374 293 MKAID 297
Cdd:COG0667 303 LAALD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-303 |
7.68e-42 |
|
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: 146.58 E-value: 7.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTYAPA------EVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLWS 87
Cdd:cd19085 2 SRLGLGCWQFGggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgeevipkdengkilfdTVDLCATWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSS-------------------DVPLEETMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 168 FNHRLLEMILnKPGlkyKPVCNQVECHPYFNQ--RKLLDFCKSKDIVLVAYSAL------GSHREEPWVDPN-----SPV 234
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQLPYNLLWRAieYEILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrLFR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 235 LLEDPV----------LCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRN 302
Cdd:cd19085 212 HFEPGAeeetfealekLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
.
gi 20532374 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 |
2.55e-34 |
|
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: 125.32 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTYA-PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRskiadGSVKREDIFYTSK-----LWS 87
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLK-----GRGNRDDVVIATKgghppGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHR---PELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAMEKCKDAGLAKSIG 164
Cdd:cd06660 76 PSRSrlsPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEE-------------------TLEALNELVREGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 165 VSNFNHRLLEMILN--KPGLKYKPVCNQVE---CHPYFNQRKLLDFCKSKDIVLVAYSALGshreepwvdpnspvlledp 239
Cdd:cd06660 137 VSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA------------------- 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 20532374 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 |
5.86e-31 |
|
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: 118.16 E-value: 5.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFGTYA---------PAEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvkREDIFYTSK- 84
Cdd:cd19102 3 TIGLGTWAiggggwgggWGPQDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 --LW------SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAMEKCKD 156
Cdd:cd19102 76 glLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEE-------------------AWGALAELKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 157 AGLAKSIGVSNFNHRLLEMIL-------NKPGlkYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALGS-------H 222
Cdd:cd19102 137 EGKVRAIGVSNFSVDQMKRCQaihpiasLQPP--YSLLRRGIE-------AEILPFCAEHGIGVIVYSPMQSglltgkmT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 223 REE----PWVD--PNSPVLLED---------PVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFE 285
Cdd:cd19102 208 PERvaslPADDwrRRSPFFQEPnlarnlalvDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAAD 287
|
330
....*....|....
gi 20532374 286 FQLTSEEMKAIDGL 299
Cdd:cd19102 288 LRLTPEELAEIEAL 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-299 |
1.64e-28 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 112.99 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVY-NNEEQVGLAIRSKiadgsvkREDIFYTSKLWSNSHRPEL 94
Cdd:COG1453 13 VSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWVRDPED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 95 VRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIpkDENGkilfdtvdlcaTWEAMEKCKDAGLAKSIGVSnfNHRLLE 174
Cdd:COG1453 86 MRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVL--KPGG-----------ALEALEKAKAEGKIRHIGFS--THGSLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 175 MILnkpglkykpvcNQVECHP---------YFNQR-----KLLDFCKSKDIVLVAYSALGSHReepwvdpnspvLLEDPV 240
Cdd:COG1453 151 VIK-----------EAIDTGDfdfvqlqynYLDQDnqageEALEAAAEKGIGVIIMKPLKGGR-----------LANPPE 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20532374 241 LCALAKKHKRTPALIALRYQLQR-GV-VVLAKSYNEQRIRQNVQVFE--FQLTSEEMKAIDGL 299
Cdd:COG1453 209 KLVELLCPPLSPAEWALRFLLSHpEVtTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-281 |
5.05e-28 |
|
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: 108.72 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN-EEQVGLAIRSKiadgsvkREDIFYTSKLWSNShrPELV 95
Cdd:cd19100 12 SRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGARD--YEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 96 RPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIpkDENGkilfdtvdlcaTWEAMEKCKDAGLAKSIGVSN-FNHRLLE 174
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVF--GPGG-----------ALEALLEAKEEGKIRFIGISGhSPEVLLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 175 MIlnkpglkykpvcnqvechpyfnqrKLLDFckskDIVLVAYSALGSHREEPwvdpnspvllEDPVLCALAKKHK----- 249
Cdd:cd19100 150 AL------------------------ETGEF----DVVLFPINPAGDHIDSF----------REELLPLAREKGVgviam 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 20532374 250 ------------RTPALIALRYQLQRGVVVLA----KSYNEqrIRQNV 281
Cdd:cd19100 192 kvlaggrllsgdPLDPEQALRYALSLPPVDVVivgmDSPEE--LDENL 237
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-297 |
1.10e-25 |
|
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: 104.23 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 11 NDGHFMPVLGFG--TYAPAEVPKSK--------ALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkRE 77
Cdd:cd19091 8 RSGLKVSELALGtmTFGGGGGFFGAwggvdqeeADRLVDIALDAGINFFDTADVYSEgesEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 78 DIFYTSKLW---------SNSHRPELVRpALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTW 148
Cdd:cd19091 81 DVLIATKVRgrmgegpndVGLSRHHIIR-AVEASLKRLGTDYIDLYQLHGFDALTPLEE-------------------TL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 149 EAMEKCKDAGLAKSIGVSNFNHRLLEMIL---NKPGLKyKPVCNQVechpYFN------QRKLLDFCKSKDIVLVAYSAL 219
Cdd:cd19091 141 RALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 220 GS-------HREEPWVD------------PNSPVLLEDPV--LCALAKKHKRTPALIALRYQLQR----GVVVLAKsyNE 274
Cdd:cd19091 216 AGgllsgkyRRGQPAPEgsrlrrtgfdfpPVDRERGYDVVdaLREIAKETGATPAQVALAWLLSRptvsSVIIGAR--NE 293
|
330 340
....*....|....*....|...
gi 20532374 275 QRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19091 294 EQLEDNLGAAGLSLTPEEIARLD 316
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
18-292 |
3.30e-25 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 102.54 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSKL------WSN 88
Cdd:COG4989 17 VLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLS----PSLREKIELQTKCgirlpsEAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 89 SHRP-------ELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkdengkilfDT-VDLCATWEAMEKCKDAGLA 160
Cdd:COG4989 93 DNRVkhydtskEHIIASVEGSLRRLGTDYLDLLLLHRP--------------------DPlMDPEEVAEAFDELKASGKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 161 KSIGVSNFNHRLLEMiLNKpGLKYKPVCNQVECHPYFNQ---RKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLE 237
Cdd:COG4989 153 RHFGVSNFTPSQFEL-LQS-ALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRA 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 238 dpVLCALAKKHKRTPALIALRYqLQR---GVVVLAKSYNEQRIRQNVQVFEFQLTSEE 292
Cdd:COG4989 231 --ALDELAEKYGVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-292 |
3.31e-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: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSK----LWSNSH 90
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKcgirLGDDPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 91 R---------PELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkdengkilfDT-VDLCATWEAMEKCKDAGLA 160
Cdd:cd19092 86 PgrikhydtsKEHILASVEGSLKRLGTDYLDLLLLHRP--------------------DPlMDPEEVAEAFDELVKSGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 161 KSIGVSNFNHRLLEMiLNKpGLKYKPVCNQVEC---HPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLE 237
Cdd:cd19092 146 RYFGVSNFTPSQIEL-LQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 238 dpVLCALAKKHKRTPALIALRYQLQ---RGVVVLAkSYNEQRIRQNVQVFEFQLTSEE 292
Cdd:cd19092 224 --ALEELAEEYGVTIEAIALAWLLRhpaRIQPILG-TTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
38-299 |
5.38e-25 |
|
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: 102.11 E-value: 5.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 38 VKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvKREDIFYTSK----------LWSNShrPELVRPALERSLK 104
Cdd:cd19083 39 VREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKgahkfggdgsVLNNS--PEFLRSAVEKSLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 105 NLQLDYVDLYLIHFPvsvkpgEEVIPKDEngkilfdtvdlcaTWEAMEKCKDAGLAKSIGVSNFNHRLLEMiLNKPGL-- 182
Cdd:cd19083 111 RLNTDYIDLYYIHFP------DGETPKAE-------------AVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDGYvd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 183 ----KYKPVCNQVECHpyfnqrkLLDFCKSKDIVLVAYSAL------GSHREEPWVDPN--------------SPVLLED 238
Cdd:cd19083 171 vlqgEYNLLQREAEED-------ILPYCVENNISFIPYFPLasgllaGKYTKDTKFPDNdlrndkplfkgerfSENLDKV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20532374 239 PVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19083 244 DKLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-230 |
5.86e-24 |
|
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: 98.04 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 13 GHFMPVLGFGTYAPAevpkSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSkiadgsVKREDIFYTSK--LWS 87
Cdd:cd19105 10 GLKVSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALKG------LRRDKVFLATKasPRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHfpvSVKPGEEVIPKDEngkILfdtvdlcatwEAMEKCKDAGLAKSIGVS- 166
Cdd:cd19105 80 DKKDKAELLKSVEESLKRLQTDYIDIYQLH---GVDTPEERLLNEE---LL----------EALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20532374 167 --NFNHRLLEMIlnKPG------LKYKPVcnqvecHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDP 230
Cdd:cd19105 144 hdNMAEVLQAAI--ESGwfdvimVAYNFL------NQPAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLS 207
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-285 |
6.93e-24 |
|
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: 98.02 E-value: 6.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTY-----APAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WS 87
Cdd:cd19096 1 SVLGFGTMrlpesDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSvkpgEEVIPKDENGKIlfdtvdlcatWEAMEKCKDAGLAKSIGVSn 167
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNS----PEWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 168 FnH---RLLEMILNkpglkykpvCNQVEC----HPYFNQ-----RKLLDFCKSKDIVLVAYSAL--GSHREEPwvdpnsp 233
Cdd:cd19096 140 F-HdspELLKEILD---------SYDFDFvqlqYNYLDQenqagRPGIEYAAKKGMGVIIMEPLkgGGLANNP------- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 20532374 234 vlledPVLCALAKKHKRTPALIALRYQL-QRGV-VVLAKSYNEQRIRQNVQVFE 285
Cdd:cd19096 203 -----PEALAILCGAPLSPAEWALRFLLsHPEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-288 |
1.09e-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: 98.01 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTY----APAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN-EEQVGLAIRSkiadgsVKREDIFYTSKL-----W 86
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 SNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPkdenGKILfdtvdlcatwEAMEKCKDAGLAKSIGVS 166
Cdd:cd19090 75 TADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP----GGAL----------EALLELKEEGLIKHIGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFNHRLLEMILNK-------PGLKYKPvCNQVechpyfNQRKLLDFCKSKDIVLVAYSALG----SHREEPWVDPNSPVL 235
Cdd:cd19090 141 GGPPDLLRRAIETgdfdvvlTANRYTL-LDQS------AADELLPAAARHGVGVINASPLGmgllAGRPPERVRYTYRWL 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20532374 236 LEDPV-----LCALAKKHKRTPALIALRYQLQ----RGVVVLAKsyNEQRIRQNVQVFEFQL 288
Cdd:cd19090 214 SPELLdrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNVAAAEGPL 273
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-296 |
1.48e-23 |
|
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: 98.67 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 11 NDGHFMPVLGFGT------YAPAEvPKSKALEAVKLAIEAGFHHIDSAHVY-NNEEQVGLAIrsKIADGsvKREDIFYTS 83
Cdd:cd19144 8 RNGPSVPALGFGAmglsafYGPPK-PDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWF--KQNPG--KREKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 84 K-----------LWSNShRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAME 152
Cdd:cd19144 83 KfgieknvetgeYSVDG-SPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEK-------------------TVAAMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 153 KCKDAGLAKSIGVSNFNHRLLemilnKPGLKYKPVCN-QVECHPYF-----NQRKLLDFCKSKDIVLVAYSALGS----- 221
Cdd:cd19144 143 ELVQEGKIKHIGLSECSAETL-----RRAHAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRgfltg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 222 -------------HREEPWVDP-NSPVLLE--DPvLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQV 283
Cdd:cd19144 218 airspddfeegdfRRMAPRFQAeNFPKNLElvDK-IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGA 296
|
330
....*....|...
gi 20532374 284 FEFQLTSEEMKAI 296
Cdd:cd19144 297 LKVKLTEEEEKEI 309
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-176 |
2.64e-23 |
|
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: 96.54 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTY----APAEVPKSKALEAVKLAIEAGFHHIDSAHVY-NNEEQVGLAIRSkiadgsVKREDIFYTSKLWSNS-- 89
Cdd:cd19095 1 SVLGLGTSgigrVWGVPSEAEAARLLNTALDLGINLIDTAPAYgRSEERLGRALAG------LRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 90 ------HRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIpkdengkilfdtvdlcatwEAMEKCKDAGLAKSI 163
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVL-------------------ETLEDLKAAGKVRYI 135
|
170
....*....|...
gi 20532374 164 GVSNFNHRLLEMI 176
Cdd:cd19095 136 GVSGDGEELEAAI 148
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-297 |
1.21e-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: 95.80 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTYA------PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSK--- 84
Cdd:cd19149 12 SVIGLGTWAigggpwWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATKcgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 LWSNSH----------------RPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTW 148
Cdd:cd19149 85 RWDREGgsfffvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEE-------------------TM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 149 EAMEKCKDAGLAKSIGVSNFN-------HRLLEMILNKPglKYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSAL-- 219
Cdd:cd19149 146 EALEELKRQGKIRAIGASNVSveqikeyVKAGQLDIIQE--KYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLeq 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 220 ---------------GSHRE-EPWVDPNS--PVLLEDPVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQ 279
Cdd:cd19149 217 glltgkitpdrefdaGDARSgIPWFSPENreKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEE 296
|
330
....*....|....*...
gi 20532374 280 NVQVFEFQLTSEEMKAID 297
Cdd:cd19149 297 NAKAGDIRLSAEDIATMR 314
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-289 |
2.31e-22 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 93.82 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 15 FMPVLGFGTYAPAEvPKSKALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIRSKIAD-------GSVKREDifytsK 84
Cdd:cd19088 8 AMRLTGPGIWGPPA-DREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYPDDvviatkgGLVRTGP-----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 LWSNSHRPELVRPALERSLKNLQLDYVDLYLIHfpvsvkpgeevipkdengkILFDTVDLCATWEAMEKCKDAGLAKSIG 164
Cdd:cd19088 82 WWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLH-------------------RIDPKVPFEEQLGALAELQDEGLIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 165 VSNFNHRLLEMILNKPGLkykpVCNQVECHPYFNQ-RKLLDFCKSKDIVLVAYSALGSHreepwvdpnsPVLLEDPVLCA 243
Cdd:cd19088 143 LSNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGGG----------DLAQPGGLLAE 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 20532374 244 LAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLT 289
Cdd:cd19088 209 VAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-297 |
1.60e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 92.66 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 31 KSKALEAVKLAIEAGFHHIDSAHVYNN-EEQVGLAIRSKIADGSVKREDIFYTsKLWSNSHR----PELVRPALERSLKN 105
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDAADDVQIHT-KWVPDPGEltmtRAYVEAAIDRSLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 106 LQLDYVDLYLIHFpvsvkpgeevipKDENGKILFDTVdlcatwEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPglkYK 185
Cdd:cd19101 101 LGVDRLDLVQFHW------------WDYSDPGYLDAA------KHLAELQEEGKIRHLGLTNFDTERLREILDAG---VP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 186 PVCNQVEcHPYFNQR---KLLDFCKSKDIVLVAYSALGS---------HREEPWVDPNSPV------------------- 234
Cdd:cd19101 160 IVSNQVQ-YSLLDRRpenGMAALCEDHGIKLLAYGTLAGgllsekylgVPEPTGPALETRSlqkyklmidewggwdlfqe 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20532374 235 LLEdpVLCALAKKHKRTPALIALRYQLQR----GVVVLAKsyNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19101 239 LLR--TLKAIADKHGVSIANVAVRWVLDQpgvaGVIVGAR--NSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-221 |
4.31e-21 |
|
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: 89.84 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFGTYA-----PAEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvkREDIFYTSKL---- 85
Cdd:cd19086 5 EIGFGTWGlggdwWGDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVVIATKFgnrf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 86 -----WSNSHRPELVRPALERSLKNLQLDYVDLYLIHfpvsvKPGEEVIPKDEngkilfdtvdlcaTWEAMEKCKDAGLA 160
Cdd:cd19086 78 dggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLH-----NPPDEVLDNDE-------------LFEALEKLKQEGKI 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20532374 161 KSIGVS-NFNHRLLEMILNkpglkYKPVCNQVECHPyFNQR---KLLDFCKSKDIVLVAYSALGS 221
Cdd:cd19086 140 RAYGVSvGDPEEALAALRR-----GGIDVVQVIYNL-LDQRpeeELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
33-297 |
4.90e-21 |
|
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: 91.21 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 33 KALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIRskiadGSVKREDIFYTSKL---WSNSH------RPELVRPALE 100
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALK-----EYGKRDRVVIATKVgleWDEGGevvrnsSPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 101 RSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAMEKCKDAGLAKSIGVSNFNHRLLEmilnkp 180
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWPDPLVPIEE-------------------TAEALKELLDEGKIRAIGVSNFSPEQME------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 181 glKYKPVCNQVECHPYFN------QRKLLDFCKSKDIVLVAYSAL---------GSHREEPWVD----------PNSPVL 235
Cdd:cd19148 156 --TFRKVAPLHTVQPPYNlfereiEKDVLPYARKHNIVTLAYGALcrgllsgkmTKDTKFEGDDlrrtdpkfqePRFSQY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 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 |
3.01e-20 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 89.18 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 29 VPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKIadgsvKREDIFYTSKLWSNSH---------RPELVR 96
Cdd:cd19079 32 LDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFPMGdgpngrglsRKHIMA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 97 pALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDENgkilfdtVDLCATWEAMEKCKDAGLAKSIGVSN-FNHRLLEM 175
Cdd:cd19079 107 -EVDASLKRLGTDYIDLYQIHRW------------DYE-------TPIEETLEALHDVVKSGKVRYIGASSmYAWQFAKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 176 --ILNKPGLKyKPVCNQvechPYFN------QRKLLDFCKSKDIVLVAYSALGSHR---------EEPWVDPNSPVLLED 238
Cdd:cd19079 167 lhLAEKNGWT-KFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLARGRlarpwgdttERRRSTTDTAKLKYD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20532374 239 -------PVLCA---LAKKHKRTPALIALRYQLQRGVVV-----LAKSYneqRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19079 242 yfteadkEIVDRveeVAKERGVSMAQVALAWLLSKPGVTapivgATKLE---HLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-259 |
7.93e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 88.14 E-value: 7.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 19 LGFGTY--APAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKIADGSVKREDIFYTSK--------- 84
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 -------------------------LWSNSHrPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgEEVIPKDeNGKILF 139
Cdd:cd19099 86 eplrplkyleeklgrglidvadsagLRHCIS-PAYLEDQIERSLKRLGLDTIDLYLLHNP------EEQLLEL-GEEEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 140 DTVDlcATWEAMEKCKDAGLAKSIGVSNFN----------HRLLEMIL--------NKPGLK-----YKPVCNQVECHPY 196
Cdd:cd19099 158 DRLE--EAFEALEEAVAEGKIRYYGISTWDgfrappalpgHLSLEKLVaaaeevggDNHHFKviqlpLNLLEPEALTEKN 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20532374 197 FNQRK---LLDFCKSKDIVLVAYSALGShreepwVDPNSPVLLEDPvlcaLAKKHKRTPALIALRY 259
Cdd:cd19099 236 TVKGEalsLLEAAKELGLGVIASRPLNQ------GQLLGELRLADL----LALPGGATLAQRALQF 291
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-297 |
4.81e-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: 85.73 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 42 IEAGFHHIDSAHVYNN----------EEQVGLAIRSkiadgSVKREDIFYTSKL--WSNSHRPEL----VRPALERSLKN 105
Cdd:cd19081 36 VDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKS-----RGKRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 106 LQLDYVDLYLIHFPvsvkpgeevipkDENgkilfdtVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILN---KPGL 182
Cdd:cd19081 111 LQTDYIDLYQAHWD------------DPA-------TPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 183 KyKPVCNQvechPYFN-------QRKLLDFCKSKDIVLVAYSALGS-------HREEP--------------WVDPNSPV 234
Cdd:cd19081 172 P-RYVSLQ----PEYNlvdresfEGELLPLCREEGIGVIPYSPLAGgfltgkyRSEADlpgstrrgeaakryLNERGLRI 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20532374 235 LledPVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19081 247 L---DALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
17-296 |
5.26e-18 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 82.65 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGT------YAPAEVPKSKALeaVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvkREDIFYTSK--- 84
Cdd:cd19076 13 SALGLGCmgmsafYGPADEEESIAT--LHRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RDEVVIATKfgi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 LWS-------NSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAMEKCKDA 157
Cdd:cd19076 84 VRDpgsgfrgVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEE-------------------TVGAMAELVEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 158 GLAKSIGVSNFN-------HRL-----LEMilnkpglKYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALG----- 220
Cdd:cd19076 145 GKVRYIGLSEASadtirraHAVhpitaVQS-------EYSLWTRDIE-------DEVLPTCRELGIGFVAYSPLGrgflt 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 221 ------SHREEPWVDPNSP-----------VLLEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNV 281
Cdd:cd19076 211 gaikspEDLPEDDFRRNNPrfqgenfdknlKLVE--KLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENV 288
|
330
....*....|....*
gi 20532374 282 QVFEFQLTSEEMKAI 296
Cdd:cd19076 289 GALDVVLTPEELAEI 303
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
18-291 |
1.82e-17 |
|
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: 81.10 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WSNSHR 91
Cdd:cd19074 6 ELSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 92 PE---LVRP----ALERSLKNLQLDYVDLYLIHfpvsvKPGEEViPKDEngkilfdtvdlcaTWEAMEKCKDAGLAKSIG 164
Cdd:cd19074 80 PNdrgLSRKhifeSIHASLKRLQLDYVDIYYCH-----RYDPET-PLEE-------------TVRAMDDLIRQGKILYWG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 165 VSNFN-HRLLEM--ILNKPGLkYKPVCNQVECHpYFNQRK---LLDFCKSKDIVLVAYSAL-----------------GS 221
Cdd:cd19074 141 TSEWSaEQIAEAhdLARQFGL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsRS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20532374 222 HREEPWVDPNSPVLLEDPV------LCALAKKHKRTPALIALRYQLQR-GV--VVLAKSYNEQrIRQNVQVFEFQLTSE 291
Cdd:cd19074 219 RATDEDNRDKKRRLLTDENlekvkkLKPIADELGLTLAQLALAWCLRNpAVssAIIGASRPEQ-LEENVKASGVKLSPE 296
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-294 |
7.01e-17 |
|
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: 79.52 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 16 MPVLGFGTyAPA-----EVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSkiadgsVKREDIFYTSK--- 84
Cdd:cd19163 13 VSKLGFGA-SPLggvfgPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALKG------IPRDSYYLATKvgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 ---LWSNS--HRPELVRPALERSLKNLQLDYVDLYLIHfPVSVKPGEEVIpkdengkilfdtvdLCATWEAMEKCKDAGL 159
Cdd:cd19163 86 yglDPDKMfdFSAERITKSVEESLKRLGLDYIDIIQVH-DIEFAPSLDQI--------------LNETLPALQKLKEEGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 160 AKSIGVSNFNHRLLEMILNKPG------LKYkpvcnqveCHpY--FNQR--KLLDFCKSKDIVLVAYSALG----SHREE 225
Cdd:cd19163 151 VRFIGITGYPLDVLKEVLERSPvkidtvLSY--------CH-YtlNDTSllELLPFFKEKGVGVINASPLSmgllTERGP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20532374 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 |
7.37e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 79.62 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 34 ALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSKL-WSNSHRPEL---VRPALERSLKNL 106
Cdd:cd19104 34 QIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL-------PAGPYITTKVrLDPDDLGDIggqIERSVEKSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 107 QLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTvdlcATWEAMEKCKDAGLAKSIGVSNFNH-RLLEMIL--NKPG-- 181
Cdd:cd19104 107 KRDSVDLLQLHNRIGDERDKPVGGTLSTTDVLGLG----GVADAFERLRSEGKIRFIGITGLGNpPAIRELLdsGKFDav 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 182 ------LKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGS---------HREEPwVDPNSPVLLE----DPVLc 242
Cdd:cd19104 183 qvyynlLNPSAAEARPRGWSAQDYGGIIDAAAEHGVGVMGIRVLAAgalttsldrGREAP-PTSDSDVAIDfrraAAFR- 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20532374 243 ALAKKHKRTPALIALRYQL-QRGV--VVLAKSyNEQRIRQNVQVFEF-QLTSEEMKAIDGL 299
Cdd:cd19104 261 ALAREWGETLAQLAHRFALsNPGVstVLVGVK-NREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-299 |
1.30e-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: 78.53 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 36 EAVKLAIEAGFHHIDSAHVYnneeqvGLAIRSKIAdGSV----KREDIF----YTSKLWSNSHRPelVRPALERSLKNLQ 107
Cdd:cd19103 36 AVFDKAMAAGLNLWDTAAVY------GMGASEKIL-GEFlkryPREDYIistkFTPQIAGQSADP--VADMLEGSLARLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 108 LDYVDLYLIHFPVSV-KPGEEVIPKDENGKIlfdtvdlcatweamekckdaglaKSIGVSNFNH---RLLEMILNKPGLK 183
Cdd:cd19103 107 TDYIDIYWIHNPADVeRWTPELIPLLKSGKV-----------------------KHVGVSNHNLaeiKRANEILAKAGVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 184 YKPVCNQVE-CHPYFNQRKLLDFCKSKDIVLVAYSAL-----------------GSHREEPWvdpnSPVL--LED--PVL 241
Cdd:cd19103 164 LSAVQNHYSlLYRSSEEAGILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGRAETY----NPLLpqLEEltAVM 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19103 240 AEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-282 |
1.68e-16 |
|
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: 78.36 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGT-YAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLA-------IRSKIadgsvKREDIFYTSK---- 84
Cdd:cd19082 1 SRIVLGTaDFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGAServigewLKSRG-----NRDKVVIATKgghp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 -LWSNS-HR--PELVRPALERSLKNLQLDYVDLYLIH-----FPVsvkpgEEVIpkdengkilfdtvdlcatwEAMEKCK 155
Cdd:cd19082 76 dLEDMSrSRlsPEDIRADLEESLERLGTDYIDLYFLHrddpsVPV-----GEIV-------------------DTLNELV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 156 DAGLAKSIGVSNFNH-RLLEMI--LNKPGLkYKPVCNQvechPYFN-----------------QRKLLDFCKSKDIVLVA 215
Cdd:cd19082 132 RAGKIRAFGASNWSTeRIAEANayAKAHGL-PGFAASS----PQWSlarpneppwpgptlvamDEEMRAWHEENQLPVFA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 216 YSALG----SHREEPWVDPNSPVL-----------LEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIR 278
Cdd:cd19082 207 YSSQArgffSKRAAGGAEDDSELRrvyyseenferLE--RAKELAEEKGVSPTQIALAYVLNQPfpTVPIIGPRTPEQLR 284
|
....
gi 20532374 279 QNVQ 282
Cdd:cd19082 285 DSLA 288
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
31-297 |
5.62e-16 |
|
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: 77.22 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 31 KSKALEAVKLAIEAGFHHIDSAHVY-----------------------NNEEQVGLAirSKIADGSvkrEDIFYTSKLWS 87
Cdd:cd19094 17 EAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqgrteeiigswlkkkGNRDKVVLA--TKVAGPG---EGITWPRGGGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 88 NsHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKP----GEEVIPKDENgkilfDTVDLCATWEAMEKCKDAGLAKSI 163
Cdd:cd19094 92 R-LDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfggGYYTEPSEEE-----DSVSFEEQLEALGELVKAGKIRHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 164 GVSNFN----HRLLEM--ILNKPglkyKPVCNQvecHPY--FNQRKLLDF---CKSKDIVLVAYSAL------GSHREEP 226
Cdd:cd19094 166 GLSNETpwgvMKFLELaeQLGLP----RIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLaggvltGKYLDGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 227 WVDPNSPVLL--------EDP-------VLCALAKKHKRTPALIALRYQLQR---GVVVLAKSYNEQrIRQNVQVFEFQL 288
Cdd:cd19094 239 ARPEGGRLNLfpgymaryRSPqaleavaEYVKLARKHGLSPAQLALAWVRSRpfvTSTIIGATTLEQ-LKENIDAFDVPL 317
|
....*....
gi 20532374 289 TSEEMKAID 297
Cdd:cd19094 318 SDELLAEID 326
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
41-299 |
8.00e-16 |
|
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: 76.46 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 41 AIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLW------------SNSHrpelVRPALERSLKN 105
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVFgpmgddpndrglSRRH----IRRAVEASLRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 106 LQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAMEKCKDAGLAKSIGVSNF-------------NHRL 172
Cdd:cd19087 108 LQTDYIDLYQMHHFDRDTPLEE-------------------TLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaaRRGL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 173 LEMILNKPglKYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALG---------------SHR--------EEPWVD 229
Cdd:cd19087 169 LRFVSEQP--MYNLLKRQAE-------LEILPAARAYGLGVIPYSPLAgglltgkygkgkrpeSGRlveraryqARYGLE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20532374 230 PNSPVLLEdpvLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGL 299
Cdd:cd19087 240 EYRDIAER---FEALAAEAGLTPASLALAWVLSHPAVtsPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-259 |
2.60e-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: 74.49 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 29 VPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVglairskIADGSVKREDIFYTSKL----WSNSHRPELVRPALERSLK 104
Cdd:cd19097 23 PSEKEAKKILEYALKAGINTLDTAPAYGDSEKV-------LGKFLKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 105 NLQLDYVDLYLIHfpvsvkpGEEVIPKDeNGKIlfdtvdlcatWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKY 184
Cdd:cd19097 96 RLKVDSLDGLLLH-------NPDDLLKH-GGKL----------VEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 185 kpVcnQVechPY--FNQR----KLLDFCKSKDIVLVAYSA-----LGSHREEP--WVDPNSPVLLEdpvLCALAKKHKRT 251
Cdd:cd19097 158 --I--QL---PFniLDQRflksGLLAKLKKKGIEIHARSVflqglLLMEPDKLpaKFAPAKPLLKK---LHELAKKLGLS 227
|
....*...
gi 20532374 252 PALIALRY 259
Cdd:cd19097 228 PLELALGF 235
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-297 |
8.86e-15 |
|
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: 73.41 E-value: 8.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 42 IEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLWSN----------SHRPELVRpALERSLKNLQL 108
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKYTMNrrpgdpnaggNHRKNLRR-SVEASLRRLQT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 109 DYVDLYLIHFPVSVKPGEEVIPK-DE---NGKILFdtVDLCAT--WEAmekCKDAGLAKSIGVSNF-----NHRLLEmil 177
Cdd:cd19080 113 DYIDLLYVHAWDFTTPVEEVMRAlDDlvrAGKVLY--VGISDTpaWVV---ARANTLAELRGWSPFvalqiEYSLLE--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 178 nkpglkykpvcNQVEchpyfnqRKLLDFCKSKDIVLVAYSALG-------------SHREEPWVDPNSPVLLED------ 238
Cdd:cd19080 185 -----------RTPE-------RELLPMARALGLGVTPWSPLGgglltgkyqrgeeGRAGEAKGVTVGFGKLTErnwaiv 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20532374 239 PVLCALAKKHKRTPALIALRYQLQR---GVVVLAKSYNEQrIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19080 247 DVVAAVAEELGRSAAQVALAWVRQKpgvVIPIIGARTLEQ-LKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-299 |
2.97e-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: 71.82 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLG---FGTYA-PAEVPKSKALeaVKLAIEAGFHHIDSAHVYNN---EEQVGlAIRSKIADGSV--KredifyTSKLWSN 88
Cdd:cd19075 4 ILGtmtFGSQGrFTTAEAAAEL--LDAFLERGHTEIDTARVYPDgtsEELLG-ELGLGERGFKIdtK------ANPGVGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 89 SHRPELVRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDEngkilfdTVDLCATWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19075 75 GLSPENVRKQLETSLKRLKVDKVDVFYLHAP------------DR-------STPLEETLAAIDELYKEGKFKEFGLSNY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 169 NHRLLEMILN--------KP----GLkYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSAL------GSHREEPWV-- 228
Cdd:cd19075 136 SAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLaggfltGKYKYSEDKag 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 229 ----DPNSPVL---------------LEdpVLCALAKKHKRTPALIALRY-----QLQRG---VVVLAKSyNEQRIRQNV 281
Cdd:cd19075 208 ggrfDPNNALGklyrdrywkpsyfeaLE--KVEEAAEKEGISLAEAALRWlyhhsALDGEkgdGVILGAS-SLEQLEENL 284
|
330
....*....|....*....
gi 20532374 282 Q-VFEFQLTSEEMKAIDGL 299
Cdd:cd19075 285 AaLEKGPLPEEVVKAIDEA 303
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-297 |
5.09e-14 |
|
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: 71.11 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 19 LGFG----TYAPAEVP-KSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgsvkREDIFYTSK------ 84
Cdd:cd19078 7 IGLGcmgmSHGYGPPPdKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKfgfkid 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 85 ------LWSNShRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIpkdengkilfdtvdlcatwEAMEKCKDAG 158
Cdd:cd19078 80 ggkpgpLGLDS-RPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVA-------------------GTMKELIKEG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 159 LAKSIGVSNFNhrlLEMIlnKPGLKYKPVCN-QVECHPYFN--QRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSP-- 233
Cdd:cd19078 140 KIRHWGLSEAG---VETI--RRAHAVCPVTAvQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKfd 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 234 --------------------VLLEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLTSE 291
Cdd:cd19078 215 egddraslprftpealeanqALVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPE 292
|
....*.
gi 20532374 292 EMKAID 297
Cdd:cd19078 293 ELREIE 298
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
20-297 |
9.06e-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: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 20 GFG----TYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVG--LAIRSKIADGSVKREDIFYTSKLWSNSH--- 90
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKGGLDPDtlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 91 ---RPELVRPALERSLKNL-QLDYVDLYlihfpvsvkpgeEVIPKDENgkilfdtVDLCATWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19077 89 pdgSPEAVRKSIENILRALgGTKKIDIF------------EPARVDPN-------VPIEETIKALKELVKEGKIRGIGLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 167 NFNHrllEMIlnKPGLKYKPV-CNQVECHPYFN---QRKLLDFCKSKDIVLVAYSALGS-----HREEPWVDPNSPVLLE 237
Cdd:cd19077 150 EVSA---ETI--RRAHAVHPIaAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRglltgRIKSLADIPEGDFRRH 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 238 DP---------------VLCALAKKHKRTPALIAL---RYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAID 297
Cdd:cd19077 225 LDrfngenfeknlklvdALQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
19-296 |
5.55e-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: 62.45 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 19 LGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKIadgsvkREDIFYTSK----LWSNSHR 91
Cdd:cd19145 20 MGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKfgihEIGGSGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 92 -----PELVRPALERSLKNLQLDYVDLYLIH-----FPVSVKPGE--EVIpkdENGKIlfdtvdlcatweamekcKDAGL 159
Cdd:cd19145 94 evrgdPAYVRAACEASLKRLDVDYIDLYYQHridttVPIEITMGElkKLV---EEGKI-----------------KYIGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 160 ----AKSIGVSNFNHRLLEMilnkpGLKYKPVCNQVEchpyfnqRKLLDFCKSKDIVLVAYSALGshREEPWvdpNSPVL 235
Cdd:cd19145 154 seasADTIRRAHAVHPITAV-----QLEWSLWTRDIE-------EEIIPTCRELGIGIVPYSPLG--RGFFA---GKAKL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 236 LEDPV-------------------------LCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQL 288
Cdd:cd19145 217 EELLEnsdvrkshprfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKL 296
|
....*...
gi 20532374 289 TSEEMKAI 296
Cdd:cd19145 297 TKEDLKEI 304
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-282 |
2.06e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 60.42 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 42 IEAGFHHIDSAHVYN----------NEEQVG--LAIRSKiadgsvkREDIFYTSKL---------WSNSHR---PELVRP 97
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGrwLKDRGN-------RDDVVIATKVgagprdpdgGPESPEglsAETIEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 98 ALERSLKNLQLDYVDLYLIHfpvsvkpgeevipkdengkILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEM-- 175
Cdd:cd19752 100 EIDKSLRRLGTDYIDLYYAH-------------------VDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERar 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 176 -ILNKPGLKyKPVCNQVEcHPYF---------NQR----KLLDFCKS-KDIVLVAYSAL--GSH------REEPWVDPNS 232
Cdd:cd19752 161 qIARQQGWA-EFSAIQQR-HSYLrprpgadfgVQRivtdELLDYASSrPDLTLLAYSPLlsGAYtrpdrpLPEQYDGPDS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 20532374 233 PVLLEdpVLCALAKKHKRTPALIALRYQLQR--GVV-VLAKSYNEQrIRQNVQ 282
Cdd:cd19752 239 DARLA--VLEEVAGELGATPNQVVLAWLLHRtpAIIpLLGASTVEQ-LEENLA 288
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
18-167 |
9.10e-10 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 59.10 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFGTYAPAEV-PKSKALEAVKLAIEAGFHHIDSAHVYN----------NEEQVGLAIRSKiadGSvkREDIFYTSKLW 86
Cdd:PRK10625 15 TLGLGTMTFGEQnSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKR---GS--REKLIIASKVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 ------SNSHRPEL------VRPALERSLKNLQLDYVDLYLIHFPVSvkpgeeviPKDENGKILFD------TVDLCATW 148
Cdd:PRK10625 90 gpsrnnDKGIRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWPQR--------PTNCFGKLGYSwtdsapAVSLLETL 161
|
170
....*....|....*....
gi 20532374 149 EAMEKCKDAGLAKSIGVSN 167
Cdd:PRK10625 162 DALAEQQRAGKIRYIGVSN 180
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-129 |
4.81e-09 |
|
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: 56.45 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFG---TYApAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRskiaDGSVKREDIFYTSKL-W---- 86
Cdd:cd19143 15 ALSFGswvTFG-NQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKIfWgggg 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 20532374 87 --SNSH---RPELVRpALERSLKNLQLDYVDLYLIHFPVSVKPGEEVI 129
Cdd:cd19143 90 ppPNDRglsRKHIVE-GTKASLKRLQLDYVDLVFCHRPDPATPIEETV 136
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-166 |
1.09e-08 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 55.44 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTYA---PAEVPKSKALEAVKLAIEAGFHHIDSAHVYN---NEEQVGLAIRSKiadgsvKREDIFYTSKL----- 85
Cdd:cd19162 1 PRLGLGAASlgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALARH------PRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 86 -----WSNSHRPEL------VRPALERSLKNLQLDYVDLYLIHFPvsvkpgeevipkDENgkilfDTVDLCATWEAMEKC 154
Cdd:cd19162 75 pgaagRPAGADRRFdfsadgIRRSIEASLERLGLDRLDLVFLHDP------------DRH-----LLQALTDAFPALEEL 137
|
170
....*....|..
gi 20532374 155 KDAGLAKSIGVS 166
Cdd:cd19162 138 RAEGVVGAIGVG 149
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-266 |
4.05e-08 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 53.80 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 20 GFGTYAPAEVpkskALEAVKLAIEAGFHHIDSAhvyNN--------EEQVGLAIRSkiaDGSVKREDIFYTSK----LW- 86
Cdd:cd19089 21 NFGDYTSPEE----ARELLRTAFDLGITHFDLA---NNygpppgsaEENFGRILKR---DLRPYRDELVISTKagygMWp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 ----SNSHRPELVRpALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAMEKCKDAGLAKS 162
Cdd:cd19089 91 gpygDGGSRKYLLA-SLDQSLKRMGLDYVDIFYHHRYDPDTPLEE-------------------TMTALADAVRSGKALY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 163 IGVSNFN----HRLLEmILNKpgLKYKPVCNQVechPY--FNQ---RKLLDFCKSKDIVLVAYSAL-------------- 219
Cdd:cd19089 151 VGISNYPgakaRRAIA-LLRE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIGFIAFSPLaqglltdkylngip 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 20532374 220 -GSHREEPWVDPNSPVLLEDPV-----LCALAKKHKRTPALIALRYQLQRGVV 266
Cdd:cd19089 225 pDSRRAAESKFLTEEALTPEKLeqlrkLNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-165 |
5.54e-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: 53.38 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTyAP-----AEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgsvKREDIFYTSKL--- 85
Cdd:cd19152 1 PKLGFGT-APlgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgrl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 86 ---------------WSNS-HRPEL------VRPALERSLKNLQLDYVDLYLIHFPvsvkpgEEVIPKDENgKILFDTVD 143
Cdd:cd19152 74 lvplqeveptfepgfWNPLpFDAVFdysydgILRSIEDSLQRLGLSRIDLLSIHDP------DEDLAGAES-DEHFAQAI 146
|
170 180
....*....|....*....|..
gi 20532374 144 LCAtWEAMEKCKDAGLAKSIGV 165
Cdd:cd19152 147 KGA-FRALEELREEGVIKAIGL 167
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
17-152 |
5.62e-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: 53.62 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 17 PVLGFGTYA--PAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSKL-WSNsh 90
Cdd:cd19142 14 SNVGLGTWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIyWSY-- 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20532374 91 RPE---LVRP----ALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKD----ENGKILFDTvdlCATWEAME 152
Cdd:cd19142 88 GSEergLSRKhiieSVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMsyliDNGLIMYWG---TSRWSPVE 157
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-285 |
2.24e-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: 51.51 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFGTYAPA---EVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQV-GLAIrSKIADgSVKREDIFYTSK-----LWSN 88
Cdd:cd19164 17 IFGAATFSYQyttDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL-KALRD-EFPRDTYFIITKvgrygPDDF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 89 SHRPELVRPALERSLKNLQLDYVDLYLIHfPVSVKPGEEVIpkdENGKILFdtvdlcatweameKCKDAGLAKSIGVSNF 168
Cdd:cd19164 95 DYSPEWIRASVERSLRRLHTDYLDLVYLH-DVEFVADEEVL---EALKELF-------------KLKDEGKIRNVGISGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 169 N----HRLLEMILNKPG------LKYKPVCNQVECHPYFNQRKlldFCKSKDIVLVAYSALG----SHREEPWVDPNSPV 234
Cdd:cd19164 158 PlpvlLRLAELARTTAGrpldavLSYCHYTLQNTTLLAYIPKF---LAAAGVKVVLNASPLSmgllRSQGPPEWHPASPE 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 20532374 235 LLEDPV-LCALAKKHKRTPALIALRYQLQ----RGVVVLAKSyNEQRIRQNVQVFE 285
Cdd:cd19164 235 LRAAAAkAAEYCQAKGTDLADVALRYALRewggEGPTVVGCS-NVDELEEAVEAYW 289
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
20-285 |
1.32e-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: 49.07 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 20 GFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSKL-----WSNSHR 91
Cdd:cd19153 21 ALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVgryrdSEFDYS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 92 PELVRPALERSLKNLQLDYVDLYLIH-------FPVSvkpgEEVIPkdengkilfdtvdlcatweAMEKCKDAGLAKSIG 164
Cdd:cd19153 97 AERVRASVATSLERLHTTYLDVVYLHdiefvdyDTLV----DEALP-------------------ALRTLKDEGVIKRIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 165 VSNFNHRLLEMILNK--PGlkyKPVCNQVECHPYFNQRKLLD----FCKSKDIVLVAYSALG----SHREEPWVDPNSPV 234
Cdd:cd19153 154 IAGYPLDTLTRATRRcsPG---SLDAVLSYCHLTLQDARLESdapgLVRGAGPHVINASPLSmgllTSQGPPPWHPASGE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 235 LLEdpvLCALAKKH-----KRTPALiALRYQL----QRGVVVLAKSYNEQrIRQNVQVFE 285
Cdd:cd19153 231 LRH---YAAAADAVcasveASLPDL-ALQYSLaahaGVGTVLLGPSSLAQ-LRSMLAAVD 285
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
18-281 |
1.39e-06 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 49.01 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFGTyAP-----AEVPKSKALEAVKLAIEAGFHHIDSAHVYNN---EEQVGLAIRSKiadgSVKREDIFYTSKLWSNS 89
Cdd:PLN02587 13 SVGFGA-SPlgsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTKCGRYG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 90 H----RPELVRPALERSLKNLQLDYVDLYLIHfpvsvkpgeevipkdengKILFDTVD--LCATWEAMEKCKDAGLAKSI 163
Cdd:PLN02587 88 EgfdfSAERVTKSVDESLARLQLDYVDILHCH------------------DIEFGSLDqiVNETIPALQKLKESGKVRFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 164 GVSNFNHRLLEMILNK--PG-----LKYkpvcnqveCHPYFNQRKLLD---FCKSKDIVLVAYSALG----SHREEPWVD 229
Cdd:PLN02587 150 GITGLPLAIFTYVLDRvpPGtvdviLSY--------CHYSLNDSSLEDllpYLKSKGVGVISASPLAmgllTENGPPEWH 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 20532374 230 PNSPVLLEdpvLCALAKKH----KRTPALIALRYQL--QRGVVVLAKSYNEQRIRQNV 281
Cdd:PLN02587 222 PAPPELKS---ACAAAATHckekGKNISKLALQYSLsnKDISTTLVGMNSVQQVEENV 276
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
18-202 |
4.60e-06 |
|
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: 47.44 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 18 VLGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgSVKREDIFYTSKL-WSNSHR 91
Cdd:cd19141 14 CLGLGTWVTfgSQISDEVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKK----GWRRSSYVITTKIfWGGKAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 92 PE--LVRP----ALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPK----DENGKILFDTVdlcATWEAMEKCKDAGLAK 161
Cdd:cd19141 90 TErgLSRKhiieGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAfthvINQGMAMYWGT---SRWSAMEIMEAYSVAR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 20532374 162 sigvsNFNhrlleMIlnkpglkyKPVCNQVECHpYFNQRKL 202
Cdd:cd19141 167 -----QFN-----LI--------PPIVEQAEYH-LFQREKV 188
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
19-202 |
7.45e-06 |
|
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: 46.96 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 19 LGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgSVKREDIFYTSKL-WSNSHRP 92
Cdd:cd19159 16 LGLGTWVTfgGQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAET 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 93 E--LVRP----ALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPK-----DENGKILFDTvdlcATWEAMEKCKDAGLAK 161
Cdd:cd19159 92 ErgLSRKhiieGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAmthviNQGMAMYWGT----SRWSAMEIMEAYSVAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 20532374 162 sigvsNFNhrlleMIlnkpglkyKPVCNQVECHpYFNQRKL 202
Cdd:cd19159 168 -----QFN-----MI--------PPVCEQAEYH-LFQREKV 189
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
41-297 |
1.07e-05 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 46.52 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 41 AIEAGFHHIDSAHVY-----NNEEQVGLAIRSkiaDGSVKREDIFYTSK----LW-----SNSHRPELVrPALERSLKNL 106
Cdd:PRK09912 52 AFDLGITHFDLANNYgpppgSAEENFGRLLRE---DFAAYRDELIISTKagydMWpgpygSGGSRKYLL-ASLDQSLKRM 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 107 QLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAMEKCKDAGLAKSIGVSNFN----HRLLEMI--LNKP 180
Cdd:PRK09912 128 GLEYVDIFYSHRVDENTPMEE-------------------TASALAHAVQSGKALYVGISSYSpertQKMVELLreWKIP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 181 GLKYKPVCNQVecHPYFNQRKLLDFCKSKDIVLVAYSALGS-----------------HREEPWVDPNSPVLLEDP---- 239
Cdd:PRK09912 189 LLIHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLAQglltgkylngipqdsrmHREGNKVRGLTPKMLTEAnlns 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20532374 240 --VLCALAKKHKRTPALIALRYQL--QRGVVVLAKSYNEQRIRQNVQVFE-FQLTSEEMKAID 297
Cdd:PRK09912 267 lrLLNEMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALNnLTFSTEELAQID 329
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
19-202 |
3.31e-04 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 41.89 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 19 LGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgSVKREDIFYTSKLW------- 86
Cdd:cd19160 18 LGLGTWVTfgSQISDETAEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSK----GWRRSSYVVTTKIYwggqaet 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 87 ----SNSHRPELVRPALERslknLQLDYVDLYLIHFPVSVKPGEEVIPK-----DENGKILFDTvdlcATWEAMEKCKDA 157
Cdd:cd19160 94 erglSRKHIIEGLRGSLDR----LQLEYVDIVFANRSDPNSPMEEIVRAmtyviNQGMAMYWGT----SRWSAMEIMEAY 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 20532374 158 GLAKsigvsNFNhrlleMIlnkpglkyKPVCNQVECHpYFNQRKL 202
Cdd:cd19160 166 SVAR-----QFN-----LI--------PPVCEQAEYH-LFQREKV 191
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
32-294 |
6.48e-04 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 40.85 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 32 SKALeaVKLAIEAGFHHIDSAHVY-----NNEEQVGLAIRSKIADgsvKREDIFYTSK----LWSNSH-----RPELVrP 97
Cdd:cd19151 32 SRAM--LRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKP---YRDELIISTKagytMWPGPYgdwgsKKYLI-A 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 98 ALERSLKNLQLDYVDLYLIHFPVSVKPGEEvipkdengkilfdtvdlcaTWEAMEKCKDAGLAKSIGVSNFNH------- 170
Cdd:cd19151 106 SLDQSLKRMGLDYVDIFYHHRPDPETPLEE-------------------TMGALDQIVRQGKALYVGISNYPPeeareaa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 171 RLLEMiLNKPGLKYKPVCNQVECHPyfnQRKLLDFCKSKDIVLVAYSALG---------------SHREEPWVDPNSPVL 235
Cdd:cd19151 167 AILKD-LGTPCLIHQPKYSMFNRWV---EEGLLDVLEEEGIGCIAFSPLAqglltdrylngipedSRAAKGSSFLKPEQI 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20532374 236 LEDPV-----LCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQ-VFEFQLTSEEMK 294
Cdd:cd19151 243 TEEKLakvrrLNEIAQARGQKLAQMALAWVLRNKRVtsVLIGASKPSQIEDAVGaLDNREFSEEELA 309
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
19-200 |
3.75e-03 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 38.53 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 19 LGFGTYAP--AEVPKSKALEAVKLAIEAGFHHIDSAHVY---NNEEQVGLAIRSKiadgSVKREDIFYTSKL-WSNSHRP 92
Cdd:cd19158 16 LGLGTWVTfgGQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKK----GWRRSSLVITTKIfWGGKAET 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 93 E--LVRP----ALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPK-----DENGKILFDTvdlcATWEAMEKCKDAGLAK 161
Cdd:cd19158 92 ErgLSRKhiieGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAmthviNQGMAMYWGT----SRWSSMEIMEAYSVAR 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 20532374 162 SIGVSnfnhrllemilnkpglkyKPVCNQVECHPYFNQR 200
Cdd:cd19158 168 QFNLI------------------PPICEQAEYHMFQREK 188
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
23-118 |
5.22e-03 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 38.17 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532374 23 TYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQ---VG-----------LAIRSKIADGSVKREDIFYTSKLWSN 88
Cdd:cd19146 26 KSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESerwVGewmasrgnrdeMVLATKYTTGYRRGGPIKIKSNYQGN 105
|
90 100 110
....*....|....*....|....*....|
gi 20532374 89 sHRPELvRPALERSLKNLQLDYVDLYLIHF 118
Cdd:cd19146 106 -HAKSL-RLSVEASLKKLQTSYIDILYVHW 133
|
|
| |
