|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-306 |
0e+00 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 706.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 6 QCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKL 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 86 WSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 166 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPVLCALA 245
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
4DBS_A 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYF 306
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-319 |
5.16e-178 |
|
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: 494.32 E-value: 5.16e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 13 GHFMPVLGFGTYAPPE-VPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHR 91
Cdd:cd19109 1 GNSIPIIGLGTYSEPKtTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 92 PELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 172 QLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPVLCALAKKHKRT 251
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 252 PALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNYPY 319
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-323 |
4.33e-137 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 390.63 E-value: 4.33e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGTY-APPevprSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHRPEL 94
Cdd:cd19107 4 MPILGLGTWkSPP----GQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 95 VRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLE 174
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 175 MILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQrDKRWVDPNSPVLLEDPVLCALAKKHKRTPAL 254
Cdd:cd19107 160 RILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP-DRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQ 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4DBS_A 255 IALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNYPYSDEY 323
Cdd:cd19107 239 VLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-306 |
4.47e-134 |
|
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: 382.89 E-value: 4.47e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 10 LNDGHFMPVLGFGTY--APPEVPrskalEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKI-ADGSVKREDIFYTSKLW 86
Cdd:cd19106 1 LHTGQKMPLIGLGTWksKPGQVK-----AAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19106 76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 167 NFNRRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQrDKRWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSP-DRPWAKPDEPVLLEEPKVKALAK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYF 306
Cdd:cd19106 233 KYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-303 |
8.82e-128 |
|
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: 366.61 E-value: 8.82e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 7 CVKLNDGHFMPVLGFGTYAppEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWK--LKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKpgeELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFK---ENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 167 NFNRRQLEMILNkpGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQ-RDKRWvdpNSPVLLEDPVLCALA 245
Cdd:cd19116 157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLvPRGQT---NPPPRLDDPTLVAIA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNL 303
Cdd:cd19116 232 KKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQ 289
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-297 |
2.68e-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: 2.68e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIadgsVKREDIFYTSKLWSTFHRPELV 95
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 96 RPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDEngkvifdivdlctTWEAMEKCKDAGLAKSIGVSNFNRRQLEM 175
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEARLE-------------TWRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 176 ILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKrwvdpnspvLLEDPVLCALAKKHKRTPALI 255
Cdd:cd19071 141 LLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP---------LLDDPVLKEIAKKYGKTPAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
4DBS_A 256 ALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAID 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 |
5.59e-118 |
|
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: 341.94 E-value: 5.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGTY--APPEVPrskalEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHRPE 93
Cdd:cd19110 4 IPAVGLGTWkaSPGEVT-----EAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 94 LVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQL 173
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 174 EMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKrwVDpnspvLLEDPVLCALAKKHKRTPA 253
Cdd:cd19110 159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEG--VD-----LIDDPVIQRIAKKHGKSPA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 254 LIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNYPYSDEY 323
Cdd:cd19110 232 QILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
7-306 |
7.22e-118 |
|
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: 341.70 E-value: 7.22e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 7 CVKLNDGHFMPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19154 3 SITLSNGVKMPLIGLGTW---QSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 167 NFNRRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGS----QRDKRWVDPNSPVLLEDPVLC 242
Cdd:cd19154 160 NFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgraNFTKSTGVSPAPNLLQDPIVK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
4DBS_A 243 ALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYF 306
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-306 |
8.40e-118 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 340.11 E-value: 8.40e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 12 DGHFMPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWSTFHR 91
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 92 PELVRPALENSLKKAQLDYVDLYLIHSPMSlkpgeelsptdengkvifdiVDLCTTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 172 QLEMILNKPGlkYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAKKHKRT 251
Cdd:COG0656 134 HLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKT 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
4DBS_A 252 PALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYF 306
Cdd:COG0656 201 PAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLG 255
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-306 |
4.07e-115 |
|
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: 334.76 E-value: 4.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYAPPEvprSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSKP---GEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELsPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGVGF-PESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 FNRRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGS-QRDKRWVDPNSPVLLEDPVLCALAK 246
Cdd:cd19123 160 FSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKIAE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYF 306
Cdd:cd19123 238 KHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
6-299 |
1.98e-110 |
|
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: 322.37 E-value: 1.98e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 6 QCVKLNDGHFMPVLGFGTY-APPevprSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSK 84
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWqADP----GVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 LWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGeelSPTDENGKVI-FDIVDlctTWEAMEKCKDAGLAKSI 163
Cdd:cd19125 77 LWCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKG---AHMPEPEEVLpPDIPS---TWKAMEKLVDSGKVRAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 164 GVSNFNRRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQrDKRWVDPNspvLLEDPVLCA 243
Cdd:cd19125 151 GVSNFSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSP-GTTWVKKN---VLKDPIVTK 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
4DBS_A 244 LAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 299
Cdd:cd19125 225 VAEKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-299 |
8.17e-103 |
|
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: 302.65 E-value: 8.17e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 12 DGHFMPVLGFGTYAPPEVPRSKALEVTKlAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVK-REDIFYTSKLWSTFH 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPEDIKAAVLE-AIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 91 RPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVdlcTTWEAMEKCKDAGLAKSIGVSNFNR 170
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPFDIK---GVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 171 RQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdKRWvdpNSPVLLEDPVLCALAKKHKR 250
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPG-TKW---GSNAVMESDVLKEIAAAKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
4DBS_A 251 TPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 299
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-302 |
1.72e-96 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 287.50 E-value: 1.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 5 QQCVKLNDGHFMPVLGFGTY-APPEVPrSKALEVtklAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTS 83
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWqSSPEEI-ETAVDT---ALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 84 KLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELS-PTDENGKVIFDI-VDLCTTWEAMEKCKDAGLAK 161
Cdd:cd19155 77 KLPPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSgKLDPTGEHKQDYtTDLLDIWKAMEAQVDQGLTR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 162 SIGVSNFNRRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGS----QRDKRWVDP--NSPVL 235
Cdd:cd19155 157 SIGLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaaHFSPGTGSPsgSSPDL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4DBS_A 236 LEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRN 302
Cdd:cd19155 235 LQDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKN 301
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-306 |
6.47e-96 |
|
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: 285.55 E-value: 6.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 13 GHFMPVLGFGTY-APPEVPRskalEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHR 91
Cdd:cd19111 1 GFPMPVIGLGTYqSPPEEVR----AAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 92 PELVRPALENSLKKAQLDYVDLYLIHSPMSL--KPGEELSPTDENgkvifdivDLCTTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19111 77 FKDTEKSLEKSLENLKLPYVDLYLIHHPCGFvnKKDKGERELASS--------DVTSVWRAMEALVSEGKVKSIGLSNFN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 170 RRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGS-QRDKRWVDPNSPVLLEDPVLCALAKKH 248
Cdd:cd19111 149 PRQINKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKEL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 249 KRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYF 306
Cdd:cd19111 227 DKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYF 284
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-308 |
7.51e-94 |
|
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: 280.50 E-value: 7.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 11 NDGHFMPVLGFGTYAPPEVPRSKAlevTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFH 90
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNA---VKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 91 RPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDI-VDLCTTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 170 RRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDkrwvdpnsPVLLEDPVLCALAKKHK 249
Cdd:cd19129 158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME--------PKLLEDPVITAIARRVN 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 250 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNvqvFEFQLTAED-MKAIDGLDRNLHYFNS 308
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIREN---FDISTLPEDaMREINEGIKTRYRFNS 284
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-311 |
2.63e-93 |
|
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: 279.76 E-value: 2.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTY-APPEVPRSKALEvtklAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLW 86
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWrMEPGEIKELILN----AIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFHrpELVRPALENSLKKAQLDYVDLYLIHSPMSLKP---GEELSPTDENGKV-IFDIVDLCTTWEAMEKCKDAGLAKS 162
Cdd:cd19112 79 NSDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLdIDVTISLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 163 IGVSNFnrrqlEMILNKPGLKY---KPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALG-SQRDKRWVDPNSPvlLED 238
Cdd:cd19112 157 IGISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LDD 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4DBS_A 239 PVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSF 311
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPAKF 302
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-300 |
2.01e-91 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 272.71 E-value: 2.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWS 87
Cdd:cd19131 2 ITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMslkPGEELsptdengkvifdIVDlctTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PAQDK------------YVE---TWKALIELKKEGRVKSIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 FNRRQLEMILNKPGLKykPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19131 137 FTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEK 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
4DBS_A 248 HKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD 300
Cdd:cd19131 204 HGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-305 |
1.12e-90 |
|
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: 271.41 E-value: 1.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 13 GHFMPVLGFGT-----YAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLws 87
Cdd:cd19120 1 GSKIPAIAFGTgtawyKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 tFHRPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeelsPTDENGKVifdivDLCTTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19120 75 -SPGIKDPREALRKSLAKLGVDYVDLYLIHSP----------FFAKEGGP-----TLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 FNRRQLEMILNKPglKYKPVCNQVECHPYFN--RSKLLDFCKSKDIVLVAYSALGSQrdkrWVDPNSPVlleDPVLCALA 245
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPL----TRDAGGPL---DPVLEKIA 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHY 305
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-297 |
3.48e-90 |
|
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: 269.14 E-value: 3.48e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSTFHRPELV 95
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 96 RPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSIGVSNFNRRQLEM 175
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEE-------------------TLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 176 ILNKPGLkyKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGsQRDkrwvdpnspvLLEDPVLCALAKKHKRTPALI 255
Cdd:cd19073 135 ALDISPL--PIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA-RGE----------VLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
4DBS_A 256 ALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-307 |
4.13e-90 |
|
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: 271.60 E-value: 4.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19115 5 VKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLK---PGEELSPT--DENGKVIFDIVDLCTTWEAMEKCKDAGLAKS 162
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPGwfYDGKKVEFSNAPIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 163 IGVSNFNrRQLEMILnkpgLKY---KPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPN---SPVLL 236
Cdd:cd19115 162 IGVSNFS-AQLLMDL----LRYariRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDLPGakdTPPLF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4DBS_A 237 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHyFN 307
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR-FN 306
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-299 |
5.19e-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: 270.52 E-value: 5.19e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 5 QQCVKLNDGHFMPVLGFGTY--APPEVprSKALEVtklAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYT 82
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTWqsKPNEV--AKAVEA---ALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 83 SKLWSTFHRPelVRPALENSLKKAQLDYVDLYLIHSPMSLKPG--EELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLA 160
Cdd:cd19117 74 TKLWCTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 161 KSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQrdkrwvdpNSPvLLEDPV 240
Cdd:cd19117 152 KAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGST--------NAP-LLKEPV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
4DBS_A 241 LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTAEDMKAIDGL 299
Cdd:cd19117 223 IIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDEL 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-299 |
1.73e-89 |
|
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: 268.90 E-value: 1.73e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 10 LNDGHFMPVLGFGTY--APPEVPRSkalevTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIAD-GSVKREDIFYTSKLW 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaEPGEVGAA-----VKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPT----DENGKVIFDI-VDLCTTWEAMEKCKDAGLAK 161
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavpTNGGEVDLDLsVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 162 SIGVSNFNRRQLEMILNKPGLkyKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdPNSPVLLEDPVL 241
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTAEDMKAIDGL 299
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-300 |
1.59e-88 |
|
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: 265.46 E-value: 1.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYAPPEvpRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWS 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPD--GDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKpgeelsptdengkvifdIVDlctTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19126 75 DDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDK-----------------FID---TWKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 FNRRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19126 135 FQEHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
4DBS_A 248 HKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD 300
Cdd:cd19126 202 YGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-307 |
4.40e-87 |
|
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: 263.92 E-value: 4.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19113 3 IKLNSGYKMPSVGFGCW---KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLK--PGEELSP----TDENGKVIFDIVDLCTTWEAMEKCKDAGLAK 161
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPpgfyCGDGDNFVYEDVPILDTWKALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 162 SIGVSNFNRRQLEMILNkpGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQ-----RDKRWVdpNSPVLL 236
Cdd:cd19113 160 SIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL--NTPTLF 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4DBS_A 237 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHyFN 307
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR-FN 305
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-299 |
2.25e-86 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 260.26 E-value: 2.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGTYappevpRSKALE----VTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHR 91
Cdd:cd19136 1 MPILGLGTF------RLRGEEevrqAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 92 PELVRPALENSLKKAQLDYVDLYLIHSpmslkPGEELSPTDENGKVIFDIVdlctTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19136 75 YEKARAACLGSLERLGTDYLDLYLIHW-----PGVQGLKPSDPRNAELRRE----SWRALEDLYKEGKLRAIGVSNYTVR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 172 QLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQrdkrwvdpnSPVLLEDPVLCALAKKHKRT 251
Cdd:cd19136 146 HLEELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG---------DLRLLEDPTVLAIAKKYGRT 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
4DBS_A 252 PALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 299
Cdd:cd19136 215 PAQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-300 |
1.28e-85 |
|
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: 257.89 E-value: 1.28e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYAPPevPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLWS 87
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIP--DPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLWI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSlkpgeelsptDENGkvifdivdlctTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19133 75 QDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG----------DVYG-----------AWRAMEELYKEGKIRAIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 FNRRQLEMILnkPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKrwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19133 134 FYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN---------LFENPVLTEIAEK 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
4DBS_A 248 HKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD 300
Cdd:cd19133 203 YGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-306 |
2.44e-85 |
|
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: 257.70 E-value: 2.44e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 7 CVKLNDGHFMPVLGFGTYAPPEvpRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIFYTSKLW 86
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEE--GSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEelsptdengkvifdivdlctTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19157 75 NADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKE--------------------TWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 167 NFNRRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAK 246
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAE 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYF 306
Cdd:cd19157 202 KYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRVG 261
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-301 |
2.05e-84 |
|
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: 254.89 E-value: 2.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 10 LNDGHFMPVLGFGTYAppeVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSkiadGSVKREDIFYTSKLWSTF 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYP---LKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 90 HRPELVRPALENSLKKAQLDYVDLYLIHSPMslkPGEELsptdengkvifdIVDlctTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWPN---PSRDL------------YVE---AWQALIEAREEGLVRSIGVSNFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 170 RRQLEMILNKPGLKykPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGsqRDKRwvdpnspvLLEDPVLCALAKKHK 249
Cdd:cd19132 136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG--RGSG--------LLDEPVIKAIAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
4DBS_A 250 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDR 301
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-299 |
3.85e-83 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 252.84 E-value: 3.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 9 KLNDGHFMPVLGFGTY--APPEVPrskalEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGsVKREDIFYTSKLW 86
Cdd:cd19121 5 KLNTGASIPAVGLGTWqaKAGEVK-----AAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFH-RPELvrpALENSLKKAQLDYVDLYLIHSPMSLKP--GEELSPTDENGKVIFDIV-DLCTTWEAMEKCKDAGLAKS 162
Cdd:cd19121 79 STYHrRVEL---CLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGSRDLDWDwNHVDTWKQMEKVLKTGKTKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 163 IGVSNFNRRQLEMILnkPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQrdkrwvdpNSPVLLEDPVLc 242
Cdd:cd19121 156 IGVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGST--------GSPLISDEPVV- 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
4DBS_A 243 ALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFqlTAEDMKAIDGL 299
Cdd:cd19121 225 EIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-299 |
4.81e-83 |
|
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: 252.44 E-value: 4.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVR 96
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 97 PALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMI 176
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 177 LNKpgLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGsqrdKRWVDPNSpVLLEDPVLCALAKKHKRTPALIA 256
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLG----GSYGDGNL-TFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
4DBS_A 257 LRYQLQR---GVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 299
Cdd:cd19128 232 IAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-300 |
5.85e-81 |
|
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: 246.55 E-value: 5.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYAPPevPRSKALEVTKlAIEAGFRHIDSAHLYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWS 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTP--PEETADAVAT-ALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMslkpgeelsPTDengkviFDivDLCTTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPV---------PND------FD--RTIQAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 FNRRQLEMILNKPGLKykPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPV-LLEDPVLCALAK 246
Cdd:cd19127 137 FTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGPTGPGdVLQDPTITGLAE 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
4DBS_A 247 KHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD 300
Cdd:cd19127 215 KYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-299 |
2.08e-80 |
|
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: 244.86 E-value: 2.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 13 GHFMPVLGFGTYapPEVPRsKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSTFHRP 92
Cdd:cd19140 5 GVRIPALGLGTY--PLTGE-ECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 93 ELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAE-------------------TLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 173 LEMILNKPGLKYkpVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAKKHKRTP 252
Cdd:cd19140 139 LREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
4DBS_A 253 ALIALRYQLQR-GVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 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 |
8.55e-79 |
|
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: 241.27 E-value: 8.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYAPPEvpRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWS 87
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQD--GAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSlkpgeelsptdenGKVIfdivdlcTTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19156 75 SDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVK-------------GKFK-------DTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 FNRRQLEMILNKpgLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 248 HKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHY 305
Cdd:cd19156 202 YGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-301 |
5.40e-78 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 240.09 E-value: 5.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYAPPEvPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWS 87
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPelVRPALENSLKKAQLDYVDLYLIHSPMSLK-----PGEELSPTDENGKVIFDI-VDLCTTWEAMEKCKDAGLAK 161
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAAsGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 162 SIGVSNFNRRQLEMILNKpgLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSqrdkrwvdpNSPVLLEDPVL 241
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGS---------HGAPNLKNPLV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVfeFQLTAEDMKAIDGLDR 301
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-299 |
2.54e-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: 234.53 E-value: 2.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 7 CVKLNDGHFMPVLGFGT-----YAPpevprskalEVTKLAI-EAGFRHIDSAHLYNNEEQVGLAIRskiaDGSVKREDIF 80
Cdd:cd19135 4 TVRLSNGVEMPILGLGTshsggYSH---------EAVVYALkECGYRHIDTAKRYGCEELLGKAIK----ESGVPREDLF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 81 YTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENgkvifdivdlctTWEAMEKCKDAGLA 160
Cdd:cd19135 71 LTTKLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKETRAE------------TWRALEELYDEGLC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 161 KSIGVSNFNRRQLEMILNKPGLKykPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPV 240
Cdd:cd19135 139 RAIGVSNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEPT 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
4DBS_A 241 LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 299
Cdd:cd19135 206 VTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-305 |
3.00e-75 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 233.22 E-value: 3.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 13 GHFMPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHRP 92
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 93 ELVRPALENSLKKAQLDYVDLYLIHSPMSLK---PGEELSPTDENG---KVIFDIVDLCTTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWKDKelkKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 167 NFNrrqLEMILNKpgLKY---KPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPV--LLEDPVL 241
Cdd:cd19114 158 NFN---VQLILDL--LTYakiKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
4DBS_A 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHY 305
Cdd:cd19114 233 KKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-300 |
4.65e-72 |
|
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: 223.63 E-value: 4.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 10 LNDGHFMPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSTF 89
Cdd:cd19130 4 LNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 90 HRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPgeelsptdengkvifdivDLCTTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAG------------------NYVHTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 170 RRQLEMILNKPGLKykPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAKKHK 249
Cdd:cd19130 139 PPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAAAHG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
4DBS_A 250 RTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD 300
Cdd:cd19130 206 KTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-300 |
1.05e-68 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 215.10 E-value: 1.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 8 VKLNDGHFMPVLGFGTYappEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKiadgSVKREDIFYTSKLWS 87
Cdd:cd19134 3 VTLNDDNTMPVIGLGVG---ELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSlkpgeelsptdENGKVifdiVDlctTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19134 76 PDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKY----VD---SWGGLMKLREEGLARSIGVSN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 FNRRQLEMILNKPGlkYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAKK 247
Cdd:cd19134 138 FTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAA 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
4DBS_A 248 HKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD 300
Cdd:cd19134 205 HGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLD 257
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-299 |
1.71e-68 |
|
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: 214.14 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGTYappevpRSKALEVT---KLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSTFHRP 92
Cdd:cd19139 1 IPAFGLGTF------RLKDDVVIdsvRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 93 ELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeelSPTDEngkvifdiVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19139 71 DKLLPSLEESLEKLRTDYVDLTLIHWP---------SPNDE--------VPVEEYIGALAEAKEQGLTRHIGVSNFTIAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 173 LEMILNKPGlKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAKKHKRTP 252
Cdd:cd19139 134 LDEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATP 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
4DBS_A 253 ALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 299
Cdd:cd19139 202 AQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
16-297 |
9.47e-68 |
|
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: 212.86 E-value: 9.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGTYA------PPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSkiadgsVKREDIFYTSKLW 86
Cdd:cd19072 4 VPVLGLGTWGigggmsKDYSDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFHRPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeelsptdeNgkvifDIVDLCTTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP--------------N-----PSIPIEETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 167 NFNRRQLEMILNKPGlKYKPVCNQVECHpYFNR---SKLLDFCKSKDIVLVAYSALgsQRDKRWVDPNSPVLLEdpvlca 243
Cdd:cd19072 139 NFSLEELEEAQSYLK-KGPIVANQVEYN-LFDReeeSGLLPYCQKNGIAIIAYSPL--EKGKLSNAKGSPLLDE------ 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
4DBS_A 244 LAKKHKRTPALIALRYQLQR-GVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19072 209 IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-300 |
2.24e-65 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 207.55 E-value: 2.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 19 LGFGTYA----PPEVPRSKALEVTKLAIEAGFRHIDSAHLYN---NEEQVGLAIrskiADGSVKREDIFYTSKL------ 85
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 86 WSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeelsptdengkviFDIVDLCTTWEAMEKCKDAGLAKSIGV 165
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP-------------------DPDTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 166 SNFNRRQLEMILNKPglKYKPVCNQVECHPYFNR--SKLLDFCKSKDIVLVAYSALGS----------------QRDKRW 227
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLRRRqeEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4DBS_A 228 VDPNSPVLLEDPVLCALAKKHKRTPALIALRY--QLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD 300
Cdd:pfam00248 216 KKGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-297 |
7.31e-65 |
|
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: 206.32 E-value: 7.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 9 KLNDGHFMPVLGFGTYAPPEVPRSKALEVTKlAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADG-SVKREDIFYTSKLWS 87
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEGAKGETYAAVTK-ALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPT-DENGKVIFdIVDLCT----TWEAMEKCKDAGLAKS 162
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVI-LKDLTEnpepTWRAMEEIYESGKAKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 163 IGVSNFNRRQLEMILNKPglKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDkrwVDPNSPVLLEDPVLC 242
Cdd:cd19122 160 IGVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ---VPSTGERVSENPTLN 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
4DBS_A 243 ALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEfqLTAEDMKAID 297
Cdd:cd19122 235 EVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAIN 287
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-300 |
8.03e-63 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 200.68 E-value: 8.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 3 SKQQCVKLNDGHFMPVLGFGTY-APPEVPRSKALEvtklAIEAGFRHIDSAHLYNNEEQVGLAIRSkiadGSVKREDIFY 81
Cdd:PRK11565 2 ANPTVIKLQDGNVMPQLGLGVWqASNEEVITAIHK----ALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 82 TSKLWSTFHRPelVRPALENSLKKAQLDYVDLYLIHSPMslkpgeelsPTDENgkvifdIVDlctTWEAMEKCKDAGLAK 161
Cdd:PRK11565 74 TTKLWNDDHKR--PREALEESLKKLQLDYVDLYLMHWPV---------PAIDH------YVE---AWKGMIELQKEGLIK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 162 SIGVSNFNRRQLEMILNKPGLKykPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALgSQRDKRWVDpnspvlleDPVL 241
Cdd:PRK11565 134 SIGVCNFQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPL-AQGGKGVFD--------QKVI 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
4DBS_A 242 CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD 300
Cdd:PRK11565 203 RDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLD 261
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-312 |
3.71e-58 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 188.31 E-value: 3.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGTYappevpRSK---ALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIrskiADGSVKREDIFYTSKLWSTFHRP 92
Cdd:PRK11172 3 IPAFGLGTF------RLKdqvVIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 93 ELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeelSPTDEngkvifdiVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:PRK11172 73 DKLIPSLKESLQKLRTDYVDLTLIHWP---------SPNDE--------VSVEEFMQALLEAKKQGLTREIGISNFTIAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 173 LEMILNKPGlKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCALAKKHKRTP 252
Cdd:PRK11172 136 MKQAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATP 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 253 ALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFA 312
Cdd:PRK11172 204 AQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSPEGLA 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-297 |
3.22e-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: 183.22 E-value: 3.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 6 QCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVT--KLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIF 80
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAQEIEalRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 81 YTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSlkpgeelsptdengkvifdiVDLCTTWEAMEKCKDAGLA 160
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG--------------------VPLAETVAAMEELKKEGKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 161 KSIGVSNFNRRQLEMILNKPGLKyKPVCNQVECHpYFNRS---KLLDFCKSKDIVLVAYSALGSQRDKRwvdpnsPVLLE 237
Cdd:cd19138 134 RAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN-LGSRGieyDLLPWCREHGVPVMAYSPLAQGGLLR------RGLLE 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
4DBS_A 238 DPVLCALAKKHKRTPALIALRYQL-QRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19138 206 NPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-297 |
3.79e-47 |
|
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: 159.66 E-value: 3.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 13 GHFMPVLGFGT-----YAPPEVPR-SKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSkiadgsVKREDIFYTS 83
Cdd:cd19137 1 GEKIPALGLGTwgiggFLTPDYSRdEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 84 KLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSI 163
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEE-------------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 164 GVSNFNRRQLEMILNKpgLKYKPVCNQVECHPY---FNRSKLLDFCKSKDIVLVAYSALgsqrdKRWVDPNSPVLLEdpv 240
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-----RRGLEKTNRTLEE--- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 241 lcaLAKKHKRTPALIALRYQLQR-GVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19137 206 ---IAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-297 |
2.24e-41 |
|
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: 145.75 E-value: 2.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 13 GHFMPVLGFGTYA-----PPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSK 84
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 ---LWSTFH------RPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeelsptDENgkvifdiVDLCTTWEAMEKCK 155
Cdd:cd19084 74 cglRWDGGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 156 DAGLAKSIGVSNFNRRQLEMIlnkpgLKY-KPVCNQVechPY--FNR---SKLLDFCKSKDIVLVAYSALGS-------- 221
Cdd:cd19084 135 KEGKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYGPLAQglltgkyk 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 222 -----------QRDKRWVDPNSPVLLE--DpVLCALAKKHKRTPALIALRYQLQR-GV-VVLAKSYNEQRIRQNVQVFEF 286
Cdd:cd19084 207 keptfppddrrSRFPFFRGENFEKNLEivD-KLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDW 285
|
330
....*....|.
4DBS_A 287 QLTAEDMKAID 297
Cdd:cd19084 286 ELTEEELKEID 296
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-297 |
5.84e-41 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 144.29 E-value: 5.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTYA---------PPEVPRSkALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRskiadGSVKREDIFYTSK 84
Cdd:cd19093 3 SPLGLGTWQwgdrlwwgyGEYGDED-LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 LWSTFHR--PELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGeelsptdengkvifdivdLCTTWEAMEKCKDAGLAKS 162
Cdd:cd19093 77 FAPLPWRltRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQ------------------IEALMDGLADAVEEGLVRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 163 IGVSNFNRRQLEMI---LNKPGlkYKPVCNQVE---CHPYFNRSKLLDFCKSKDIVLVAYS--ALGS----------QRD 224
Cdd:cd19093 139 VGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSplAQGLltgkyspenpPPG 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4DBS_A 225 KRWVDPNSPVLLE-DPVLCAL---AKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19093 217 GRRRLFGRKNLEKvQPLLDALeeiAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
17-297 |
9.65e-41 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 144.55 E-value: 9.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGT----YAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYN---NEEQVGLAIRSKiadgsvKREDIFYTSKLWSTF 89
Cdd:COG0667 14 SRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR------PRDDVVIATKVGRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 90 --------HRPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeelsptDENgkvifdiVDLCTTWEAMEKCKDAGLAK 161
Cdd:COG0667 88 gpgpngrgLSREHIRRAVEASLRRLGTDYIDLYQLHRP------------DPD-------TPIEETLGALDELVREGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 162 SIGVSNFNRRQLEMILNKPGLKYKPVCNQVEchpY--FNRS---KLLDFCKSKDIVLVAYSALGS--------------Q 222
Cdd:COG0667 149 YIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAARELGVGVLAYSPLAGglltgkyrrgatfpE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 223 RDKRWVDPNSPVLLED-----PVLCALAKKHKRTPALIALRYQLQRGVVVL----AKSynEQRIRQNVQVFEFQLTAEDM 293
Cdd:COG0667 226 GDRAATNFVQGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENLAAADLELSAEDL 303
|
....
4DBS_A 294 KAID 297
Cdd:COG0667 304 AALD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-303 |
2.99e-39 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 140.03 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGT------YAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLWS 87
Cdd:cd19085 2 SRLGLGCwqfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEE-------------------TMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 FNRRQLEMILnKPGlkyKPVCNQVechPY--FNRSK---LLDFCKSKDIVLVAYSAL-----------------GSQRDK 225
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQL---PYnlLWRAIeyeILPFCREHGIGVLAYSPLaqglltgkfssaedfppGDARTR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 226 RWV---DPNSPVLLED-PVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 299
Cdd:cd19085 209 LFRhfePGAEEETFEAlEKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
....
4DBS_A 300 DRNL 303
Cdd:cd19085 289 SDPL 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-282 |
1.00e-31 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 118.39 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTYA-PPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRskiadGSVKREDIFYTSKLWSTFHR- 91
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLK-----GRGNRDDVVIATKGGHPPGGd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 92 -------PELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSIG 164
Cdd:cd06660 76 psrsrlsPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEE-------------------TLEALNELVREGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 165 VSNFNRRQLEMILN--KPGLKYKPVCNQVEcHPYFNRS----KLLDFCKSKDIVLVAYSALGsqrdkrwvdpnspvlled 238
Cdd:cd06660 137 VSNWSAERLAEALAyaKAHGLPGFAAVQPQ-YSLLDRSpmeeELLDWAEENGLPLLAYSPLA------------------ 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
4DBS_A 239 pvlcalakkhkRTPALIALRYQLQR--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 |
5.04e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 110.46 E-value: 5.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFGTYA----------PPEVPRsKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvkREDIFYTSK 84
Cdd:cd19102 3 TIGLGTWAiggggwgggwGPQDDR-DSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 ---LW------STFHRPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeelSPTDengkvifDIVDlctTWEAMEKCK 155
Cdd:cd19102 75 cglLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWP---------DPDE-------PIEE---AWGALAELK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 156 DAGLAKSIGVSNFNRRQLEMILnkpglKYKPV-CNQVechPY--FNR---SKLLDFCKSKDIVLVAYSALGS-------- 221
Cdd:cd19102 136 EEGKVRAIGVSNFSVDQMKRCQ-----AIHPIaSLQP---PYslLRRgieAEILPFCAEHGIGVIVYSPMQSglltgkmt 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 222 -QRDKR-WVD---PNSPVLLED---------PVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFE 285
Cdd:cd19102 208 pERVASlPADdwrRRSPFFQEPnlarnlalvDALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAAD 287
|
330
....*....|....
4DBS_A 286 FQLTAEDMKAIDGL 299
Cdd:cd19102 288 LRLTPEELAEIEAL 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-304 |
6.11e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 105.67 E-value: 6.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLY-NNEEQVGLAIRSKiadgsvkREDIFYTSKLWSTFHRPEL 94
Cdd:COG1453 13 VSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWVRDPED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 95 VRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsPTDENGkvifdivdlctTWEAMEKCKDAGLAKSIGVSNFNRRQL- 173
Cdd:COG1453 86 MRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEK--VLKPGG-----------ALEALEKAKAEGKIRHIGFSTHGSLEVi 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 174 ---------EMILnkpgLKYKPVcNQvechPYFNRSKLLDFCKSKDIVLVAYSALGSQRdkrwvdpnspvLLEDPVLCAL 244
Cdd:COG1453 153 keaidtgdfDFVQ----LQYNYL-DQ----DNQAGEEALEAAAEKGIGVIIMKPLKGGR-----------LANPPEKLVE 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
4DBS_A 245 AKKHKRTPALIALRYQLQR-GV-VVLAKSYNEQRIRQNVQVFE--FQLTAEDMKAIDGLDRNLH 304
Cdd:COG1453 213 LLCPPLSPAEWALRFLLSHpEVtTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERLAEELG 276
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-291 |
7.64e-26 |
|
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: 103.79 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTY----APPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN-EEQVGLAIRSkiadgsVKREDIFYTSKLwSTFHR 91
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKV-GRLPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 92 ------PELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPtdenGKVIfdivdlcttwEAMEKCKDAGLAKSIGV 165
Cdd:cd19090 74 dtadysADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP----GGAL----------EALLELKEEGLIKHIGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 166 S----NFNRR-----QLEMILnkPGLKYKPvCNQVechpyfNRSKLLDFCKSKDIVLVAYSALG----SQRDKRWVDPNS 232
Cdd:cd19090 140 GggppDLLRRaietgDFDVVL--TANRYTL-LDQS------AADELLPAAARHGVGVINASPLGmgllAGRPPERVRYTY 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 233 PVLLEDPV-----LCALAKKHKRTPALIALRYQLQ----RGVVVLAKsyNEQRIRQNVQVFEFQLTAE 291
Cdd:cd19090 211 RWLSPELLdrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNVAAAEGPLPEE 276
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
32-292 |
5.12e-25 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 102.15 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 32 SKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSK---------LWSTFHR----PELV 95
Cdd:COG4989 31 AEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLS----PSLREKIELQTKcgirlpseaRDNRVKHydtsKEHI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 96 RPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSptdengkvifdivdlcttwEAMEKCKDAGLAKSIGVSNFNRRQLEM 175
Cdd:COG4989 107 IASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVA-------------------EAFDELKASGKVRHFGVSNFTPSQFEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 176 iLNKpGLKYKPVCNQVECHPYFN---RSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEdpVLCALAKKHKRTP 252
Cdd:COG4989 168 -LQS-ALDQPLVTNQIELSLLHTdafDDGTLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRA--ALDELAEKYGVSP 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
4DBS_A 253 ALIALRYqLQR---GVVVLAKSYNEQRIRQNVQVFEFQLTAED 292
Cdd:COG4989 244 EAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-292 |
7.48e-25 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 101.48 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSK---------- 84
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKcgirlgddpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 LWSTFH---RPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSptdengkvifdivdlcttwEAMEKCKDAGLAK 161
Cdd:cd19092 86 PGRIKHydtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVA-------------------EAFDELVKSGKVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 162 SIGVSNFNRRQLEMiLNKpGLKYKPVCNQVEC---HPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEd 238
Cdd:cd19092 147 YFGVSNFTPSQIEL-LQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA- 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
4DBS_A 239 pVLCALAKKHKRTPALIALRYQLQ---RGVVVLAkSYNEQRIRQNVQVFEFQLTAED 292
Cdd:cd19092 224 -ALEELAEEYGVTIEAIALAWLLRhpaRIQPILG-TTNPERIRSAVKALDIELTREE 278
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-281 |
1.52e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 99.48 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN-EEQVGLAIRSKiadgsvkREDIFYTSKLWStfHRPELV 95
Cdd:cd19100 12 SRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGA--RDYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 96 RPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsPTDENGkvifdivdlctTWEAMEKCKDAGLAKSIGVSnfnrrqlem 175
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQ--VFGPGG-----------ALEALLEAKEEGKIRFIGIS--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 176 ilnkpglkykpvcnqveCHpyfNRSKLLDFCKSK--DIVLVAYSALGSQRDKRwvdpnspvllEDPVLCALAKKHK---- 249
Cdd:cd19100 141 -----------------GH---SPEVLLRALETGefDVVLFPINPAGDHIDSF----------REELLPLAREKGVgvia 190
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
4DBS_A 250 -------------RTPALIALRYQLQRGVVVLA----KSYNEqrIRQNV 281
Cdd:cd19100 191 mkvlaggrllsgdPLDPEQALRYALSLPPVDVVivgmDSPEE--LDENL 237
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
19-299 |
4.08e-24 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 99.80 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 19 LGFGTYAP------PEVPRSKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvKREDIFYTSKLWSTF 89
Cdd:cd19083 14 IGLGTNAVgghnlyPNLDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 90 --------HRPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgEELSPTDEngkvifdivdlctTWEAMEKCKDAGLAK 161
Cdd:cd19083 88 ggdgsvlnNSPEFLRSAVEKSLKRLNTDYIDLYYIHFP------DGETPKAE-------------AVGALQELKDEGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 162 SIGVSNFNRRQLEMiLNKPGlkykpvcnQVEC--HPY--FNR---SKLLDFCKSKDIVLV-----AYSALGSQRDKRWVD 229
Cdd:cd19083 149 AIGVSNFSLEQLKE-ANKDG--------YVDVlqGEYnlLQReaeEDILPYCVENNISFIpyfplASGLLAGKYTKDTKF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 230 PNSPVLLEDPV---------------LCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTAED 292
Cdd:cd19083 220 PDNDLRNDKPLfkgerfsenldkvdkLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEE 299
|
....*..
4DBS_A 293 MKAIDGL 299
Cdd:cd19083 300 IAFIDAL 306
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-289 |
1.17e-23 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 97.29 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 15 FMPVLGFGTYAPPEvPRSKALEVTKLAIEAGFRHIDSAHLYN---NEEQVGLAIRSKIAD-------GSVKREDifytsK 84
Cdd:cd19088 8 AMRLTGPGIWGPPA-DREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPYPDDvviatkgGLVRTGP-----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 LWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSIG 164
Cdd:cd19088 82 WWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEE-------------------QLGALAELQDEGLIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 165 VSNFNRRQLEMILNKPGLkykpVCNQVECHPYfNRS--KLLDFCKSKDIVLVAYSALGSQRDkrwvdpnspvLLEDPVLC 242
Cdd:cd19088 143 LSNVTVAQIEEARAIVRI----VSVQNRYNLA-NRDdeGVLDYCEAAGIAFIPWFPLGGGDL----------AQPGGLLA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
4DBS_A 243 ALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLT 289
Cdd:cd19088 208 EVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-296 |
5.14e-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: 97.13 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 11 NDGHFMPVLGFGT------YAPPEvPRSKALEVTKLAIEAGFRHIDSAHLY-NNEEQVGLAIrsKIADGsvKREDIFYTS 83
Cdd:cd19144 8 RNGPSVPALGFGAmglsafYGPPK-PDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWF--KQNPG--KREKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 84 KL----------WSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEelsptdengkvifdivdlcTTWEAMEK 153
Cdd:cd19144 83 KFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIE-------------------KTVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 154 CKDAGLAKSIGVSNFNRRQLemilnKPGLKYKPVCN-QVECHPYF-----NRSKLLDFCKSKDIVLVAYSALG------- 220
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETL-----RRAHAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGrgfltga 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 221 --SQRD----------KRWVDPNSPVLLE--DPvLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVF 284
Cdd:cd19144 219 irSPDDfeegdfrrmaPRFQAENFPKNLElvDK-IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGAL 297
|
330
....*....|..
4DBS_A 285 EFQLTAEDMKAI 296
Cdd:cd19144 298 KVKLTEEEEKEI 309
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-169 |
1.85e-22 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 94.22 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTY----APPEVPRSKALEVTKLAIEAGFRHIDSAHLY-NNEEQVGLAIRSkiadgsVKREDIFYTSKLWSTF-- 89
Cdd:cd19095 1 SVLGLGTSgigrVWGVPSEAEAARLLNTALDLGINLIDTAPAYgRSEERLGRALAG------LRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 90 ------HRPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeelSPTDENGKVIfdivdlcttwEAMEKCKDAGLAKSI 163
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGP---------SDDELTGEVL----------ETLEDLKAAGKVRYI 135
|
....*.
4DBS_A 164 GVSNFN 169
Cdd:cd19095 136 GVSGDG 141
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-297 |
2.13e-22 |
|
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: 95.37 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 11 NDGHFMPVLGFG--TYAPPEVPRSK--------ALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkRE 77
Cdd:cd19091 8 RSGLKVSELALGtmTFGGGGGFFGAwggvdqeeADRLVDIALDAGINFFDTADVYSEgesEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 78 DIFYTSKLWSTF---------HRPELVRpALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTW 148
Cdd:cd19091 81 DVLIATKVRGRMgegpndvglSRHHIIR-AVEASLKRLGTDYIDLYQLHGFDALTPLEE-------------------TL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 149 EAMEKCKDAGLAKSIGVSNFNRRQLEMIL---NKPGLKyKPVCNQVechpYFN---RS---KLLDFCKSKDIVLVAYSAL 219
Cdd:cd19091 141 RALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgRDlehELMPLALDQGVGLLVWSPL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 220 -----------------GSQRDKRWVD--PNSPVLLEDPV--LCALAKKHKRTPALIALRYQLQR----GVVVLAKsyNE 274
Cdd:cd19091 216 aggllsgkyrrgqpapeGSRLRRTGFDfpPVDRERGYDVVdaLREIAKETGATPAQVALAWLLSRptvsSVIIGAR--NE 293
|
330 340
....*....|....*....|...
4DBS_A 275 QRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19091 294 EQLEDNLGAAGLSLTPEEIARLD 316
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
33-297 |
2.69e-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: 91.98 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 33 KALEVTKLAIEAGFRHIDSAHLYN---NEEQVGLAIRskiadGSVKREDIFYTSKL---WSTFH------RPELVRPALE 100
Cdd:cd19148 26 EAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALK-----EYGKRDRVVIATKVgleWDEGGevvrnsSPARIRKEVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 101 NSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSIGVSNFNRRQLEmilnkp 180
Cdd:cd19148 101 DSLRRLQTDYIDLYQVHWPDPLVPIEE-------------------TAEALKELLDEGKIRAIGVSNFSPEQME------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 181 glKYKPVCNQVECHPYFN------RSKLLDFCKSKDIVLVAYSAL------GSQR--------DKRWVDPN------SPV 234
Cdd:cd19148 156 --TFRKVAPLHTVQPPYNlfereiEKDVLPYARKHNIVTLAYGALcrgllsGKMTkdtkfegdDLRRTDPKfqeprfSQY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4DBS_A 235 LLEDPVLCALAKKH--KRTPALiALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19148 234 LAAVEELDKLAQERygKSVIHL-AVRWLLDQPgvSIALWGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-297 |
6.08e-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: 91.12 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 31 RSKALEVTKLAIEAGFRHIDSAHLYNN-EEQVGLAIRSKIADGSVKREDIFYTSklWSTFHR-----PELVRPALENSLK 104
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDAADDVQIHTK--WVPDPGeltmtRAYVEAAIDRSLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 105 KAQLDYVDLYLIHspmslkpgeeLSPTDENGKVifdivdlcTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPglkY 184
Cdd:cd19101 100 RLGVDRLDLVQFH----------WWDYSDPGYL--------DAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---V 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 185 KPVCNQVEcHPYFNR---SKLLDFCKSKDIVLVAYSALGS---------QRDKRWVDPNSPV------------------ 234
Cdd:cd19101 159 PIVSNQVQ-YSLLDRrpeNGMAALCEDHGIKLLAYGTLAGgllsekylgVPEPTGPALETRSlqkyklmidewggwdlfq 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 235 -LLEdpVLCALAKKHKRTPALIALRYQLQR----GVVVLAKsyNEQRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19101 238 eLLR--TLKAIADKHGVSIANVAVRWVLDQpgvaGVIVGAR--NSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-285 |
6.45e-21 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 89.93 E-value: 6.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTY-----APPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WS 87
Cdd:cd19096 1 SVLGFGTMrlpesDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSlkpgEELSPTDENGKVifdivdlcttWEAMEKCKDAGLAKSIGVSn 167
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNS----PEWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 F--NRRQLEMILNkpglkykpvCNQVEC----HPYFN-----RSKLLDFCKSKDIVLVAYSALgsqRDKRWVDPNSPVLl 236
Cdd:cd19096 140 FhdSPELLKEILD---------SYDFDFvqlqYNYLDqenqaGRPGIEYAAKKGMGVIIMEPL---KGGGLANNPPEAL- 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
4DBS_A 237 edpvlcALAKKHKRTPALIALRYQL-QRGV-VVLAKSYNEQRIRQNVQVFE 285
Cdd:cd19096 207 ------AILCGAPLSPAEWALRFLLsHPEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-230 |
1.12e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 89.18 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 13 GHFMPVLGFGTYAPPevprSKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSkiadgsVKREDIFYTSK--LWS 87
Cdd:cd19105 10 GLKVSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALKG------LRRDKVFLATKasPRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 88 TFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEelsptdENGKVIfdivdlcttwEAMEKCKDAGLAKSIGVS- 166
Cdd:cd19105 80 DKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERL------LNEELL----------EALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4DBS_A 167 NFNrrQLEMILnkpglkykpvcNQVECHPY------FN-------RSKLLDFCKSKDIVLVAYSALGSQRDKRWVDP 230
Cdd:cd19105 144 HDN--MAEVLQ-----------AAIESGWFdvimvaYNflnqpaeLEEALAAAAEKGIGVVAMKTLAGGYLQPALLS 207
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-297 |
1.12e-19 |
|
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: 87.71 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTYA------PPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSK--- 84
Cdd:cd19149 12 SVIGLGTWAigggpwWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATKcgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 LWST----FH------------RPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTW 148
Cdd:cd19149 85 RWDReggsFFfvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEE-------------------TM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 149 EAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGL-----KYKPVCNQVEchpyfnrSKLLDFCKSKDIVLVAYSAL---- 219
Cdd:cd19149 146 EALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLdiiqeKYSMLDRGIE-------KELLPYCKKNNIAFQAYSPLeqgl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 220 --------------GSQRDKRWVDPNS--PVLLEDPVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNV 281
Cdd:cd19149 219 ltgkitpdrefdagDARSGIPWFSPENreKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENA 298
|
330
....*....|....*.
4DBS_A 282 QVFEFQLTAEDMKAID 297
Cdd:cd19149 299 KAGDIRLSAEDIATMR 314
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
17-296 |
3.28e-19 |
|
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: 86.12 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGT------YAPPevPRSKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvkREDIFYTSK--- 84
Cdd:cd19076 13 SALGLGCmgmsafYGPA--DEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RDEVVIATKfgi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 LWSTFH-------RPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDA 157
Cdd:cd19076 84 VRDPGSgfrgvdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEE-------------------TVGAMAELVEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 158 GLAKSIGVSNFN----RR----------QLEmilnkpglkYKPVCNQVECHpyfnrskLLDFCKSKDIVLVAYSALG--- 220
Cdd:cd19076 145 GKVRYIGLSEASadtiRRahavhpitavQSE---------YSLWTRDIEDE-------VLPTCRELGIGFVAYSPLGrgf 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 221 ----------------SQRDKRWV----DPNSPVLLEdpvLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIR 278
Cdd:cd19076 209 ltgaikspedlpeddfRRNNPRFQgenfDKNLKLVEK---LEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLE 285
|
330
....*....|....*...
4DBS_A 279 QNVQVFEFQLTAEDMKAI 296
Cdd:cd19076 286 ENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-297 |
6.46e-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: 85.34 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 42 IEAGFRHIDSAHLYNN----------EEQVGLAIRSkiadgSVKREDIFYTSKL--WSTFHRPEL----VRPALENSLKK 105
Cdd:cd19081 36 VDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKS-----RGKRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 106 AQLDYVDLYLIHSPmslkpgEELSPTDEngkvifdivdlctTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILN---KPGL 182
Cdd:cd19081 111 LQTDYIDLYQAHWD------DPATPLEE-------------TLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 183 KyKPVCNQVEchpY--FNRSK----LLDFCKSKDIVLVAYSALGS---------------------QRDKRWVDPNSPVL 235
Cdd:cd19081 172 P-RYVSLQPE---YnlVDRESfegeLLPLCREEGIGVIPYSPLAGgfltgkyrseadlpgstrrgeAAKRYLNERGLRIL 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
4DBS_A 236 ledPVLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19081 248 ---DALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
29-297 |
1.92e-18 |
|
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: 84.17 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 29 VPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKIadgsvKREDIFYTSKLwstFHRpelVRP-------- 97
Cdd:cd19079 32 LDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKV---YFP---MGDgpngrgls 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 98 ------ALENSLKKAQLDYVDLYLIHSPmslkpgeelsptDENgkvifdiVDLCTTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19079 101 rkhimaEVDASLKRLGTDYIDLYQIHRW------------DYE-------TPIEETLEALHDVVKSGKVRYIGASSMYAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 172 QLEMILN---KPGLKyKPVCNQvechPYFN-------RsKLLDFCKSKDIVLVAYSALGSQR---------DKRWVDPNS 232
Cdd:cd19079 162 QFAKALHlaeKNGWT-KFVSMQ----NHYNllyreeeR-EMIPLCEEEGIGVIPWSPLARGRlarpwgdttERRRSTTDT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 233 PVLLED-------PVLCA---LAKKHKRTPALIALRYQLQRGVVV-----LAKSYneqRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19079 236 AKLKYDyfteadkEIVDRveeVAKERGVSMAQVALAWLLSKPGVTapivgATKLE---HLEDAVAALDIKLSEEEIKYLE 312
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
18-291 |
5.69e-18 |
|
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: 82.64 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFGTYAP--PEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSkiadgsVKREDIFYTSKL-WSTFHR 91
Cdd:cd19074 6 ELSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 92 PE---LVRP----ALENSLKKAQLDYVDLYLIHSPmslkpgEELSPTDEngkvifdivdlctTWEAMEKCKDAGLAKSIG 164
Cdd:cd19074 80 PNdrgLSRKhifeSIHASLKRLQLDYVDIYYCHRY------DPETPLEE-------------TVRAMDDLIRQGKILYWG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 165 VSNFNRRQLE--MILNKPGLKYKPVCNQVECHpYFNRSK---LLDFCKSKDIVLVAYSAL-------------------- 219
Cdd:cd19074 141 TSEWSAEQIAeaHDLARQFGLIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsrsr 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 220 -GSQRDKRWVDPnspvLLEDPV------LCALAKKHKRTPALIALRYQLQR-GV--VVLAKSYNEQrIRQNVQVFEFQLT 289
Cdd:cd19074 220 aTDEDNRDKKRR----LLTDENlekvkkLKPIADELGLTLAQLALAWCLRNpAVssAIIGASRPEQ-LEENVKASGVKLS 294
|
..
4DBS_A 290 AE 291
Cdd:cd19074 295 PE 296
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-259 |
4.76e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 80.05 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 19 LGFGTY--APPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKIADGSVKREDIFYTSK--------- 84
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 -------------------------LWSTFHrPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeELSPTDENGKVIF 139
Cdd:cd19099 86 eplrplkyleeklgrglidvadsagLRHCIS-PAYLEDQIERSLKRLGLDTIDLYLLHNP-------EEQLLELGEEEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 140 DIVDLctTWEAMEKCKDAGLAKSIGVSNFN------------------RRQLEMILNKPGLKYkpVcnQVECHPY----- 196
Cdd:cd19099 158 DRLEE--AFEALEEAVAEGKIRYYGISTWDgfrappalpghlsleklvAAAEEVGGDNHHFKV--I--QLPLNLLepeal 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 197 -------FNRSKLLDFCKSKDIVLVAYSALGSQRDKRwvdpnspvllEDPVLCALAKKHKRTPALIALRY 259
Cdd:cd19099 232 tekntvkGEALSLLEAAKELGLGVIASRPLNQGQLLG----------ELRLADLLALPGGATLAQRALQF 291
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-259 |
5.73e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 79.11 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 29 VPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVglairskIADGSVKREDIFYTSKL----WSTFHRPELVRPALENSLK 104
Cdd:cd19097 23 PSEKEAKKILEYALKAGINTLDTAPAYGDSEKV-------LGKFLKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 105 KAQLDYVDLYLIHSPMSLkpgeelsptDENGKVIfdivdlcttWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKY 184
Cdd:cd19097 96 RLKVDSLDGLLLHNPDDL---------LKHGGKL---------VEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 185 kpVcnQVECHPY---FNRSKLLDFCKSKDIVLVAYSA-----LGSQRDKR--WVDPNSPVLLEdpvLCALAKKHKRTPAL 254
Cdd:cd19097 158 --I--QLPFNILdqrFLKSGLLAKLKKKGIEIHARSVflqglLLMEPDKLpaKFAPAKPLLKK---LHELAKKLGLSPLE 230
|
....*
4DBS_A 255 IALRY 259
Cdd:cd19097 231 LALGF 235
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
40-297 |
8.33e-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: 76.84 E-value: 8.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 40 LAIEAGFRHIDSAHLY-----------------------NNEEQVGLAirSKIADGSvkrEDIFYTSKLWSTFHRpELVR 96
Cdd:cd19094 26 YAFDEGVNFIDTAEMYpvppspetqgrteeiigswlkkkGNRDKVVLA--TKVAGPG---EGITWPRGGGTRLDR-ENIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 97 PALENSLKKAQLDYVDLYLIH-----SPMSLKPGEELSPTDEngkvifDIVDLCTTWEAMEKCKDAGLAKSIGVSN---- 167
Cdd:cd19094 100 EAVEGSLKRLGTDYIDLYQLHwpdryTPLFGGGYYTEPSEEE------DSVSFEEQLEALGELVKAGKIRHIGLSNetpw 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 168 ----FNR--RQLemilnkpGLKyKPVCNQvecHPY--FNRSKLLDF---CKSKDIVLVAYSALG---------------- 220
Cdd:cd19094 174 gvmkFLElaEQL-------GLP-RIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLAggvltgkyldgaarpe 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 221 -------SQRDKRWVDPNSPVLLEDpvLCALAKKHKRTPALIALRYQLQR---GVVVLAKSYNEQrIRQNVQVFEFQLTA 290
Cdd:cd19094 243 ggrlnlfPGYMARYRSPQALEAVAE--YVKLARKHGLSPAQLALAWVRSRpfvTSTIIGATTLEQ-LKENIDAFDVPLSD 319
|
....*..
4DBS_A 291 EDMKAID 297
Cdd:cd19094 320 ELLAEID 326
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-166 |
8.85e-16 |
|
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: 75.21 E-value: 8.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFGTYA-----PPEVPRSKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvkREDIFYTSKL---- 85
Cdd:cd19086 5 EIGFGTWGlggdwWGDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVVIATKFgnrf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 86 -----WSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMslkpgEELSPTDEngkvifdivdlctTWEAMEKCKDAGLA 160
Cdd:cd19086 78 dggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPP-----DEVLDNDE-------------LFEALEKLKQEGKI 139
|
....*.
4DBS_A 161 KSIGVS 166
Cdd:cd19086 140 RAYGVS 145
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-299 |
5.06e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 74.29 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 41 AIEAGFRHIDSAHLYnneeqvGLAIRSKIAdGSV----KREDIFYTSKLWSTF--HRPELVRPALENSLKKAQLDYVDLY 114
Cdd:cd19103 41 AMAAGLNLWDTAAVY------GMGASEKIL-GEFlkryPREDYIISTKFTPQIagQSADPVADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 115 LIHSPMSL-KPGEELSPTDENGKVifdivdlcttweamekckdaglaKSIGVSNFNRRQLEM---ILNKPGLKYKPVCNQ 190
Cdd:cd19103 114 WIHNPADVeRWTPELIPLLKSGKV-----------------------KHVGVSNHNLAEIKRaneILAKAGVSLSAVQNH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 191 vecHPYFNRSK----LLDFCKSKDIVLVAYSAL-----------------GSQRDKRWvdpnSPVL--LED--PVLCALA 245
Cdd:cd19103 171 ---YSLLYRSSeeagILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGRAETY----NPLLpqLEEltAVMAEIG 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
4DBS_A 246 KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 299
Cdd:cd19103 244 AKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-297 |
9.75e-15 |
|
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: 73.42 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 19 LGFG----TYAPPEVP-RSKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgsvkREDIFYTSKLWSTFH 90
Cdd:cd19078 7 IGLGcmgmSHGYGPPPdKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKFGFKID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 91 -----------RPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSptdengkvifdivdlcttwEAMEKCKDAGL 159
Cdd:cd19078 80 ggkpgplgldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVA-------------------GTMKELIKEGK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 160 AKSIGVS----NFNRRqlemilnkpGLKYKPVCN-QVECHPYFNR--SKLLDFCKSKDIVLVAYSALG------------ 220
Cdd:cd19078 141 IRHWGLSeagvETIRR---------AHAVCPVTAvQSEYSMMWREpeKEVLPTLEELGIGFVPFSPLGkgfltgkident 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 221 ---SQRDKRWVDPNSP-------VLLEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIRQNVQVFEFQL 288
Cdd:cd19078 212 kfdEGDDRASLPRFTPealeanqALVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIEL 289
|
....*....
4DBS_A 289 TAEDMKAID 297
Cdd:cd19078 290 TPEELREIE 298
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
41-299 |
2.12e-14 |
|
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: 72.61 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 41 AIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKLW------------STFHrpelVRPALENSLKK 105
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVFgpmgddpndrglSRRH----IRRAVEASLRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 106 AQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSIGVSNF-------------NRRQ 172
Cdd:cd19087 108 LQTDYIDLYQMHHFDRDTPLEE-------------------TLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaaRRGL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 173 LEMILNKPglKYKPVCNQVECHpyfnrskLLDFCKSKDIVLVAYSALGS-----------------------QRDKRWVD 229
Cdd:cd19087 169 LRFVSEQP--MYNLLKRQAELE-------ILPAARAYGLGVIPYSPLAGglltgkygkgkrpesgrlverarYQARYGLE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4DBS_A 230 PNSPVLLEdpvLCALAKKHKRTPALIALRYQLQRGVV--VLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGL 299
Cdd:cd19087 240 EYRDIAER---FEALAAEAGLTPASLALAWVLSHPAVtsPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-291 |
3.31e-14 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 71.81 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 16 MPVLGFGT------YAPpeVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSkiadgsVKREDIF------ 80
Cdd:cd19163 13 VSKLGFGAsplggvFGP--VDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALKG------IPRDSYYlatkvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 81 -YTSKLWSTF-HRPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeELSPTdengkviFDIVdLCTTWEAMEKCKDAG 158
Cdd:cd19163 85 rYGLDPDKMFdFSAERITKSVEESLKRLGLDYIDIIQVHDI-------EFAPS-------LDQI-LNETLPALQKLKEEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 159 LAKSIGVSNFNRRQLEMILNKPG------LKYkpvcnqveCHpY--FNRS--KLLDFCKSKDIVLVAYSALG----SQRD 224
Cdd:cd19163 150 KVRFIGITGYPLDVLKEVLERSPvkidtvLSY--------CH-YtlNDTSllELLPFFKEKGVGVINASPLSmgllTERG 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4DBS_A 225 KRwvdPNSPVLLEDPVLCALAKKHKRTP----ALIALRYQLQ--RGVVVLAKSYNEQRIRQNVQVFEFQLTAE 291
Cdd:cd19163 221 PP---DWHPASPEIKEACAKAAAYCKSRgvdiSKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLDAH 290
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
20-297 |
5.22e-14 |
|
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: 71.12 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 20 GFG----TYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVG--LAIRSKIADGSVKREDIFYTSK--LWSTFHR 91
Cdd:cd19077 9 GLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKggLDPDTLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 92 P----ELVRPALENSLKK-AQLDYVDLYlihspmslkpgeELSPTDENgkvifdiVDLCTTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19077 89 PdgspEAVRKSIENILRAlGGTKKIDIF------------EPARVDPN-------VPIEETIKALKELVKEGKIRGIGLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 167 NFNRRQLEMILnkpglKYKPV-CNQVECHPyFNRSKL----LDFCKSKDIVLVAYSALGS-----QRDKRWVDPNSPVLL 236
Cdd:cd19077 150 EVSAETIRRAH-----AVHPIaAVEVEYSL-FSREIEengvLETCAELGIPIIAYSPLGRglltgRIKSLADIPEGDFRR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4DBS_A 237 EDP---------------VLCALAKKHKRTPALIAL---RYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19077 224 HLDrfngenfeknlklvdALQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-299 |
1.36e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 67.29 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 31 RSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKL-WSTFHRPEL---VRPALENSL 103
Cdd:cd19104 31 REEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL-------PAGPYITTKVrLDPDDLGDIggqIERSVEKSL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 104 KKAQLDYVDLYLIHS---PMSLKPGEELSPTDengkvifDIVDLCTTWEAMEKCKDAGLAKSIGVSNF-NRRQLEMIL-- 177
Cdd:cd19104 104 KRLKRDSVDLLQLHNrigDERDKPVGGTLSTT-------DVLGLGGVADAFERLRSEGKIRFIGITGLgNPPAIRELLds 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 178 NKPG--------LKYKPVCNQVECHPYFNRSKLLDFCKSKD-----IVLVAYSALGSQRDKrwvDPNSPVLLEDPV---- 240
Cdd:cd19104 177 GKFDavqvyynlLNPSAAEARPRGWSAQDYGGIIDAAAEHGvgvmgIRVLAAGALTTSLDR---GREAPPTSDSDVaidf 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 241 -----LCALAKKHKRTPALIALRYQL-QRGV--VVLAKSyNEQRIRQNVQVFEF-QLTAEDMKAIDGL 299
Cdd:cd19104 254 rraaaFRALAREWGETLAQLAHRFALsNPGVstVLVGVK-NREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
18-296 |
2.79e-12 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 66.30 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFG------TYAPPeVPRSKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKIadgsvkREDIFYTSKLWST 88
Cdd:cd19145 14 AQGLGcmglsgDYGAP-KPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKFGIH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 89 FHR---------PELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGL 159
Cdd:cd19145 87 EIGgsgvevrgdPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEI-------------------TMGELKKLVEEGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 160 AKSIGVSNFN----RR----------QLEMILnkpglkykpVCNQVEchpyfnrSKLLDFCKSKDIVLVAYSALGsqrdk 225
Cdd:cd19145 148 IKYIGLSEASadtiRRahavhpitavQLEWSL---------WTRDIE-------EEIIPTCRELGIGIVPYSPLG----- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 226 RWVDPNSPVLLEDPV-------------------------LCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRIR 278
Cdd:cd19145 207 RGFFAGKAKLEELLEnsdvrkshprfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLN 286
|
330
....*....|....*...
4DBS_A 279 QNVQVFEFQLTAEDMKAI 296
Cdd:cd19145 287 QNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-299 |
3.96e-12 |
|
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: 65.66 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLG---FGTYAPPEVPrSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLA--------IRSKIADGSVKRedifyts 83
Cdd:cd19075 4 ILGtmtFGSQGRFTTA-EAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELglgergfkIDTKANPGVGGG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 84 klwstfHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSI 163
Cdd:cd19075 76 ------LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEE-------------------TLAAIDELYKEGKFKEF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 164 GVSNFNRRQLEMILN--------KP----GLkYKPVCNQVEchpyfnrSKLLDFCKSKDIVLVAYSALG--------SQR 223
Cdd:cd19075 131 GLSNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLAggfltgkyKYS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 224 DK-----RWvDPNSPVL---------------LEdpVLCALAKKHKRTPALIALRY-----QLQRG---VVVLAKSyNEQ 275
Cdd:cd19075 203 EDkagggRF-DPNNALGklyrdrywkpsyfeaLE--KVEEAAEKEGISLAEAALRWlyhhsALDGEkgdGVILGAS-SLE 278
|
330 340
....*....|....*....|....*
4DBS_A 276 RIRQNVQ-VFEFQLTAEDMKAIDGL 299
Cdd:cd19075 279 QLEENLAaLEKGPLPEEVVKAIDEA 303
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-282 |
2.00e-11 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 63.73 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGT-YAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLA-------IRSKIadgsvKREDIFYTSK---- 84
Cdd:cd19082 1 SRIVLGTaDFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGAServigewLKSRG-----NRDKVVIATKgghp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 -LWSTF-HR--PELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdIVDlcttweAMEKCKDAGLA 160
Cdd:cd19082 76 dLEDMSrSRlsPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGE-------------IVD------TLNELVRAGKI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 161 KSIGVSNFNrrqLEMIL---------NKPGlkykPVCNQvechPYFN-----------------RSKLLDFCKSKDIVLV 214
Cdd:cd19082 137 RAFGASNWS---TERIAeanayakahGLPG----FAASS----PQWSlarpneppwpgptlvamDEEMRAWHEENQLPVF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 215 AYSALG----SQRDKRWVDPNSPVL-----------LEdpVLCALAKKHKRTPALIALRYQLQRG--VVVLAKSYNEQRI 277
Cdd:cd19082 206 AYSSQArgffSKRAAGGAEDDSELRrvyyseenferLE--RAKELAEEKGVSPTQIALAYVLNQPfpTVPIIGPRTPEQL 283
|
....*
4DBS_A 278 RQNVQ 282
Cdd:cd19082 284 RDSLA 288
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-297 |
2.01e-11 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 63.78 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 42 IEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvkREDIFYTSKlwSTF------------HRPELVRpALENSLKKA 106
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATK--YTMnrrpgdpnaggnHRKNLRR-SVEASLRRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 107 QLDYVDLYLIHSPMSLKPGEELSPT-DE---NGKVIFdiVDLCTT--WEAmekCKDAGLAKSIGVSNFNRRQLEMILnkp 180
Cdd:cd19080 111 QTDYIDLLYVHAWDFTTPVEEVMRAlDDlvrAGKVLY--VGISDTpaWVV---ARANTLAELRGWSPFVALQIEYSL--- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 181 glkykpvcnqvechpyFNRS---KLLDFCKSKDIVLVAYSALG-------------SQRDKRWVDPNSPVLLED------ 238
Cdd:cd19080 183 ----------------LERTperELLPMARALGLGVTPWSPLGgglltgkyqrgeeGRAGEAKGVTVGFGKLTErnwaiv 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
4DBS_A 239 PVLCALAKKHKRTPALIALRYQLQR---GVVVLAKSYNEQrIRQNVQVFEFQLTAEDMKAID 297
Cdd:cd19080 247 DVVAAVAEELGRSAAQVALAWVRQKpgvVIPIIGARTLEQ-LKDNLGALDLTLSPEQLARLD 307
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
18-305 |
5.41e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 62.56 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFGTYAPPEV-PRSKALEVTKLAIEAGFRHIDSAHLYN----------NEEQVGLAIRSKiadGSvkREDIFYTSKLW 86
Cdd:PRK10625 15 TLGLGTMTFGEQnSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKR---GS--REKLIIASKVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFH------RPEL------VRPALENSLKKAQLDYVDLYLIHSPMslkpgeelSPTDENGKVIFD------IVDLCTTW 148
Cdd:PRK10625 90 GPSRnndkgiRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWPQ--------RPTNCFGKLGYSwtdsapAVSLLETL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 149 EAMEKCKDAGLAKSIGVSN---FNRRQLEMILNKPGLKyKPVCNQvecHPY--FNRS---KLLDFCKSKDIVLVAYSAL- 219
Cdd:PRK10625 162 DALAEQQRAGKIRYIGVSNetaFGVMRYLHLAEKHDLP-RIVTIQ---NPYslLNRSfevGLAEVSQYEGVELLAYSCLa 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 220 ----------GSQ----------RDKRWVDPNSPVLLEDPVlcALAKKHKRTPALIALRYQLQRGVV---VLAKSYNEQr 276
Cdd:PRK10625 238 fgtltgkylnGAKpagarntlfsRFTRYSGEQTQKAVAAYV--DIAKRHGLDPAQMALAFVRRQPFVastLLGATTMEQ- 314
|
330 340
....*....|....*....|....*....
4DBS_A 277 IRQNVQVFEFQLTAEDMKAIDGLDRNLHY 305
Cdd:PRK10625 315 LKTNIESLHLTLSEEVLAEIEAVHQVYTY 343
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-266 |
1.69e-10 |
|
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: 61.12 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 20 GFGTYAPPEVPRSKALEvtklAIEAGFRHIDsahLYNN--------EEQVGLAIRSkiaDGSVKREDIFYTSKL-WSTFH 90
Cdd:cd19089 21 NFGDYTSPEEARELLRT----AFDLGITHFD---LANNygpppgsaEENFGRILKR---DLRPYRDELVISTKAgYGMWP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 91 RP-------ELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSI 163
Cdd:cd19089 91 GPygdggsrKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEE-------------------TMTALADAVRSGKALYV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 164 GVSNFNRRQLEM---ILNKpgLKYKPVCNQVechPY--FNRS---KLLDFCKSKDIVLVAYSAL--GSQRDKRWVDP--- 230
Cdd:cd19089 152 GISNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRWaedGLLEVLEEAGIGFIAFSPLaqGLLTDKYLNGIppd 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
4DBS_A 231 ---------------NSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVV 266
Cdd:cd19089 227 srraaeskflteealTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-166 |
5.63e-10 |
|
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: 59.29 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTYA---PPEVPRSKALEVTKLAIEAGFRHIDSAHLYN---NEEQVGLAIRSKiadgsvKREDIFYTSKLWSTFH 90
Cdd:cd19162 1 PRLGLGAASlgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALARH------PRAEYVVSTKVGRLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 91 RPELVRPA----------------LENSLKKAQLDYVDLYLIHSPmslKPGEELSPTDengkvifdivdlctTWEAMEKC 154
Cdd:cd19162 75 PGAAGRPAgadrrfdfsadgirrsIEASLERLGLDRLDLVFLHDP---DRHLLQALTD--------------AFPALEEL 137
|
170
....*....|..
4DBS_A 155 KDAGLAKSIGVS 166
Cdd:cd19162 138 RAEGVVGAIGVG 149
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-201 |
7.67e-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: 56.07 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFG---TYAPpEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRskiaDGSVKREDIFYTSKLWSTFHR 91
Cdd:cd19143 15 ALSFGswvTFGN-QVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKIFWGGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 92 PEL---------VRPALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKS 162
Cdd:cd19143 90 PPPndrglsrkhIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEE-------------------TVRAMNDLIDQGKAFY 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
4DBS_A 163 IGVSNFNRRQLE---MILNKPGLkYKPVCNQVECHpYFNRSK 201
Cdd:cd19143 151 WGTSEWSAQQIEeahEIADRLGL-IPPVMEQPQYN-LFHRER 190
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-282 |
3.76e-08 |
|
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: 53.87 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 42 IEAGFRHIDSAHLYN----------NEEQVG--LAIRSKiadgsvkREDIFYTSKLWSTFHRP------------ELVRP 97
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGrwLKDRGN-------RDDVVIATKVGAGPRDPdggpespeglsaETIEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 98 ALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSIGVSNFNRRQLEM-- 175
Cdd:cd19752 100 EIDKSLRRLGTDYIDLYYAHVDDRDTPLEE-------------------TLEAFNELVKAGKVRAIGASNFAAWRLERar 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 176 -ILNKPGLKyKPVCNQVEcHPYFN-------------RSKLLDFCKS-KDIVLVAYSAL--GS-QRDKR-----WVDPNS 232
Cdd:cd19752 161 qIARQQGWA-EFSAIQQR-HSYLRprpgadfgvqrivTDELLDYASSrPDLTLLAYSPLlsGAyTRPDRplpeqYDGPDS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
4DBS_A 233 PVLLEdpVLCALAKKHKRTPALIALRYQLQR--GVV-VLAKSYNEQrIRQNVQ 282
Cdd:cd19752 239 DARLA--VLEEVAGELGATPNQVVLAWLLHRtpAIIpLLGASTVEQ-LEENLA 288
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
17-202 |
3.38e-07 |
|
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: 50.93 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGTYA--PPEVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKL-WSTfh 90
Cdd:cd19142 14 SNVGLGTWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIyWSY-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 91 RPE---LVRP----ALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdIVdlcttwEAMEKCKDAGLAKSI 163
Cdd:cd19142 88 GSEergLSRKhiieSVRASLRRLQLDYIDIVIIHKADPMCPMEE-------------VV------RAMSYLIDNGLIMYW 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
4DBS_A 164 GVSNF----------NRRQLEMILnkpglkykPVCNQVECHPyFNRSKL 202
Cdd:cd19142 149 GTSRWspveimeafsIARQFNCPT--------PICEQSEYHM-FCREKM 188
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
19-285 |
1.72e-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: 48.69 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 19 LGFGTYA-------PPEVprSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKLW-- 86
Cdd:cd19153 15 VGLGTAAlggvygdGLEQ--DEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVGry 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 --STF-HRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKpgeelsptdengkvIFDIVDlcTTWEAMEKCKDAGLAKSI 163
Cdd:cd19153 89 rdSEFdYSAERVRASVATSLERLHTTYLDVVYLHDIEFVD--------------YDTLVD--EALPALRTLKDEGVIKRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 164 GVSNFNRRQLEMILNK--PGlkyKPVCNQVECHPYFNRSKLLD----FCKSKDIVLVAYSALG-----SQRDKRWvDPNS 232
Cdd:cd19153 153 GIAGYPLDTLTRATRRcsPG---SLDAVLSYCHLTLQDARLESdapgLVRGAGPHVINASPLSmglltSQGPPPW-HPAS 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
4DBS_A 233 PVLLEdpvLCALAKKH-----KRTPALiALRYQL----QRGVVVLAKSYNEQrIRQNVQVFE 285
Cdd:cd19153 229 GELRH---YAAAADAVcasveASLPDL-ALQYSLaahaGVGTVLLGPSSLAQ-LRSMLAAVD 285
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-165 |
1.95e-06 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 48.76 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGT------YAPpeVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgsvKREDIFYTSKL-W 86
Cdd:cd19152 1 PKLGFGTaplgnlYEA--VSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 ---------STF---------HRPEL------VRPALENSLKKAQLDYVDLYLIHSPmslkpGEELSPTDENGKVIFDIV 142
Cdd:cd19152 73 llvplqevePTFepgfwnplpFDAVFdysydgILRSIEDSLQRLGLSRIDLLSIHDP-----DEDLAGAESDEHFAQAIK 147
|
170 180
....*....|....*....|...
4DBS_A 143 DlctTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19152 148 G---AFRALEELREEGVIKAIGL 167
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
21-297 |
1.98e-05 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 45.75 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 21 FGTYAPPEVPRSkaleVTKLAIEAGFRHIDSAHLY-----NNEEQVGLAIRSkiaDGSVKREDIFYTSK----LW----- 86
Cdd:PRK09912 36 FGHVNALESQRA----ILRKAFDLGITHFDLANNYgpppgSAEENFGRLLRE---DFAAYRDELIISTKagydMWpgpyg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 STFHRPELVrPALENSLKKAQLDYVDLYLIHSPmslkpgEELSPTDEngkvifdivdlctTWEAMEKCKDAGLAKSIGVS 166
Cdd:PRK09912 109 SGGSRKYLL-ASLDQSLKRMGLEYVDIFYSHRV------DENTPMEE-------------TASALAHAVQSGKALYVGIS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 167 NFN-RRQLEM--ILNK---PGLKYKPVCNQVecHPYFNRSKLLDFCKSKDIVLVAYSALGS-----------------QR 223
Cdd:PRK09912 169 SYSpERTQKMveLLREwkiPLLIHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLAQglltgkylngipqdsrmHR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 224 DKRWVDPNSPVLLEDP------VLCALAKKHKRTPALIALRYQL--QRGVVVLAKSYNEQRIRQNVQVFE-FQLTAEDMK 294
Cdd:PRK09912 247 EGNKVRGLTPKMLTEAnlnslrLLNEMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALNnLTFSTEELA 326
|
...
4DBS_A 295 AID 297
Cdd:PRK09912 327 QID 329
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
19-202 |
2.15e-05 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 45.42 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 19 LGFGTYAP--PEVPRSKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgSVKREDIFYTSKLW------- 86
Cdd:cd19159 16 LGLGTWVTfgGQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLYwggkaet 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 -STFHRPELVRpALENSLKKAQLDYVDLYLIHSPMSLKPGEE----LSPTDENGKVIFDIVdlcTTWEAMEKCKDAGLAk 161
Cdd:cd19159 92 eRGLSRKHIIE-GLKGSLQRLQLEYVDVVFANRPDSNTPMEEivraMTHVINQGMAMYWGT---SRWSAMEIMEAYSVA- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
4DBS_A 162 sigvsnfnrRQLEMIlnkpglkyKPVCNQVECHpYFNRSKL 202
Cdd:cd19159 167 ---------RQFNMI--------PPVCEQAEYH-LFQREKV 189
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
18-202 |
2.79e-05 |
|
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: 45.13 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFGTYAP--PEVPRSKALEVTKLAIEAGFRHIDSAHLY---NNEEQVGLAIRSKiadgSVKREDIFYTSKL-WST--- 88
Cdd:cd19141 14 CLGLGTWVTfgSQISDEVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKK----GWRRSSYVITTKIfWGGkae 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 89 ----FHRPELVRpALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdIVDLCT--------------TWEA 150
Cdd:cd19141 90 tergLSRKHIIE-GLKASLERLQLEYVDIVFANRPDPNTPMEE-------------IVRAFThvinqgmamywgtsRWSA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
4DBS_A 151 MEKCKDAGLAksigvsnfnrRQLEMIlnkpglkyKPVCNQVECHpYFNRSKL 202
Cdd:cd19141 156 MEIMEAYSVA----------RQFNLI--------PPIVEQAEYH-LFQREKV 188
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
17-164 |
4.05e-05 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 44.62 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 17 PVLGFGT------YAPpeVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKIADG---SVKREDIFYTSK 84
Cdd:cd19161 1 SELGLGTaglgnlYTA--VSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREKPRDEfvlSTKVGRLLKPAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 85 LWSTFHRPELVRP----------------ALENSLKKAQLDYVDLYLIHspmslkpgeELSPT---DENGKVIFDIvdLC 145
Cdd:cd19161 79 EGSVPDPNGFVDPlpfeivydysydgimrSFEDSLQRLGLNRIDILYVH---------DIGVYthgDRKERHHFAQ--LM 147
|
170 180
....*....|....*....|
4DBS_A 146 TT-WEAMEKCKDAGLAKSIG 164
Cdd:cd19161 148 SGgFKALEELKKAGVIKAFG 167
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
18-281 |
3.96e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 41.69 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFGtyAPP------EVPRSKALEVTKLAIEAGFRHIDSAHLYNN---EEQVGLAIRSKiadgSVKREDIFYTSKLW-- 86
Cdd:PLN02587 13 SVGFG--ASPlgsvfgPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTKCGry 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 87 -STFH-RPELVRPALENSLKKAQLDYVDLYLIHSPmslkpgeELSPTDEngkvifdIVDlcTTWEAMEKCKDAGLAKSIG 164
Cdd:PLN02587 87 gEGFDfSAERVTKSVDESLARLQLDYVDILHCHDI-------EFGSLDQ-------IVN--ETIPALQKLKESGKVRFIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 165 VSNFNRRQLEMILNK--PG-----LKYkpvcnqveCHPYFNRSKLLD---FCKSKDIVLVAYS--ALGSQRDK---RWvD 229
Cdd:PLN02587 151 ITGLPLAIFTYVLDRvpPGtvdviLSY--------CHYSLNDSSLEDllpYLKSKGVGVISASplAMGLLTENgppEW-H 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
4DBS_A 230 PNSPVLLEdpvLCALAKKH----KRTPALIALRYQL--QRGVVVLAKSYNEQRIRQNV 281
Cdd:PLN02587 222 PAPPELKS---ACAAAATHckekGKNISKLALQYSLsnKDISTTLVGMNSVQQVEENV 276
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-117 |
6.92e-04 |
|
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: 40.72 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 18 VLGFGTYAP---PEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQV-GLAIrSKIADgSVKREDIFYTSKL----WSTF 89
Cdd:cd19164 17 IFGAATFSYqytTDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL-KALRD-EFPRDTYFIITKVgrygPDDF 94
|
90 100
....*....|....*....|....*....
4DBS_A 90 -HRPELVRPALENSLKKAQLDYVDLYLIH 117
Cdd:cd19164 95 dYSPEWIRASVERSLRRLHTDYLDLVYLH 123
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
98-266 |
2.39e-03 |
|
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: 39.31 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 98 ALENSLKKAQLDYVDLYLIHSPMSLKPGEElsptdengkvifdivdlctTWEAMEKCKDAGLAKSIGVSNFN----RRQL 173
Cdd:cd19151 106 SLDQSLKRMGLDYVDIFYHHRPDPETPLEE-------------------TMGALDQIVRQGKALYVGISNYPpeeaREAA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DBS_A 174 EMI--LNKPGLKYKPVcnqvecHPYFNR---SKLLDFCKSKDIVLVAYSAL-----------GSQRDKRWVDPNSPvLLE 237
Cdd:cd19151 167 AILkdLGTPCLIHQPK------YSMFNRwveEGLLDVLEEEGIGCIAFSPLaqglltdrylnGIPEDSRAAKGSSF-LKP 239
|
170 180 190
....*....|....*....|....*....|....*....
4DBS_A 238 DPV----------LCALAKKHKRTPALIALRYQLQRGVV 266
Cdd:cd19151 240 EQIteeklakvrrLNEIAQARGQKLAQMALAWVLRNKRV 278
|
|
| |
