|
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) ... |
7-305 |
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: 576.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 7 TRLTLHDGNAIPVMGLGTYASAEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKL 86
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 87 WCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAH----SNQPLDFDDVDFCLTWEALEGCKDAGLVKSIGV 162
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELfpkdENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 163 SNFNRRQLERLLSKPGLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDNTWVDPNSPVLLEDPVLRSVA 242
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785353101 243 AKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRYAQF 305
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
14-316 |
2.07e-162 |
|
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: 455.03 E-value: 2.07e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGTYASAE-VPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWCSFFS 92
Cdd:cd19109 1 GNSIPIIGLGTYSEPKtTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 93 PNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDahSNQPLD------FDDVDFCLTWEALEGCKDAGLVKSIGVSNFN 166
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGD--EIYPRDengkwlYHKTNLCATWEALEACKDAGLVKSIGVSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 167 RRQLERLLSKPGLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDNTWVDPNSPVLLEDPVLRSVAAKYN 246
Cdd:cd19109 159 RRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 247 RSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRYAQFTVMKQHPEYPF 316
Cdd:cd19109 239 KTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
14-320 |
1.38e-129 |
|
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: 371.75 E-value: 1.38e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGTYASaevPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWCSFFSP 93
Cdd:cd19107 1 GAKMPILGLGTWKS---PPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 94 NLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHSnqPLDFD------DVDFCLTWEALEGCKDAGLVKSIGVSNFNR 167
Cdd:cd19107 78 GLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELF--PLDESgnvipsDTTFLDTWEAMEELVDEGLVKAIGVSNFNH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 168 RQLERLLSKPGLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTArDNTWVDPNSPVLLEDPVLRSVAAKYNR 247
Cdd:cd19107 156 LQIERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP-DRPWAKPEDPSLLEDPKIKEIAAKHNK 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785353101 248 SPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRYAQFTVMKQHPEYPFHDEY 320
Cdd:cd19107 235 TTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
11-302 |
5.73e-122 |
|
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: 351.58 E-value: 5.73e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 11 LHDGNAIPVMGLGTYASaeVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWCSF 90
Cdd:cd19116 5 LNDGNEIPAIALGTWKL--KDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 91 FSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKP-SDAHSNQPLDFDDVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQ 169
Cdd:cd19116 83 HEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKEnNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 170 LERLLSkpGLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTA-RDNTWvdpNSPVLLEDPVLRSVAAKYNRS 248
Cdd:cd19116 163 INRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLvPRGQT---NPPPRLDDPTLVAIAKKYGKT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1785353101 249 PAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:cd19116 238 TAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
17-294 |
1.09e-118 |
|
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: 341.77 E-value: 1.09e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIadgtVKREEIFYTGKLWCSFFSPNLV 96
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 97 RQGLEASLKALQLDYLDLFIMHWPFSVKPSDAhsnqpldfdDVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQLERLLSK 176
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGKEGGS---------KEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 177 PglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDntwvdpnspVLLEDPVLRSVAAKYNRSPAEVAMRF 256
Cdd:cd19071 145 A--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR---------PLLDDPVLKEIAKKYGKTPAQVLLRW 213
|
250 260 270
....*....|....*....|....*....|....*...
gi 1785353101 257 ILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19071 214 ALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
11-302 |
4.08e-118 |
|
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: 342.44 E-value: 4.08e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 11 LHDGNAIPVMGLGTYASA--EVpksdgTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKI-ADGTVKREEIFYTGKLW 87
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKpgQV-----KAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 88 CSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSD----AHSNQPLDFDDVDFCLTWEALEGCKDAGLVKSIGVS 163
Cdd:cd19106 76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDnpfpKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 164 NFNRRQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTArDNTWVDPNSPVLLEDPVLRSVAA 243
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSP-DRPWAKPDEPVLLEEPKVKALAK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785353101 244 KYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:cd19106 233 KYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
17-320 |
6.38e-115 |
|
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: 334.23 E-value: 6.38e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYASA--EVpksdgTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWCSFFSPN 94
Cdd:cd19110 4 IPAVGLGTWKASpgEV-----TEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 95 LVRQGLEASLKALQLDYLDLFIMHWPFSVKPsdAHSNQPLDFD------DVDFCLTWEALEGCKDAGLVKSIGVSNFNRR 168
Cdd:cd19110 79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKP--GEPDLPLDRSgmvipsDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 169 QLERLLSKPGLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDNtwVDpnspvLLEDPVLRSVAAKYNRS 248
Cdd:cd19110 157 QLERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEG--VD-----LIDDPVIQRIAKKHGKS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785353101 249 PAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRYAQFTVMKQHPEYPFHDEY 320
Cdd:cd19110 230 PAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
13-302 |
7.11e-115 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 332.40 E-value: 7.11e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 13 DGNAIPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRskiADGtVKREEIFYTGKLWCSFFS 92
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA---ASG-VPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 93 PNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDahsnqpldfddvdfclTWEALEGCKDAGLVKSIGVSNFNRRQLER 172
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGPGPYVE----------------TWRALEELYEEGLIRAIGVSNFDPEHLEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 173 LLSKPGlkYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNRSPAEV 252
Cdd:COG0656 138 LLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKTPAQV 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1785353101 253 AMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:COG0656 205 VLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
9-302 |
9.11e-108 |
|
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: 315.89 E-value: 9.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYASAevpKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWC 88
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSK---PGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPS---DAHSNQPLDFDDVDFCLTWEALEGCKDAGLVKSIGVSNF 165
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGvgfPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 166 NRRQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTA-RDNTWVDPNSPVLLEDPVLRSVAAK 244
Cdd:cd19123 161 SVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGdRPAAMKAEGEPVLLEDPVINKIAEK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785353101 245 YNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:cd19123 239 HGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRY 296
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-301 |
4.45e-103 |
|
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: 304.33 E-value: 4.45e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYASAEVpksDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWC 88
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQSKGA---EGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHS----NQPLDFDDVDFCLTWEALEGCKDAGLVKSIGVSN 164
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESgtmeNGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 165 FNRRQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGT-ARDNTWVDP---NSPVLLEDPVLRS 240
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpGRANFTKSTgvsPAPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785353101 241 VAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLR 301
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
7-296 |
5.74e-103 |
|
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: 303.11 E-value: 5.74e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 7 TRLTLHDGNAIPVMGLGTYASaevPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKL 86
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQA---DPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 87 WCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKpSDAHSNQPLDFDDVDFCLTWEALEGCKDAGLVKSIGVSNFN 166
Cdd:cd19125 78 WCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLK-KGAHMPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 167 RRQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTArDNTWVDPNspvLLEDPVLRSVAAKYN 246
Cdd:cd19125 157 VKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSP-GTTWVKKN---VLKDPIVTKVAEKLG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1785353101 247 RSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGL 296
Cdd:cd19125 231 KTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
13-296 |
5.09e-97 |
|
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: 288.01 E-value: 5.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 13 DGNAIPVMGLGTYASAEVPKsDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVK-REEIFYTGKLWCSFF 91
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE-DIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 92 SPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPsDAHSNQPL--DFDDVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQ 169
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKP-GKFSFPIEeeDFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSCKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 170 LERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGtARDNTWvdpNSPVLLEDPVLRSVAAKYNRSP 249
Cdd:cd19124 159 LQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLG-APGTKW---GSNAVMESDVLKEIAAAKGKTV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1785353101 250 AEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGL 296
Cdd:cd19124 233 AQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
9-305 |
4.51e-89 |
|
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: 268.62 E-value: 4.51e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYASaevPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWC 88
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQS---SPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHS-----NQPLDFD-DVDFCLTWEALEGCKDAGLVKSIGV 162
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSgkldpTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 163 SNFNRRQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGT-ARDNTWVDPNSPV-----LLEDP 236
Cdd:cd19155 161 SNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpGAAHFSPGTGSPSgsspdLLQDP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785353101 237 VLRSVAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRYAQF 305
Cdd:cd19155 239 VVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGRTF 307
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
14-305 |
3.52e-87 |
|
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: 263.20 E-value: 3.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGTYASaevPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWCSFFSP 93
Cdd:cd19111 1 GFPMPVIGLGTYQS---PPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 94 NLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHSNQPLDFDDVDfcLTWEALEGCKDAGLVKSIGVSNFNRRQLERL 173
Cdd:cd19111 78 KDTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDKGERELASSDVT--SVWRAMEALVSEGKVKSIGLSNFNPRQINKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 174 LSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGT-ARDNTWVDPNSPVLLEDPVLRSVAAKYNRSPAEV 252
Cdd:cd19111 156 LAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELDKTPAQV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1785353101 253 AMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRYAQF 305
Cdd:cd19111 234 LLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFDF 286
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
9-297 |
1.03e-86 |
|
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: 260.77 E-value: 1.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRskiaDGTVKREEIFYTGKLWC 88
Cdd:cd19131 2 ITLNDGNTIPQLGLGVW---QVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFsvkPSDAHsnqpldfddvdFCLTWEALEGCKDAGLVKSIGVSNFNRR 168
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PAQDK-----------YVETWKALIELKKEGRVKSIGVSNFTIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 169 QLERLLSKPGLKykPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNRS 248
Cdd:cd19131 141 HLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEKHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1785353101 249 PAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLN 297
Cdd:cd19131 208 PAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
17-294 |
1.29e-85 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 257.58 E-value: 1.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIrskiADGTVKREEIFYTGKLWCSFFSPNLV 96
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 97 RQGLEASLKALQLDYLDLFIMHWPFSvkpsdahsnqpldfdDVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQLERLLSK 176
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNP---------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 177 PGLKykPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLgtARDNtwvdpnspvLLEDPVLRSVAAKYNRSPAEVAMRF 256
Cdd:cd19073 139 SPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL--ARGE---------VLRDPVIQEIAEKYDKTPAQVALRW 205
|
250 260 270
....*....|....*....|....*....|....*...
gi 1785353101 257 ILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19073 206 LVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-298 |
2.12e-84 |
|
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: 255.89 E-value: 2.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYASAEvpkSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRskiaDGTVKREEIFYTGKLWC 88
Cdd:cd19117 6 FKLNTGAEIPAVGLGTWQSKP---NEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLWC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPnlVRQGLEASLKALQLDYLDLFIMHWPFSVKPsDAHSNQPL-------DFDDVDFCLTWEALEGCKDAGLVKSIG 161
Cdd:cd19117 79 TWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDP-DGNDFLFKkddgtkdHEPDWDFIKTWELMQKLPATGKVKAIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 162 VSNFNRRQLERLLSKPGLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTArdntwvdpNSPvLLEDPVLRSV 241
Cdd:cd19117 156 VSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGST--------NAP-LLKEPVIIKI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785353101 242 AAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVfeFELKPEDMEMLDGLNR 298
Cdd:cd19117 227 AKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
14-294 |
5.15e-84 |
|
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: 254.46 E-value: 5.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGTyASAEVPKSDGT------EATKLAIDLGYRHIDCAYIYGNEVQIGEAIRskiaDGTVKREEIFYTGKLW 87
Cdd:cd19120 1 GSKIPAIAFGT-GTAWYKSGDDDiqrdlvDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 88 CSffSPNlVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDahsnqpLDFDDVdfcltWEALEGCKDAGLVKSIGVSNFNR 167
Cdd:cd19120 76 PG--IKD-PREALRKSLAKLGVDYVDLYLIHSPFFAKEGG------PTLAEA-----WAELEALKDAGLVRSIGVSNFRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 168 RQLERLLSKPglKYKPVCNQVEYHVYLN--QSKLHEYCKCHNIVLVAYSVLGTardnTWVDPNSPVlleDPVLRSVAAKY 245
Cdd:cd19120 142 EDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSP----LTRDAGGPL---DPVLEKIAEKY 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1785353101 246 NRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19120 213 GVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
9-302 |
5.26e-84 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 254.24 E-value: 5.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYASAEvpKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRskiaDGTVKREEIFYTGKLWC 88
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEE--GSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKVWN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDahsnqpldfddvdfclTWEALEGCKDAGLVKSIGVSNFNRR 168
Cdd:cd19157 76 ADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKE----------------TWKALEKLYKDGRVRAIGVSNFQVH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 169 QLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNRS 248
Cdd:cd19157 140 HLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAEKYNKS 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1785353101 249 PAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:cd19157 207 VAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
17-296 |
1.35e-82 |
|
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: 250.63 E-value: 1.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYasaevpKSDGTEATKLAID----LGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWCSFFS 92
Cdd:cd19136 1 MPILGLGTF------RLRGEEEVRQAVDaalkAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 93 PNLVRQGLEASLKALQLDYLDLFIMHWPFS--VKPSD-AHSNQPLDfddvdfclTWEALEGCKDAGLVKSIGVSNFNRRQ 169
Cdd:cd19136 75 YEKARAACLGSLERLGTDYLDLYLIHWPGVqgLKPSDpRNAELRRE--------SWRALEDLYKEGKLRAIGVSNYTVRH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 170 LERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTArdntwvdpnSPVLLEDPVLRSVAAKYNRSP 249
Cdd:cd19136 147 LEELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG---------DLRLLEDPTVLAIAKKYGRTP 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1785353101 250 AEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGL 296
Cdd:cd19136 216 AQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
9-297 |
2.97e-82 |
|
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: 249.41 E-value: 2.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYasaEVPKSDGTE-ATKLAIDLGYRHIDCAYIYGNEVQIGEAIRskiaDGTVKREEIFYTGKLW 87
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 88 CSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSvkpsDAHSnqpldfddvdfclTWEALEGCKDAGLVKSIGVSNFNR 167
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG----DVYG-------------AWRAMEELYKEGKIRAIGVSNFYP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 168 RQLERLLskPGLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDNtwvdpnspvLLEDPVLRSVAAKYNR 247
Cdd:cd19133 137 DRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN---------LFENPVLTEIAEKYGK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1785353101 248 SPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLN 297
Cdd:cd19133 206 SVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-304 |
1.13e-81 |
|
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: 249.71 E-value: 1.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYasaevpKSDGTEATKL---AIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGK 85
Cdd:cd19112 3 ITLNSGHKMPVIGLGVW------RMEPGEIKELilnAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 86 LWCSffSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVK------PSDAHSNQPLDFDDVDFCL--TWEALEGCKDAGLV 157
Cdd:cd19112 77 LWNS--DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKhtgvgtTGSALGEDGVLDIDVTISLetTWHAMEKLVSAGLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 158 KSIGVSNFnrrqlERLLSKPGLKY---KPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDNT-WVDPNSPvlL 233
Cdd:cd19112 155 RSIGISNY-----DIFLTRDCLAYskiKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAeWFGSVSP--L 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785353101 234 EDPVLRSVAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRYAQ 304
Cdd:cd19112 228 DDPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQ 298
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-302 |
1.73e-81 |
|
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: 249.29 E-value: 1.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWC 88
Cdd:cd19113 3 IKLNSGYKMPSVGFGCW---KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHSNQP----------LDFDDVDFCLTWEALEGCKDAGLVK 158
Cdd:cd19113 80 NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVPIEEKYPpgfycgdgdnFVYEDVPILDTWKALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 159 SIGVSNFNRRQLERLLSkpGLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTAR----DNTWVdPNSPVLLE 234
Cdd:cd19113 160 SIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSfvelNQGRA-LNTPTLFE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785353101 235 DPVLRSVAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:cd19113 237 HDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
12-296 |
4.84e-81 |
|
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: 246.02 E-value: 4.84e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 12 HDGNAIPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIrskiADGTVKREEIFYTGKLWCSFF 91
Cdd:cd19140 3 VNGVRIPALGLGTY---PLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 92 SPNLVRQGLEASLKALQLDYLDLFIMHWPFSvkpsdahsnqpldfdDVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQLE 171
Cdd:cd19140 76 SPDDFLASVEESLRKLRTDYVDLLLLHWPNK---------------DVPLAETLGALNEAQEAGLARHIGVSNFTVALLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 172 --RLLSKPGLkykpVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNRSP 249
Cdd:cd19140 141 eaVELSEAPL----FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1785353101 250 AEVAMRFILQK-GAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGL 296
Cdd:cd19140 206 AQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
18-296 |
9.50e-79 |
|
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: 241.27 E-value: 9.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 18 PVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWCSFFSPNLVR 97
Cdd:cd19128 2 PRLGFGTY---KITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 98 QGLEASLKALQLDYLDLFIMHWPFSVKPSD----AHSNQPLDFDDVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQLERL 173
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTdgdpRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 174 LSKpgLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDntwvDPNSpVLLEDPVLRSVAAKYNRSPAEVA 253
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYG----DGNL-TFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1785353101 254 MRFILQK---GAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGL 296
Cdd:cd19128 232 IAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
9-297 |
1.08e-78 |
|
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: 240.42 E-value: 1.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYasaEVPKSDGTE-ATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSkiadGTVKREEIFYTGKLW 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVF---QTPDGDETErAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 88 CSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDahsnqpldfddvdfclTWEALEGCKDAGLVKSIGVSNFNR 167
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFID----------------TWKALEKLYASGKVKAIGVSNFQE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 168 RQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNR 247
Cdd:cd19126 138 HHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGEKYGK 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1785353101 248 SPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLN 297
Cdd:cd19126 205 SAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
11-296 |
1.96e-78 |
|
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: 240.78 E-value: 1.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 11 LHDGNAIPVMGLGTYASA--EVpksdgTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIAD-GTVKREEIFYTGKLW 87
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEpgEV-----GAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 88 CSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKP-SDAHSNQPLDFDD--------VDFCLTWEALEGCKDAGLVK 158
Cdd:cd19118 76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPtGDLNPLTAVPTNGgevdldlsVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 159 SIGVSNFNRRQLERLLSKPGLkyKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGtarDNTwvdPNSPVLLEDPVL 238
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLG---NNL---AGLPLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785353101 239 RSVAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGvfEFELKPEDMEMLDGL 296
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
11-298 |
5.73e-78 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 238.32 E-value: 5.73e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 11 LHDGNAIPVMGLGTYAsaeVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSkiadGTVKREEIFYTGKLWCSF 90
Cdd:cd19132 1 LNDGTQIPAIGFGTYP---LKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 91 FSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvKPSdahsnqpldfddVDFCL-TWEALEGCKDAGLVKSIGVSNFNRRQ 169
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWP---NPS------------RDLYVeAWQALIEAREEGLVRSIGVSNFLPEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 170 LERLLSKPGLKykPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDntwvdpnspvLLEDPVLRSVAAKYNRSP 249
Cdd:cd19132 139 LDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG----------LLDEPVIKAIAEKHGKTP 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1785353101 250 AEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNR 298
Cdd:cd19132 207 AQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
9-302 |
1.01e-76 |
|
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: 235.88 E-value: 1.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYASaevpkSDGTEA---TKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKiadgTVKREEIFYTGK 85
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRV-----QDGAEAenaVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 86 LWCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDahsnqpldfddvdfclTWEALEGCKDAGLVKSIGVSNF 165
Cdd:cd19156 72 LWNSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFKD----------------TWKAFEKLYKEKKVRAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 166 NRRQLERLLSKpgLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKY 245
Cdd:cd19156 136 HEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKKY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785353101 246 NRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:cd19156 203 GKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
9-296 |
6.23e-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: 233.76 E-value: 6.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYASAEvpKSDgtEATKLAI-DLGYRHIDCAYIYGNEVQIGEAIRskiADGtVKREEIFYTGKLW 87
Cdd:cd19135 5 VRLSNGVEMPILGLGTSHSGG--YSH--EAVVYALkECGYRHIDTAKRYGCEELLGKAIK---ESG-VPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 88 CSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSvkPSDAHSNQPLDFDdvdfclTWEALEGCKDAGLVKSIGVSNFNR 167
Cdd:cd19135 77 PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDC--PSSGKNVKETRAE------TWRALEELYDEGLCRAIGVSNFLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 168 RQLERLLSKPGLKykPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNR 247
Cdd:cd19135 149 EHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGK-----------ALEEPTVTELAKKYQK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1785353101 248 SPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGL 296
Cdd:cd19135 216 TPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
6-296 |
7.53e-76 |
|
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: 233.96 E-value: 7.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 6 DTRLTLHDGNAIPVMGLGTYASAevpKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGtVKREEIFYTGK 85
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAK---AGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 86 LWCSFFSPnlVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHSNQPL------DFD-DVDFCLTWEALEGCKDAGLVK 158
Cdd:cd19121 77 LWSTYHRR--VELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTlpdgsrDLDwDWNHVDTWKQMEKVLKTGKTK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 159 SIGVSNFNRRQLERLLskPGLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTArdntwvdpNSPVLLEDPVL 238
Cdd:cd19121 155 AIGVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGST--------GSPLISDEPVV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785353101 239 RsVAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFElkPEDMEMLDGL 296
Cdd:cd19121 225 E-IAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
12-302 |
2.75e-73 |
|
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: 227.73 E-value: 2.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 12 HDGNAIPVMGLGTYASaevPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWCSFF 91
Cdd:cd19129 1 NGSGAIPALGFGTLIP---DPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 92 SPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPS------DAHSNQPLDfDDVDFCLTWEALEGCKDAGLVKSIGVSNF 165
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGdeqdprDANGNVIYD-DGVTLLDTWRAMERLVDEGRCKAIGLSDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 166 NRRQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDntwvdpnsPVLLEDPVLRSVAAKY 245
Cdd:cd19129 157 SLEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME--------PKLLEDPVITAIARRV 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785353101 246 NRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNlgvFEFELKPEDM--EMLDGLNRNLRY 302
Cdd:cd19129 227 NKTPAQVLLAWAIQRGTALLTTSKTPSRIREN---FDISTLPEDAmrEINEGIKTRYRF 282
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-298 |
9.84e-73 |
|
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: 226.61 E-value: 9.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTyASAEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWC 88
Cdd:cd19119 4 FKLNTGASIPALGLGT-ASPHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFspNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHSNQPL-------------DFDDVDfclTWEALEGCKDAG 155
Cdd:cd19119 83 TFY--DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSGKPFtpvnddgktryaaSGDHIT---TYKQLEKIYLDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 156 LVKSIGVSNFNRRQLERLLSKpgLKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTardntwvdpNSPVLLED 235
Cdd:cd19119 158 RAKAIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGS---------HGAPNLKN 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785353101 236 PVLRSVAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVfeFELKPEDMEMLDGLNR 298
Cdd:cd19119 227 PLVKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
9-297 |
2.02e-72 |
|
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: 224.59 E-value: 2.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYASaevPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKiadgTVKREEIFYTGKLWC 88
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQT---PPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFsvkpsdahsnqPLDFDD-VDfclTWEALEGCKDAGLVKSIGVSNFNR 167
Cdd:cd19127 74 SDYGYDKALRGFDASLRRLGLDYVDLYLLHWPV-----------PNDFDRtIQ---AYKALEKLLAEGRVRAIGVSNFTP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 168 RQLERLLSKPGLKykPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDNTWVDPNSPV-LLEDPVLRSVAAKYN 246
Cdd:cd19127 140 EHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGPTGPGdVLQDPTITGLAEKYG 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1785353101 247 RSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLN 297
Cdd:cd19127 218 KTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
9-302 |
7.40e-72 |
|
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: 224.61 E-value: 7.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWC 88
Cdd:cd19115 5 VKLNSGYDMPLVGFGLW---KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHSNQP---------LDFDDVDFCLTWEALEGCKDAGLVKS 159
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDPAVRYPpgwfydgkkVEFSNAPIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 160 IGVSNFNRRQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLG----------TARDntwvdpnS 229
Cdd:cd19115 162 IGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsfleldlpGAKD-------T 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785353101 230 PVLLEDPVLRSVAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:cd19115 233 PPLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
14-304 |
5.08e-71 |
|
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: 222.43 E-value: 5.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADGTVKREEIFYTGKLWCSFFSP 93
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 94 NLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHSNQP----------LDFDDVDFCLTWEALEGCKDAGLVKSIGVS 163
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDPAENYPflwkdkelkkFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 164 NFNRRQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDNTWVDPNSPV--LLEDPVLRSV 241
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFtnLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785353101 242 AAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRYAQ 304
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFND 298
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-297 |
2.73e-70 |
|
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: 219.01 E-value: 2.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 8 RLTLHDGNAIPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIrskiADGTVKREEIFYTGKLW 87
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 88 CSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPsdahsnqpldfddvDFCLTWEALEGCKDAGLVKSIGVSNFNR 167
Cdd:cd19130 74 NDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAG--------------NYVHTWEAMIELRAAGRTRSIGVSNFLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 168 RQLERLLSKPGLKykPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNR 247
Cdd:cd19130 140 PHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAAAHGK 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1785353101 248 SPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLN 297
Cdd:cd19130 207 TPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
14-294 |
8.17e-67 |
|
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: 210.16 E-value: 8.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGTYA---SAEVPKSDG---TEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRskiadgTVKREEIFYTG 84
Cdd:cd19072 1 GEEVPVLGLGTWGiggGMSKDYSDDkkaIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 85 KLWCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsdahsNqpldfDDVDFCLTWEALEGCKDAGLVKSIGVSN 164
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP----------N-----PSIPIEETLRAMEELVEEGKIRYIGVSN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 165 FNRRQLERLLSKPGlKYKPVCNQVEYHVYLN--QSKLHEYCKCHNIVLVAYSVLGTARDNTWVDPnspvlledPVLRSVA 242
Cdd:cd19072 140 FSLEELEEAQSYLK-KGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS--------PLLDEIA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1785353101 243 AKYNRSPAEVAMRFILQK-GAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19072 211 KKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
9-302 |
1.61e-66 |
|
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: 209.33 E-value: 1.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTyasAEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRskiADGtVKREEIFYTGKLWC 88
Cdd:cd19134 3 VTLNDDNTMPVIGLGV---GELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASG-IPRGELFVTTKLAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsdahsnQPLDFDDVDfclTWEALEGCKDAGLVKSIGVSNFNRR 168
Cdd:cd19134 76 PDQGFTASQAACRASLERLGLDYVDLYLIHWP-----------AGREGKYVD---SWGGLMKLREEGLARSIGVSNFTAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 169 QLERLLSKPGlkYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNRS 248
Cdd:cd19134 142 HLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAAHGRT 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1785353101 249 PAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
7-290 |
1.99e-66 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 209.54 E-value: 1.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 7 TRLTLHDGNAIPVMGLGTY-ASAEvpksDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSkiadGTVKREEIFYTGK 85
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWqASNE----EVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 86 LWCSffSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvKPSDAHsnqpldfddvdFCLTWEALEGCKDAGLVKSIGVSNF 165
Cdd:PRK11565 77 LWND--DHKRPREALEESLKKLQLDYVDLYLMHWP---VPAIDH-----------YVEAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 166 NRRQLERLLSKPGLKykPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDNtwvdpnspvLLEDPVLRSVAAKY 245
Cdd:PRK11565 141 QIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG---------VFDQKVIRDLADKY 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1785353101 246 NRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDM 290
Cdd:PRK11565 210 GKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDEL 254
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
20-297 |
6.40e-66 |
|
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: 208.70 E-value: 6.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 20 MGLGTYA----SAEVPKSDGTEATKLAIDLGYRHIDCAYIYG---NEVQIGEAIrskiADGTVKREEIFYTGKL------ 86
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 87 WCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSvkpsdahsnqpldfdDVDFCLTWEALEGCKDAGLVKSIGVSNFN 166
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP---------------DTPIEETWDALEELKKEGKIRAIGVSNFD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 167 RRQLERLLSKPglKYKPVCNQVEYHVY--LNQSKLHEYCKCHNIVLVAYSVLG----------------TARDNTWVDPN 228
Cdd:pfam00248 142 AEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGgglltgkytrdpdkgpGERRRLLKKGT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785353101 229 SPVLLEDPVLRSVAAKYNRSPAEVAMRFILQ--KGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLN 297
Cdd:pfam00248 220 PLNLEALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
17-296 |
3.99e-63 |
|
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: 200.27 E-value: 3.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYasaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIrskiADGTVKREEIFYTGKLWCSFFSPNLV 96
Cdd:cd19139 1 IPAFGLGTF---RLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKDKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 97 RQGLEASLKALQLDYLDLFIMHWPfsvKPSDAhsnqpldfddVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQLERLLSK 176
Cdd:cd19139 74 LPSLEESLEKLRTDYVDLTLIHWP---SPNDE----------VPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 177 PGlKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNRSPAEVAMRF 256
Cdd:cd19139 141 VG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1785353101 257 ILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGL 296
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-294 |
2.93e-57 |
|
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: 186.67 E-value: 2.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 10 TLHDGNAIPVMGLGTYASaEVPKSDGTEATKLAIDLGYRHIDCAYIYGNEVQIGEAIRSKIADG-TVKREEIFYTGKLWC 88
Cdd:cd19122 2 TLNNGVKIPAVGFGTFAN-EGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDahSNQPLDFDDVDFCL----------TWEALEGCKDAGLVK 158
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKND--QRSPKLGPDGKYVIlkdltenpepTWRAMEEIYESGKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 159 SIGVSNFNRRQLERLLSKPglKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARDntwVDPNSPVLLEDPVL 238
Cdd:cd19122 159 AIGVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ---VPSTGERVSENPTL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785353101 239 RSVAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVfeFELKPEDMEMLD 294
Cdd:cd19122 234 NEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAIN 287
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-294 |
3.93e-57 |
|
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: 185.53 E-value: 3.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 9 LTLHDGNAIPVMGLGTYASAEVPKSDGTE--ATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgtvkREEIFYT 83
Cdd:cd19138 3 VTLPDGTKVPALGQGTWYMGEDPAKRAQEieALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 84 GKLWCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVkpsdahsnqPLDfddvdfcLTWEALEGCKDAGLVKSIGVS 163
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGV---------PLA-------ETVAAMEELKKEGKIRAWGVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 164 NFNRRQLERLLSKPGLKyKPVCNQVEYHVylnQSKLHEY-----CKCHNIVLVAYSVLGTARDntwvdpNSPVLLEDPVL 238
Cdd:cd19138 140 NFDTDDMEELWAVPGGG-NCAANQVLYNL---GSRGIEYdllpwCREHGVPVMAYSPLAQGGL------LRRGLLENPTL 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785353101 239 RSVAAKYNRSPAEVAMRFILQKGAVV-LAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19138 210 KEIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-301 |
1.16e-53 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 176.37 E-value: 1.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 16 AIPVMGLGTYASAEVPKSDgteATKLAIDLGYRHIDCAYIYGNEVQIGEAIrskiADGTVKREEIFYTGKLWCSFFSPNL 95
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVID---SVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 96 VRQGLEASLKALQLDYLDLFIMHWPfsvKPSDAhsnqpldfddVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQLERLLS 175
Cdd:PRK11172 75 LIPSLKESLQKLRTDYVDLTLIHWP---SPNDE----------VSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 176 KPGlKYKPVCNQVEYHVYLNQSKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLEDPVLRSVAAKYNRSPAEVAMR 255
Cdd:PRK11172 142 AVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATPAQVILA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1785353101 256 FILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNLR 301
Cdd:PRK11172 210 WAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
14-294 |
3.93e-49 |
|
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: 164.67 E-value: 3.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGTY--ASAEVPK----SDGTEATKLAIDLGYRHIDCAYIYG---NEVQIGEAIRSkiadgtVKREEIFYTG 84
Cdd:cd19137 1 GEKIPALGLGTWgiGGFLTPDysrdEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 85 KLWCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsdahsNQPLDFDDvdfclTWEALEGCKDAGLVKSIGVSN 164
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP----------NPNIPLEE-----TLSAMAEGVRQGLIRYIGVSN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 165 FNRRQLERLLSKpgLKYKPVCNQVEYHVY---LNQSKLHEYCKCHNIVLVAYSVLGTArdntwvdpnspVLLEDPVLRSV 241
Cdd:cd19137 140 FNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRG-----------LEKTNRTLEEI 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1785353101 242 AAKYNRSPAEVAMRFILQKGAVV-LAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19137 207 AKNYGKTIAQIALAWLIQKPNVVaIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
17-294 |
2.19e-47 |
|
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: 161.88 E-value: 2.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYA-SAEVPKSDGTEATKL---AIDLGYRHIDCAYIYG---NEVQIGEAIRSKiadgtvKREEIFYTGKL--- 86
Cdd:COG0667 13 VSRLGLGTMTfGGPWGGVDEAEAIAIldaALDAGINFFDTADVYGpgrSEELLGEALKGR------PRDDVVIATKVgrr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 87 -----WCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsdahsnqplDfDDVDFCLTWEALEGCKDAGLVKSIG 161
Cdd:COG0667 87 mgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP--------------D-PDTPIEETLGALDELVREGKIRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 162 VSNFNRRQLERLLSKPGLKYKPVCNQVEYHVyLNQSKLHE---YCKCHNIVLVAYSVL------GTARDNTWVDPNS--- 229
Cdd:COG0667 152 VSNYSAEQLRRALAIAEGLPPIVAVQNEYSL-LDRSAEEEllpAARELGVGVLAYSPLagglltGKYRRGATFPEGDraa 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785353101 230 -----PVLLED-----PVLRSVAAKYNRSPAEVAMRFILQKGAVVL----AKSfnPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:COG0667 231 tnfvqGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENLAAADLELSAEDLAALD 307
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
17-294 |
9.64e-47 |
|
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: 159.61 E-value: 9.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYA-----SAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAI---RSK--IAD--GTVKREEIF 81
Cdd:cd19084 4 VSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALkgrRDDvvIATkcGLRWDGGKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 82 YTGKLwcsffSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsDahsnqpldfDDVDFCLTWEALEGCKDAGLVKSIG 161
Cdd:cd19084 84 VTKDL-----SPESIRKEVEQSLRRLQTDYIDLYQIHWP------D---------PNTPIEETAEALEKLKKEGKIRYIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 162 VSNFNRRQLERLlskpgLKY-KPVCNQVEYHVyLNQ---SKLHEYCKCHNIVLVAYSVLGT------------------- 218
Cdd:cd19084 144 VSNFSVEQLEEA-----RKYgPIVSLQPPYSM-LEReieEELLPYCRENGIGVLPYGPLAQglltgkykkeptfppddrr 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 219 ARDNTWVDPNSPVLLE--DpVLRSVAAKYNRSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19084 218 SRFPFFRGENFEKNLEivD-KLKEIAEKYGKSLAQLAIAWTLAQPGVtsAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-294 |
8.25e-45 |
|
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: 154.31 E-value: 8.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYA---------SAEVPKsDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRskiadGTVKREEIFYTG 84
Cdd:cd19093 2 VSPLGLGTWQwgdrlwwgyGEYGDE-DLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLK-----ELGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 85 KLWC--SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDahsnqpldfddvdfCLTWEALEGCKDAGLVKSIGV 162
Cdd:cd19093 76 KFAPlpWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQI--------------EALMDGLADAVEEGLVRAVGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 163 SNFNRRQLER---LLSKPGlkYKPVCNQVEYH-VYLN--QSKLHEYCKCHNIVLVAYSVLGTAR-------DN------- 222
Cdd:cd19093 142 SNYSADQLRRahkALKERG--VPLASNQVEYSlLYRDpeQNGLLPACDELGITLIAYSPLAQGLltgkyspENpppggrr 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785353101 223 -----TWVDPNSPVLLEdpvLRSVAAKYNRSPAEVAMRFILQKGAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19093 220 rlfgrKNLEKVQPLLDA---LEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-300 |
1.30e-42 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 148.50 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGT------YASAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgtvkREEIFYTGKLW 87
Cdd:cd19085 1 VSRLGLGCwqfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 88 CSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSvkpsdahsnqpldfdDVDFCLTWEALEGCKDAGLVKSIGVSNFNR 167
Cdd:cd19085 74 PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSS---------------DVPLEETMEALEKLKEEGKIRAIGVSNFGP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 168 RQLERLLsKPGlkyKPVCNQVEYHVyLNQSKLHE---YCKCHNIVLVAYSVL-----------------GTARDNTWV-- 225
Cdd:cd19085 139 AQLEEAL-DAG---RIDSNQLPYNL-LWRAIEYEilpFCREHGIGVLAYSPLaqglltgkfssaedfppGDARTRLFRhf 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785353101 226 -DPNSPVLLED-PVLRSVAAKYNRSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNRNL 300
Cdd:cd19085 214 ePGAEEETFEAlEKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
18-279 |
7.13e-36 |
|
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: 129.18 E-value: 7.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 18 PVMGLGTYA-SAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgtVKREEIF--------YTGK 85
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGR-----GNRDDVViatkgghpPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 86 LWCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAhsnqpldfddvdfclTWEALEGCKDAGLVKSIGVSNF 165
Cdd:cd06660 76 PSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEE---------------TLEALNELVREGKIRYIGVSNW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 166 NRRQLERLL--SKPGLKYKPVCNQVEYHvYLNQSKLHE----YCKCHNIVLVAYSVLGtardntwvdpnspvlledpvlr 239
Cdd:cd06660 141 SAERLAEALayAKAHGLPGFAAVQPQYS-LLDRSPMEEelldWAEENGLPLLAYSPLA---------------------- 197
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1785353101 240 svaakynRSPAEVAMRFILQK--GAVVLAKSFNPTRLKQNLG 279
Cdd:cd06660 198 -------RGPAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-294 |
2.04e-33 |
|
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: 124.63 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 27 SAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN-EVQIGEAIRSKIADGTVKREEIFYTgKlWCSF-----FSPNLVRQGL 100
Cdd:cd19101 17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDAADDVQIHT-K-WVPDpgeltMTRAYVEAAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 101 EASLKALQLDYLDLFIMHWpfsvkpsdahsnqpLDFDDVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQLERLLSKPglk 180
Cdd:cd19101 95 DRSLKRLGVDRLDLVQFHW--------------WDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 181 YKPVCNQVEYHVyLNQ---SKLHEYCKCHNIVLVAYSVLG---------TARDNTWVDPNSPV----------------- 231
Cdd:cd19101 158 VPIVSNQVQYSL-LDRrpeNGMAALCEDHGIKLLAYGTLAggllsekylGVPEPTGPALETRSlqkyklmidewggwdlf 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785353101 232 --LLEdpVLRSVAAKYNRSPAEVAMRFILQK----GAVVLAKsfNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19101 237 qeLLR--TLKAIADKHGVSIANVAVRWVLDQpgvaGVIVGAR--NSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-296 |
5.83e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 118.16 E-value: 5.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYASA---------EVPKSDGTEATKLAIDLGYRHIDCAYIYG---NEVQIGEAIRSkiadgtVKREEIFYT- 83
Cdd:cd19102 1 LTTIGLGTWAIGgggwgggwgPQDDRDSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKG------LRDRPIVATk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 84 -GKLW------CSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsdahsnqplDFDDvDFCLTWEALEGCKDAGL 156
Cdd:cd19102 75 cGLLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWP--------------DPDE-PIEEAWGALAELKEEGK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 157 VKSIGVSNFNRRQLERLLSKPGLKYkpvcNQVEYhvylnqSKLHE--------YCKCHNIVLVAYSVLG----------- 217
Cdd:cd19102 140 VRAIGVSNFSVDQMKRCQAIHPIAS----LQPPY------SLLRRgieaeilpFCAEHGIGVIVYSPMQsglltgkmtpe 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 218 ---TARDNTWvDPNSPVLLED---------PVLRSVAAKYNRSPAEVAMRFILQK----GAVVLAKsfNPTRLKQNLGVF 281
Cdd:cd19102 210 rvaSLPADDW-RRRSPFFQEPnlarnlalvDALRPIAERHGRTVAQLAIAWVLRRpevtSAIVGAR--RPDQIDETVGAA 286
|
330
....*....|....*
gi 1785353101 282 EFELKPEDMEMLDGL 296
Cdd:cd19102 287 DLRLTPEELAEIEAL 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
42-289 |
1.17e-27 |
|
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: 108.80 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 42 AIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgTVKREEIF-------YTGKLWCSF------FSPNLVRQGLEASLK 105
Cdd:cd19092 33 ALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEiqtkcgiRLGDDPRPGrikhydTSKEHILASVEGSLK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 106 ALQLDYLDLFIMHWPfsvkpsDahsnqPL-DFDDVDfcltwEALEGCKDAGLVKSIGVSNFNRRQLERLLSKpgLKYKPV 184
Cdd:cd19092 109 RLGTDYLDLLLLHRP------D-----PLmDPEEVA-----EAFDELVKSGKVRYFGVSNFTPSQIELLQSY--LDQPLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 185 CNQVEYHVyLNQSKLH----EYCKCHNIVLVAYSVLGTARDNTWVDPNSPVLLEdpVLRSVAAKYNRSPAEVAMRFILQK 260
Cdd:cd19092 171 TNQIELSL-LHTEAIDdgtlDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA--ALEELAEEYGVTIEAIALAWLLRH 247
|
250 260 270
....*....|....*....|....*....|.
gi 1785353101 261 GA--VVLAKSFNPTRLKQNLGVFEFELKPED 289
Cdd:cd19092 248 PAriQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
17-285 |
2.24e-26 |
|
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: 104.61 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGT------YASAEVPKSDGTEAT-KLAIDLGYRHIDCAYIYG---NEVQIGEAIRSKIAD-------GTVKREe 79
Cdd:cd19088 1 VSRLGYGAmrltgpGIWGPPADREEAIAVlRRALELGVNFIDTADSYGpdvNERLIAEALHPYPDDvviatkgGLVRTG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 80 ifytGKLWCSFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPsdahsnqpldFDDvdfclTWEALEGCKDAGLVKS 159
Cdd:cd19088 80 ----PGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVP----------FEE-----QLGALAELQDEGLIRH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 160 IGVSNFNRRQLERLLSKPGLkykpVCNQVEYHVYLNQS-KLHEYCKCHNIVLVAYSVLGTARDntwvdpnspvLLEDPVL 238
Cdd:cd19088 141 IGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDDeGVLDYCEAAGIAFIPWFPLGGGDL----------AQPGGLL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1785353101 239 RSVAAKYNRSPAEVAMRFILQKGAVVLA--KSFNPTRLKQNLGVFEFEL 285
Cdd:cd19088 207 AEVAARLGATPAQVALAWLLARSPVMLPipGTSSVEHLEENLAAAGLRL 255
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
40-289 |
7.26e-26 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 104.46 E-value: 7.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 40 KLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgTVKREEI---------FYTGKLWCSF----FSPNLVRQGLEAS 103
Cdd:COG4989 38 EAALELGITTFDHADIYGGytcEALFGEALKLS----PSLREKIelqtkcgirLPSEARDNRVkhydTSKEHIIASVEGS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 104 LKALQLDYLDLFIMHwpfsvKPSdahsnqPL-DFDDVDfcltwEALEGCKDAGLVKSIGVSNFNRRQLErLLSKpGLKYK 182
Cdd:COG4989 114 LRRLGTDYLDLLLLH-----RPD------PLmDPEEVA-----EAFDELKASGKVRHFGVSNFTPSQFE-LLQS-ALDQP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 183 PVCNQVEYHVyLNQSKLH----EYCKCHNIVLVAYSVLGTARDNTWVDPNSPVLLEdpVLRSVAAKYNRSPAEVAMRFIL 258
Cdd:COG4989 176 LVTNQIELSL-LHTDAFDdgtlDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRA--ALDELAEKYGVSPEAIALAWLL 252
|
250 260 270
....*....|....*....|....*....|...
gi 1785353101 259 Q--KGAVVLAKSFNPTRLKQNLGVFEFELKPED 289
Cdd:COG4989 253 RhpAGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-294 |
1.10e-25 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 104.23 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 12 HDGNAIPVMGLG--TYASAEVPKS-----DGTEATKL---AIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgtvkRE 78
Cdd:cd19091 8 RSGLKVSELALGtmTFGGGGGFFGawggvDQEEADRLvdiALDAGINFFDTADVYSEgesEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 79 EIFYTGKLwcSF-FSPNLVRQGL---------EASLKALQLDYLDLFIMHWPfsvkpsDAHSnqPLDfddvdfcLTWEAL 148
Cdd:cd19091 81 DVLIATKV--RGrMGEGPNDVGLsrhhiiravEASLKRLGTDYIDLYQLHGF------DALT--PLE-------ETLRAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 149 EGCKDAGLVKSIGVSNFNRRQLERLLS---KPGLKyKPVCNQVEYHVyLNQSKLHE---YCKCHNIVLVAYSVL------ 216
Cdd:cd19091 144 DDLVRQGKVRYIGVSNFSAWQIMKALGiseRRGLA-RFVALQAYYSL-LGRDLEHElmpLALDQGVGLLVWSPLagglls 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 217 -----------GTARDNTWVD--PNSPVLLEDPV--LRSVAAKYNRSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLG 279
Cdd:cd19091 222 gkyrrgqpapeGSRLRRTGFDfpPVDRERGYDVVdaLREIAKETGATPAQVALAWLLSRPTVssVIIGARNEEQLEDNLG 301
|
330
....*....|....*
gi 1785353101 280 VFEFELKPEDMEMLD 294
Cdd:cd19091 302 AAGLSLTPEEIARLD 316
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
18-288 |
1.67e-24 |
|
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: 100.32 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 18 PVMGLGTY----ASAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN-EVQIGEAIRskiadgTVKREEIFYTGKLWC---- 88
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA------ELPREPLVLSTKVGRlped 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 -SFFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHSNQPldfddvdfclTWEALEGCKDAGLVKSIGVS---- 163
Cdd:cd19090 75 tADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPGG----------ALEALLELKEEGLIKHIGLGggpp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 164 NFNRRQLER-----LLSkpglkykpvcnqveYHVY--LNQSKLHE---YCKCHNIVLVAYSVLG----TARDNTWVDPNS 229
Cdd:cd19090 145 DLLRRAIETgdfdvVLT--------------ANRYtlLDQSAADEllpAAARHGVGVINASPLGmgllAGRPPERVRYTY 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785353101 230 PVLLEDPVLRS-----VAAKYNRSPAEVAMRFILQ---KGAVVLAKSfNPTRLKQNLGVFEFELKPE 288
Cdd:cd19090 211 RWLSPELLDRAkrlyeLCDEHGVPLPALALRFLLRdprISTVLVGAS-SPEELEQNVAAAEGPLPEE 276
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
18-280 |
1.44e-23 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 96.92 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 18 PVMGLGT---YASAEVPkSDGtEATKL---AIDLGYRHIDCAYIYGN-EVQIGEAIRskiadgTVKREEIFYTGKLWCSF 90
Cdd:cd19095 1 SVLGLGTsgiGRVWGVP-SEA-EAARLlntALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVGTHG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 91 --------FSPNLVRQGLEASLKALQLDYLDLFIMHwpfsvKPSDAHSNQPLdfddvdfcltWEALEGCKDAGLVKSIGV 162
Cdd:cd19095 73 eggrdrkdFSPAAIRASIERSLRRLGTDYIDLLQLH-----GPSDDELTGEV----------LETLEDLKAAGKVRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 163 SNFNRRqLERLLSKPGLKykpvCNQVEYHVyLNQS------KLHEyckcHNIVLVAYSVLGTARDNTWVDPNSPVLLEDP 236
Cdd:cd19095 138 SGDGEE-LEAAIASGVFD----VVQLPYNV-LDREeeellpLAAE----AGLGVIVNRPLANGRLRRRVRRRPLYADYAR 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1785353101 237 VLRSVAAKYNRSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLGV 280
Cdd:cd19095 208 RPEFAAEIGGATWAQAALRFVLSHPGVssAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-289 |
2.12e-23 |
|
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: 97.73 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYASAEVP---KSDGTEATKL---AIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgtvkREEIFYTGKlw 87
Cdd:cd19149 11 ASVIGLGTWAIGGGPwwgGSDDNESIRTihaALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATK-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 88 C---------SFF------------SPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsdahsnqpldfdDVDFCL--T 144
Cdd:cd19149 82 CglrwdreggSFFfvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQ-----------------DVETPIeeT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 145 WEALEGCKDAGLVKSIGVSNFNRRQLERLlskpgLKYKPV-CNQVEYHVyLN---QSKLHEYCKCHNIVLVAYSVL---- 216
Cdd:cd19149 145 MEALEELKRQGKIRAIGASNVSVEQIKEY-----VKAGQLdIIQEKYSM-LDrgiEKELLPYCKKNNIAFQAYSPLeqgl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 217 -------------GTAR-DNTWVDPNS--PVLLEDPVLRSVAAKYNRSPAEVAMRFILQKG--AVVLAKSFNPTRLKQNL 278
Cdd:cd19149 219 ltgkitpdrefdaGDARsGIPWFSPENreKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENA 298
|
330
....*....|.
gi 1785353101 279 GVFEFELKPED 289
Cdd:cd19149 299 KAGDIRLSAED 309
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-174 |
3.77e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 95.63 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGTYASAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN-EVQIGEAIRSKiadgtvkREEIFYTGKLWcsFFS 92
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTG--ARD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 93 PNLVRQGLEASLKALQLDYLDLFIMHwpfSVKPSDahsnqplDFDDVDFCL-TWEALEGCKDAGLVKSIGVSNFNRRQLE 171
Cdd:cd19100 79 YEGAKRDLERSLKRLGTDYIDLYQLH---AVDTEE-------DLDQVFGPGgALEALLEAKEEGKIRFIGISGHSPEVLL 148
|
...
gi 1785353101 172 RLL 174
Cdd:cd19100 149 RAL 151
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
14-301 |
5.96e-22 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 94.50 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGT--YasaevPKSDGTEATKL---AIDLGYRHIDCAYIYGN-EVQIGEAIRSKiadgtvkREEIFYTGKL- 86
Cdd:COG1453 10 GLEVSVLGFGGmrL-----PRKDEEEAEALirrAIDNGINYIDTARGYGDsEEFLGKALKGP-------RDKVILATKLp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 87 -WCSffSPNLVRQGLEASLKALQLDYLDLFIMH-------WPFSVKPSDAhsnqpldfddvdfcltWEALEGCKDAGLVK 158
Cdd:COG1453 78 pWVR--DPEDMRKDLEESLKRLQTDYIDLYLIHglnteedLEKVLKPGGA----------------LEALEKAKAEGKIR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 159 SIGVSNFNRRQLERLLskpgLKYKP--VCnQVEYHvYLNQS-----KLHEYCKCHNIVLVAYSVLGTARdntwvdpnspv 231
Cdd:COG1453 140 HIGFSTHGSLEVIKEA----IDTGDfdFV-QLQYN-YLDQDnqageEALEAAAEKGIGVIIMKPLKGGR----------- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785353101 232 LLEDPVLRSVAAKYNRSPAEVAMRFILQKGAVVLAKS--FNPTRLKQNLGVFE-FE-LKPEDMEMLDGLNRNLR 301
Cdd:COG1453 203 LANPPEKLVELLCPPLSPAEWALRFLLSHPEVTTVLSgmSTPEQLDENLKTADnLEpLTEEELAILERLAEELG 276
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
20-296 |
5.98e-22 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 93.64 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 20 MGLGTYASA------EVPKSDGTEATKLAIDLGYRHIDCAYIYG---NEVQIGEAIRSKiadgtvKREEIFYTGKLWCSF 90
Cdd:cd19083 14 IGLGTNAVGghnlypNLDEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEY------NRNEVVIATKGAHKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 91 F--------SPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsDAHSnqPLDfDDVDfcltweALEGCKDAGLVKSIGV 162
Cdd:cd19083 88 GgdgsvlnnSPEFLRSAVEKSLKRLNTDYIDLYYIHFP------DGET--PKA-EAVG------ALQELKDEGKIRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 163 SNFNRRQLERlLSKPGlkYKPVCnQVEYHVyLNQ---SKLHEYCKCHNIVLVAYSVL------GTARDNTWVDPN----- 228
Cdd:cd19083 153 SNFSLEQLKE-ANKDG--YVDVL-QGEYNL-LQReaeEDILPYCVENNISFIPYFPLasgllaGKYTKDTKFPDNdlrnd 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785353101 229 ---------SPVLLEDPVLRSVAAKYNRSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGL 296
Cdd:cd19083 228 kplfkgerfSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
18-287 |
2.35e-21 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 91.08 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 18 PVMGLGT--YASAEVPKSDGTEATKL---AIDLGYRHIDCAYIYGN---EVQIGEAIRskiadgTVKREEIFYTGKL-WC 88
Cdd:cd19096 1 SVLGFGTmrLPESDDDSIDEEKAIEMiryAIDAGINYFDTAYGYGGgksEEILGEALK------EGPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 SFFSPNLVRQGLEASLKALQLDYLDLFIMH------WPFSVKPSDAhsnqpldfddvdfcltWEALEGCKDAGLVKSIGV 162
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHglnspeWLEKARKGGL----------------LEFLEKAKKEGLIRHIGF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 163 SnF--NRRQLERLLSkpglKYKPVCNQVEYHvYLNQ-----SKLHEYCKCHNIVLVAYSVLGTARdntwvdpnspvLLED 235
Cdd:cd19096 139 S-FhdSPELLKEILD----SYDFDFVQLQYN-YLDQenqagRPGIEYAAKKGMGVIIMEPLKGGG-----------LANN 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1785353101 236 P-VLRSVAAKYNRSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLGVFEfELKP 287
Cdd:cd19096 202 PpEALAILCGAPLSPAEWALRFLLSHPEVttVLSGMSTPEQLDENIAAAD-EFEP 255
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
17-288 |
7.21e-21 |
|
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: 90.73 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYA--SAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRskiadgTVKREEIFYTGKLwcsFF 91
Cdd:cd19074 4 VSELSLGTWLtfGGQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK------GWPRESYVISTKV---FW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 92 --SPNLVRQGL---------EASLKALQLDYLDLFIMHWPfsvkpsdahsnqpldfdDVDFCL--TWEALEGCKDAGLVK 158
Cdd:cd19074 75 ptGPGPNDRGLsrkhifesiHASLKRLQLDYVDIYYCHRY-----------------DPETPLeeTVRAMDDLIRQGKIL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 159 SIGVSNFNRRQLERL--LSKPGLKYKPVCNQVEYHvYLNQSKLHE---YCKCHNIVLVAYSVL----------------- 216
Cdd:cd19074 138 YWGTSEWSAEQIAEAhdLARQFGLIPPVVEQPQYN-MLWREIEEEvipLCEKNGIGLVVWSPLaqglltgkyrdgippps 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 217 -GTARDNT---WVDPnspvLLEDPV------LRSVAAKYNRSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLGVFEFE 284
Cdd:cd19074 217 rSRATDEDnrdKKRR----LLTDENlekvkkLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVK 292
|
....
gi 1785353101 285 LKPE 288
Cdd:cd19074 293 LSPE 296
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
43-294 |
1.47e-20 |
|
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: 89.97 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 43 IDLGYRHIDCAYIYGN----------EVQIGEAIRSKiadgtVKREEIFYTGKLWCSF------FSPNLVRQGLEASLKA 106
Cdd:cd19081 36 VDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKSR-----GKRDRVVIATKVGFPMgpngpgLSRKHIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 107 LQLDYLDLFIMHWPfsvkpsdaHSNQPLDfddvdfcLTWEALEGCKDAGLVKSIGVSNFNRRQLERLL--SKPGLKYKPV 184
Cdd:cd19081 111 LQTDYIDLYQAHWD--------DPATPLE-------ETLGALNDLIRQGKVRYIGASNYSAWRLQEALelSRQHGLPRYV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 185 CNQVEYHVYLNQS---KLHEYCKCHNIVLVAYSVL---------------------GTARDNTWVDPNSPVLledPVLRS 240
Cdd:cd19081 176 SLQPEYNLVDRESfegELLPLCREEGIGVIPYSPLaggfltgkyrseadlpgstrrGEAAKRYLNERGLRIL---DALDE 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785353101 241 VAAKYNRSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19081 253 VAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
20-294 |
1.80e-20 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 89.57 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 20 MGLGTYASAE--VPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKIadgtvKREEIFYTGKLwcsFF--- 91
Cdd:cd19079 20 MSFGDPKWRPwvLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKV---YFpmg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 92 -SPN---LVR----QGLEASLKALQLDYLDLFIMHWPfsvkpsdahsnqpldFDDVDFCLTWEALEGCKDAGLVKSIGVS 163
Cdd:cd19079 92 dGPNgrgLSRkhimAEVDASLKRLGTDYIDLYQIHRW---------------DYETPIEETLEALHDVVKSGKVRYIGAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 164 NFNRRQLERLL---SKPGLKyKPVCNQvEYHVYLNQSKLHE---YCKCHNIVLVAYSVL------GTARDNT---WVDPN 228
Cdd:cd19079 157 SMYAWQFAKALhlaEKNGWT-KFVSMQ-NHYNLLYREEEREmipLCEEEGIGVIPWSPLargrlaRPWGDTTerrRSTTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 229 SPVLLED-------PVLRSV---AAKYNRSPAEVAMRFILQKGAVV-----LAKsfnPTRLKQNLGVFEFELKPEDMEML 293
Cdd:cd19079 235 TAKLKYDyfteadkEIVDRVeevAKERGVSMAQVALAWLLSKPGVTapivgATK---LEHLEDAVAALDIKLSEEEIKYL 311
|
.
gi 1785353101 294 D 294
Cdd:cd19079 312 E 312
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
17-263 |
5.49e-20 |
|
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: 86.76 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYA--SAEVPKSDGTEATKL---AIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgtvkREEI-------- 80
Cdd:cd19086 3 VSEIGFGTWGlgGDWWGDVDDAEAIRAlraALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVviatkfgn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 81 -FYTGKLWCSFFSPNLVRQGLEASLKALQLDYLDLFIMH-WPFSVKPSDAHsnqpldfddvdfcltWEALEGCKDAGLVK 158
Cdd:cd19086 76 rFDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDEL---------------FEALEKLKQEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 159 SIGVSNFNRRQLERLLSKPGLkykpVCNQVEYHVyLNQSKLHE---YCKCHNIVLVAYSVLgtarDNTWVDPNspvlled 235
Cdd:cd19086 141 AYGVSVGDPEEALAALRRGGI----DVVQVIYNL-LDQRPEEElfpLAEEHGVGVIARVPL----ASGLLTGK------- 204
|
250 260
....*....|....*....|....*...
gi 1785353101 236 pvlrsvaakynrsPAEVAMRFILQKGAV 263
Cdd:cd19086 205 -------------LAQAALRFILSHPAV 219
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
42-294 |
9.51e-20 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 87.75 E-value: 9.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 42 AIDLGYRHIDCAYIYG---NEVQIGEAIRskiadGTVKREEIFYTGKL---W------CSFFSPNLVRQGLEASLKALQL 109
Cdd:cd19148 34 ALDLGINLIDTAPVYGfglSEEIVGKALK-----EYGKRDRVVIATKVgleWdeggevVRNSSPARIRKEVEDSLRRLQT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 110 DYLDLFIMHWPFSVKPsdahsnqpldFDDvdfclTWEALEGCKDAGLVKSIGVSNFNRRQLERLLSKPGLKykpvCNQVE 189
Cdd:cd19148 109 DYIDLYQVHWPDPLVP----------IEE-----TAEALKELLDEGKIRAIGVSNFSPEQMETFRKVAPLH----TVQPP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 190 YHVYLNQSK--LHEYCKCHNIVLVAYSVL------GTARDNTWVDP-----NSPVLLEDPVLRSVAA----------KYN 246
Cdd:cd19148 170 YNLFEREIEkdVLPYARKHNIVTLAYGALcrgllsGKMTKDTKFEGddlrrTDPKFQEPRFSQYLAAveeldklaqeRYG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1785353101 247 RSPAEVAMRFILQKGA--VVLAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19148 250 KSVIHLAVRWLLDQPGvsIALWGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
32-294 |
6.48e-18 |
|
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: 82.61 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 32 KSDGTEATKLAIDLGYRHIDCAYIY---------G-NEVQIGEAIR-----------SKIADGTVKREEIFYTGklwcSF 90
Cdd:cd19094 17 EAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqGrTEEIIGSWLKkkgnrdkvvlaTKVAGPGEGITWPRGGG----TR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 91 FSPNLVRQGLEASLKALQLDYLDLFIMHWP-----FSVKPSDAHSNQPLDFddVDFCLTWEALEGCKDAGLVKSIGVSN- 164
Cdd:cd19094 93 LDRENIREAVEGSLKRLGTDYIDLYQLHWPdrytpLFGGGYYTEPSEEEDS--VSFEEQLEALGELVKAGKIRHIGLSNe 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 165 --FNRRQLERLLSKPGLKyKPVCNQVEYHVyLNQSK---LHEYCKCHNIVLVAYSVLG----------------TARDNT 223
Cdd:cd19094 171 tpWGVMKFLELAEQLGLP-RIVSIQNPYSL-LNRNFeegLAEACHRENVGLLAYSPLAggvltgkyldgaarpeGGRLNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 224 --WVDP--NSPVLLEdPVLR--SVAAKYNRSPAEVAMRFILQKGAV----VLAKSFNptRLKQNLGVFEFELKPEDMEML 293
Cdd:cd19094 249 fpGYMAryRSPQALE-AVAEyvKLARKHGLSPAQLALAWVRSRPFVtstiIGATTLE--QLKENIDAFDVPLSDELLAEI 325
|
.
gi 1785353101 294 D 294
Cdd:cd19094 326 D 326
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-263 |
8.20e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 82.00 E-value: 8.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 42 AIDLGYRHIDCAYIYG---NEVQIGEAIRskiadgTVKREEIFYTGKL--WCSFFSPNLVRQGLEASLKALQLDYLDLFI 116
Cdd:cd19103 41 AMAAGLNLWDTAAVYGmgaSEKILGEFLK------RYPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 117 MHwpfsvKPSDAHSNQPldfddvdfcltwEALEGCKDaGLVKSIGVSNFNRRQLER---LLSKPGLKYKPVCNqveyHVY 193
Cdd:cd19103 115 IH-----NPADVERWTP------------ELIPLLKS-GKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQN----HYS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 194 L-----NQSKLHEYCKCHNIVLVAYSVL-----------------GTARDNTWvdpnSPVL--LED--PVLRSVAAKYNR 247
Cdd:cd19103 173 LlyrssEEAGILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGRAETY----NPLLpqLEEltAVMAEIGAKHGA 248
|
250
....*....|....*.
gi 1785353101 248 SPAEVAMRFILQKGAV 263
Cdd:cd19103 249 SIAQVAIAWAIAKGTT 264
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-259 |
9.89e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 81.42 E-value: 9.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 40 KLAIDLGYRHIDCAYIYGN-EVQIGEAIRSKiadgtvkrEEIFYTGKL----WCSFFSPNLVRQGLEASLKALQLDYLDL 114
Cdd:cd19097 33 EYALKAGINTLDTAPAYGDsEKVLGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLDG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 115 FIMHwpfsvKPSDAHSNQPLdfddvdfclTWEALEGCKDAGLVKSIGVSNFNRRQLERLLSKPGLKYkpVcnQVEYHVyL 194
Cdd:cd19097 105 LLLH-----NPDDLLKHGGK---------LVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI--I--QLPFNI-L 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785353101 195 NQ--------SKLHEyckcHNIVLVAYSVL--G--TARDNTWVDPNSPV--LLEDpvLRSVAAKYNRSPAEVAMRFILQ 259
Cdd:cd19097 166 DQrflksgllAKLKK----KGIEIHARSVFlqGllLMEPDKLPAKFAPAkpLLKK--LHELAKKLGLSPLELALGFVLS 238
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-280 |
1.30e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 80.71 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYASAevpkSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRskiadgTVKREEIFYTGKLWCS--FF 91
Cdd:cd19105 13 VSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATKASPRldKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 92 SPNLVRQGLEASLKALQLDYLDLFIMHwpfsvkpsdaHSNQPLDFDDVDFCLtwEALEGCKDAGLVKSIGVS--NFNRRQ 169
Cdd:cd19105 83 DKAELLKSVEESLKRLQTDYIDIYQLH----------GVDTPEERLLNEELL--EALEKLKKEGKVRFIGFSthDNMAEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 170 LERLLSKPG-----LKYkpvcNQVEYHVYLNqsKLHEYCKCHNIVLVAYSVLGTARDNTWVDPnsPVLLEDPvlrsvaak 244
Cdd:cd19105 151 LQAAIESGWfdvimVAY----NFLNQPAELE--EALAAAAEKGIGVVAMKTLAGGYLQPALLS--VLKAKGF-------- 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 1785353101 245 ynrSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLGV 280
Cdd:cd19105 215 ---SLPQAALKWVLSNPRVdtVVPGMRNFAELEENLAA 249
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-258 |
3.67e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 80.39 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 8 RLTLHDGNAIPVMGLGTYAsaevpksDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgtvkREEIFYTG 84
Cdd:cd19104 14 ELTFGGGGIGGLMGRTTRE-------EQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL-------PAGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 85 KlwCSFFSPNL------VRQGLEASLKALQLDYLDLFIMH--------WPFSVKPSDAHSnqpLDFDDVdfcltWEALEG 150
Cdd:cd19104 80 K--VRLDPDDLgdiggqIERSVEKSLKRLKRDSVDLLQLHnrigderdKPVGGTLSTTDV---LGLGGV-----ADAFER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 151 CKDAGLVKSIGVSNF-NRRQLERLLSKPglkyKPVCNQVEYHVyLNQS---------------KLHEYCKCHNIVLVAYS 214
Cdd:cd19104 150 LRSEGKIRFIGITGLgNPPAIRELLDSG----KFDAVQVYYNL-LNPSaaearprgwsaqdygGIIDAAAEHGVGVMGIR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1785353101 215 VL--GTARDNTWVDPNSPVLLEDPV---------LRSVAAKYNRSPAEVAMRFIL 258
Cdd:cd19104 225 VLaaGALTTSLDRGREAPPTSDSDVaidfrraaaFRALAREWGETLAQLAHRFAL 279
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
17-293 |
1.94e-16 |
|
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: 78.03 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLG----TYASAEVPKSDGTEATKLAIDLGYRHIDCAYIYG---NEVQIGEAIRSKiadgtvkREEIFYTGK---L 86
Cdd:cd19076 12 VSALGLGcmgmSAFYGPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATKfgiV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 87 WCSFF-------SPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsDahSNQPLDfddvdfcLTWEALEGCKDAGLVKS 159
Cdd:cd19076 85 RDPGSgfrgvdgRPEYVRAACEASLKRLGTDVIDLYYQHRV------D--PNVPIE-------ETVGAMAELVEEGKVRY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 160 IGVSNFNRRQLERL-----LSKPGLKYKPVCNQVEYHVYlnqsklhEYCKCHNIVLVAYSVLGtaRDNTWVDPNSPVLLE 234
Cdd:cd19076 150 IGLSEASADTIRRAhavhpITAVQSEYSLWTRDIEDEVL-------PTCRELGIGFVAYSPLG--RGFLTGAIKSPEDLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 235 -------DP---------------VLRSVAAKYNRSPAEVAMRFILQKGAVVL----AKSfnPTRLKQNLGVFEFELKPE 288
Cdd:cd19076 221 eddfrrnNPrfqgenfdknlklveKLEAIAAEKGCTPAQLALAWVLAQGDDIVpipgTKR--IKYLEENVGALDVVLTPE 298
|
....*
gi 1785353101 289 DMEML 293
Cdd:cd19076 299 ELAEI 303
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
13-289 |
2.93e-16 |
|
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: 77.87 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 13 DGNAIPVMGLGT---YASAEVPKSDgTEATKL---AIDLGYRHIDCAYIYG-NEVQIGEAIrsKIADGtvKREEIFY--- 82
Cdd:cd19144 9 NGPSVPALGFGAmglSAFYGPPKPD-EERFAVldaAFELGCTFWDTADIYGdSEELIGRWF--KQNPG--KREKIFLatk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 83 --------TGKLWCSFfSPNLVRQGLEASLKALQLDYLDLFIMHwpfSVKPSdahsnQPLDfddvdfcLTWEALEGCKDA 154
Cdd:cd19144 84 fgieknveTGEYSVDG-SPEYVKKACETSLKRLGVDYIDLYYQH---RVDGK-----TPIE-------KTVAAMAELVQE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 155 GLVKSIGVSNFNRRQLERllskpGLKYKPVCN-QVEYHVYL-----NQSKLHEYCKCHNIVLVAYSVL------GTARDN 222
Cdd:cd19144 148 GKIKHIGLSECSAETLRR-----AHAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLgrgfltGAIRSP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 223 TWVDP-------------NSPVLLE--DPvLRSVAAKYNRSPAEVAMRFILQKGA--VVLAKSFNPTRLKQNLGVFEFEL 285
Cdd:cd19144 223 DDFEEgdfrrmaprfqaeNFPKNLElvDK-IKAIAKKKNVTAGQLTLAWLLAQGDdiIPIPGTTKLKRLEENLGALKVKL 301
|
....
gi 1785353101 286 KPED 289
Cdd:cd19144 302 TEEE 305
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-294 |
4.94e-16 |
|
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: 76.89 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 19 VMGLgTYASAEVP-KSDGTEATKLAIDLGYRHIDCAYIYG---NEVQIGEAIRSKiadgtvkREEIFYTGKLWCSFF--- 91
Cdd:cd19078 11 CMGM-SHGYGPPPdKEEMIELIRKAVELGITFFDTAEVYGpytNEELVGEALKPF-------RDQVVIATKFGFKIDggk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 92 --------SPNLVRQGLEASLKALQLDYLDLFIMHwpfSVKPsdahsNQPLDfddvdfcltwEALEGCKD---AGLVKSI 160
Cdd:cd19078 83 pgplgldsRPEHIRKAVEGSLKRLQTDYIDLYYQH---RVDP-----NVPIE----------EVAGTMKElikEGKIRHW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 161 GVSNFNRRQLERllskpGLKYKPVCN-QVEYHVYLN--QSKLHEYCKCHNIVLVAYSVLG----TAR-----------DN 222
Cdd:cd19078 145 GLSEAGVETIRR-----AHAVCPVTAvQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLGkgflTGKidentkfdegdDR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 223 TWVDPNSP-------VLLEdpVLRSVAAKYNRSPAEVAMRFILQKGA--VVLAKSFNPTRLKQNLGVFEFELKPEDMEML 293
Cdd:cd19078 220 ASLPRFTPealeanqALVD--LLKEFAEEKGATPAQIALAWLLAKKPwiVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
.
gi 1785353101 294 D 294
Cdd:cd19078 298 E 298
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-163 |
1.16e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 76.20 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 20 MGLGTYASAEVPKSD--GTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKIADGTVKREEIFYTGK--------- 85
Cdd:cd19099 6 LGLGTYRGDSDDETDeeYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 86 -------------------------LW-CsfFSPNLVRQGLEASLKALQLDYLDLFIMHWPFSVKPSDAHSNQPLDFDDV 139
Cdd:cd19099 86 eplrplkyleeklgrglidvadsagLRhC--ISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLELGEEEFYDRLEEA 163
|
170 180
....*....|....*....|....
gi 1785353101 140 dfcltWEALEGCKDAGLVKSIGVS 163
Cdd:cd19099 164 -----FEALEEAVAEGKIRYYGIS 182
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
42-296 |
9.01e-15 |
|
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: 73.38 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 42 AIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgtvkREEIFYTGK--------LWCSFFSPNLVRQGLEASLKALQLD 110
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKvfgpmgddPNDRGLSRRHIRRAVEASLRRLQTD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 111 YLDLFIMHWPFsvkpsdahSNQPLDfddvdfcLTWEALEGCKDAGLVKSIGVSNF------------NRRQLERLLS-KP 177
Cdd:cd19087 112 YIDLYQMHHFD--------RDTPLE-------ETLRALDDLVRQGKIRYIGVSNFaawqiakaqgiaARRGLLRFVSeQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 178 glKYKPVCNQVEYHVYlnqsklhEYCKCHNIVLVAYSVLG------------TARDNTWVDPNSPVLLE-DPVLRSVAAK 244
Cdd:cd19087 177 --MYNLLKRQAELEIL-------PAARAYGLGVIPYSPLAgglltgkygkgkRPESGRLVERARYQARYgLEEYRDIAER 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785353101 245 YNR-------SPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLGVFEFELKPEDMEMLDGL 296
Cdd:cd19087 248 FEAlaaeaglTPASLALAWVLSHPAVtsPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
18-278 |
1.45e-14 |
|
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: 72.59 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 18 PVMGLGT-YASAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN-------EVQIGEAIRSKIadgtvKREEIF-------- 81
Cdd:cd19082 1 SRIVLGTaDFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwvergasERVIGEWLKSRG-----NRDKVViatkgghp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 82 YTGKLWCSFFSPNLVRQGLEASLKALQLDYLDLFIMHwpfsvkpsdahsnqpldFDD----VDFCLtwEALEGCKDAGLV 157
Cdd:cd19082 76 DLEDMSRSRLSPEDIRADLEESLERLGTDYIDLYFLH-----------------RDDpsvpVGEIV--DTLNELVRAGKI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 158 KSIGVSNFNrrqLERLL------SKPGLkYKPVCNQVEYH--------------VYLNQSkLHEYCKCHNIVLVAYSVLG 217
Cdd:cd19082 137 RAFGASNWS---TERIAeanayaKAHGL-PGFAASSPQWSlarpneppwpgptlVAMDEE-MRAWHEENQLPVFAYSSQA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 218 ----TARDNTWVDPNSPVL-----------LEdpVLRSVAAKYNRSPAEVAMRFILQKG----AVVLAKSfnPTRLKQNL 278
Cdd:cd19082 212 rgffSKRAAGGAEDDSELRrvyyseenferLE--RAKELAEEKGVSPTQIALAYVLNQPfptvPIIGPRT--PEQLRDSL 287
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
14-288 |
8.74e-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: 70.27 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGtyASA------EVPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRskiadgTVKREEIF--- 81
Cdd:cd19163 10 GLKVSKLGFG--ASPlggvfgPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALK------GIPRDSYYlat 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 82 ----YTGKLWCSF-FSPNLVRQGLEASLKALQLDYLDLFIMHwpfsvkpsdahsnqpldfdDVDFCL--------TWEAL 148
Cdd:cd19163 82 kvgrYGLDPDKMFdFSAERITKSVEESLKRLGLDYIDIIQVH-------------------DIEFAPsldqilneTLPAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 149 EGCKDAGLVKSIGVSNFNRRQLERLLSKPG------LKYkpvCnqveyHVYLNQSKLHE---YCKCHNIVLVAYSVLGT- 218
Cdd:cd19163 143 QKLKEEGKVRFIGITGYPLDVLKEVLERSPvkidtvLSY---C-----HYTLNDTSLLEllpFFKEKGVGVINASPLSMg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 219 ------ARDntWvDPNSPVLLEdpVLRSvAAKYNRSP----AEVAMRFILQ--KGAVVLAKSFNPTRLKQNLGVFEFELK 286
Cdd:cd19163 215 lltergPPD--W-HPASPEIKE--ACAK-AAAYCKSRgvdiSKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLD 288
|
..
gi 1785353101 287 PE 288
Cdd:cd19163 289 AH 290
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
20-282 |
1.54e-13 |
|
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: 69.89 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 20 MGLGTYASAeVPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEA--------IRSKIADGTVKReeifytgklwc 88
Cdd:cd19075 8 MTFGSQGRF-TTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELglgergfkIDTKANPGVGGG----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 89 sfFSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsDaHSNqPLDfddvdfcltwEALEGCKD---AGLVKSIGVSNF 165
Cdd:cd19075 76 --LSPENVRKQLETSLKRLKVDKVDVFYLHAP------D-RST-PLE----------ETLAAIDElykEGKFKEFGLSNY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 166 NRRQLERLLS--------KP----GLkYKPVCNQVEyhvylnqSKLHEYCKCHNIVLVAYSVL------GTARDNTWV-- 225
Cdd:cd19075 136 SAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLaggfltGKYKYSEDKag 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 226 ----DPNSPVL---------------LEdpVLRSVAAKYNRSPAEVAMRFIL-------QKG-AVVLAKSfNPTRLKQNL 278
Cdd:cd19075 208 ggrfDPNNALGklyrdrywkpsyfeaLE--KVEEAAEKEGISLAEAALRWLYhhsaldgEKGdGVILGAS-SLEQLEENL 284
|
....
gi 1785353101 279 GVFE 282
Cdd:cd19075 285 AALE 288
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
50-294 |
7.68e-13 |
|
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: 68.01 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 50 IDCAYIYGN---EVQIGEAIRSKiadgtvkREEIFYTGKLwcSFFS----PNLV-------RQGLEASLKALQLDYLDLF 115
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKY--TMNRrpgdPNAGgnhrknlRRSVEASLRRLQTDYIDLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 116 IMHWPFSVKPSDahsnqpldfddvdfcltwEALEGCKD---AGLVKSIGVSNF-----NRRQ-LERLLSKPGlkykPVCN 186
Cdd:cd19080 119 YVHAWDFTTPVE------------------EVMRALDDlvrAGKVLYVGISDTpawvvARANtLAELRGWSP----FVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 187 QVEYHVyLNQSKLHEY---CKCHNIVLVAYSVLG------------TARDNTWVDPNSPVLLEDP-------VLRSVAAK 244
Cdd:cd19080 177 QIEYSL-LERTPERELlpmARALGLGVTPWSPLGgglltgkyqrgeEGRAGEAKGVTVGFGKLTErnwaivdVVAAVAEE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1785353101 245 YNRSPAEVAMRFILQK--GAVVLAKSFNPTRLKQNLGVFEFELKPEDMEMLD 294
Cdd:cd19080 256 LGRSAAQVALAWVRQKpgVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
15-294 |
1.20e-12 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 67.26 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 15 NAIPV--MGLG----TYASAEVPKSDGTEATKLAIDLGYRHIDCAYIYG------NEVQIGEAIRS--KIAD-------G 73
Cdd:cd19077 1 NGKLVgpIGLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGppdphaNLKLLARFFRKypEYADkvvlsvkG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 74 TVKREEIFYTGklwcsffSPNLVRQGLEASLKAL-QLDYLDLFimhwpfsvkpsdahsnQP--LDfDDVDFCLTWEALEG 150
Cdd:cd19077 81 GLDPDTLRPDG-------SPEAVRKSIENILRALgGTKKIDIF----------------EParVD-PNVPIEETIKALKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 151 CKDAGLVKSIGVSNFNRRQLERllskpGLKYKPV-CNQVEYHVyLNQSKLH----EYCKCHNIVLVAYSVLG----TARD 221
Cdd:cd19077 137 LVKEGKIRGIGLSEVSAETIRR-----AHAVHPIaAVEVEYSL-FSREIEEngvlETCAELGIPIIAYSPLGrgllTGRI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 222 NTWVD-PNSPVLLEDP---------------VLRSVAAKYNRSPAEVAMRFILQKGA---VVLAKSFNPTRLKQNLGVFE 282
Cdd:cd19077 211 KSLADiPEGDFRRHLDrfngenfeknlklvdALQELAEKKGCTPAQLALAWILAQSGpkiIPIPGSTTLERVEENLKAAN 290
|
330
....*....|..
gi 1785353101 283 FELKPEDMEMLD 294
Cdd:cd19077 291 VELTDEELKEIN 302
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
18-279 |
1.39e-12 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 67.00 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 18 PVMGLGTYASAEVPKSDGTEATKL---AIDLGYRHIDCAYIYG---NEVQIGEAIRSKiadgtvKREEIFYTGKL----- 86
Cdd:cd19162 1 PRLGLGAASLGNLARAGEDEAAATldaAWDAGIRYFDTAPLYGlglSERRLGAALARH------PRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 87 -------------WCsfFSPNLVRQGLEASLKALQLDYLDLFIMHWPfsvkpsDAHSNQPLDfddvdfcLTWEALEGCKD 153
Cdd:cd19162 75 pgaagrpagadrrFD--FSADGIRRSIEASLERLGLDRLDLVFLHDP------DRHLLQALT-------DAFPALEELRA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 154 AGLVKSIGVSNFNRRQLERLLSKPGLKYKPVCNQveyHVYLNQSKLHE---YCKCHNIVLVAYSVLgtardntwvdpNSP 230
Cdd:cd19162 140 EGVVGAIGVGVTDWAALLRAARRADVDVVMVAGR---YTLLDRRAATEllpLCAAKGVAVVAAGVF-----------NSG 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785353101 231 VLLEDPV--------------------LRSVAAKYNRSPAEVAMRFILQKGAV--VLAKSFNPTRLKQNLG 279
Cdd:cd19162 206 ILATDDPagdrydyrpatpevlararrLAAVCRRYGVPLPAAALQFPLRHPAVasVVVGAASPAELRDNLA 276
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
20-293 |
1.07e-11 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 64.38 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 20 MGLGTYASAEVPKSDGTEATKLAIDLGYRHIDCAYIYG---NEVQIGEAIRSKIadgtvkREEIFYTGKLWCSFFS---- 92
Cdd:cd19145 20 MGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGpntNEVLLGKALKDGP------REKVQLATKFGIHEIGgsgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 93 -----PNLVRQGLEASLKALQLDYLDLFIMHwpfsvkpsDAHSNQPLDfddvdfcLTWEALEGCKDAGLVKSIGVSNFNR 167
Cdd:cd19145 94 evrgdPAYVRAACEASLKRLDVDYIDLYYQH--------RIDTTVPIE-------ITMGELKKLVEEGKIKYIGLSEASA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 168 RQLERLLSkpglkYKPVCN-QVEYHVYLN--QSKLHEYCKCHNIVLVAYSVLGtaRDNTWVDPNSPVLLEDPVLR----- 239
Cdd:cd19145 159 DTIRRAHA-----VHPITAvQLEWSLWTRdiEEEIIPTCRELGIGIVPYSPLG--RGFFAGKAKLEELLENSDVRkshpr 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785353101 240 -----------------SVAAKYNRSPAEVAMRFILQKGAVVL-----AKSFNptrLKQNLGVFEFELKPEDMEML 293
Cdd:cd19145 232 fqgenleknkvlyerveALAKKKGCTPAQLALAWVLHQGEDVVpipgtTKIKN---LNQNIGALSVKLTKEDLKEI 304
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
12-302 |
2.45e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 63.72 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 12 HDGNAIPVMGLGTYASAEV-PKSDGTEATKLAIDLGYRHIDCAYIYG----------NEVQIGEAIRSKiadgtVKREEI 80
Cdd:PRK10625 8 HSSLEVSTLGLGTMTFGEQnSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKR-----GSREKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 81 FYTGKLWC------SFFSPNL------VRQGLEASLKALQLDYLDLFIMHWPfsVKPSDAHSNQPLDFDD----VDFCLT 144
Cdd:PRK10625 83 IIASKVSGpsrnndKGIRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWP--QRPTNCFGKLGYSWTDsapaVSLLET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 145 WEALEGCKDAGLVKSIGVSN---FNRRQLERLLSKPGLKyKPVCNQVEYHVyLNQS---KLHEYCKCHNIVLVAYSVL-- 216
Cdd:PRK10625 161 LDALAEQQRAGKIRYIGVSNetaFGVMRYLHLAEKHDLP-RIVTIQNPYSL-LNRSfevGLAEVSQYEGVELLAYSCLaf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 217 GT-------------------ARDNTWVDPNSPVLLEDPVlrSVAAKYNRSPAEVAMRFILQK--------GAVVLAKsf 269
Cdd:PRK10625 239 GTltgkylngakpagarntlfSRFTRYSGEQTQKAVAAYV--DIAKRHGLDPAQMALAFVRRQpfvastllGATTMEQ-- 314
|
330 340 350
....*....|....*....|....*....|...
gi 1785353101 270 nptrLKQNLGVFEFELKPEDMEMLDGLNRNLRY 302
Cdd:PRK10625 315 ----LKTNIESLHLTLSEEVLAEIEAVHQVYTY 343
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
42-263 |
7.04e-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: 59.19 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 42 AIDLGYRHIDCAYIYGN-----EVQIGEAIRSkiaDGTVKREEIFYTGK----LW----CSFFSPNLVRQGLEASLKALQ 108
Cdd:cd19089 38 AFDLGITHFDLANNYGPppgsaEENFGRILKR---DLRPYRDELVISTKagygMWpgpyGDGGSRKYLLASLDQSLKRMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 109 LDYLDLFIMHWPfsvkpsDahSNQPLDfddvdfcLTWEALegckdAGLVKS-----IGVSNFNRRQLER---LLSKpgLK 180
Cdd:cd19089 115 LDYVDIFYHHRY------D--PDTPLE-------ETMTAL-----ADAVRSgkalyVGISNYPGAKARRaiaLLRE--LG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 181 YKPVCNQVEYHVyLNQS---KLHEYCKCHNIVLVAYSVL--GTARDNTWVDP------------------NSPVLLEDPV 237
Cdd:cd19089 173 VPLIIHQPRYSL-LDRWaedGLLEVLEEAGIGFIAFSPLaqGLLTDKYLNGIppdsrraaeskflteealTPEKLEQLRK 251
|
250 260
....*....|....*....|....*.
gi 1785353101 238 LRSVAAKYNRSPAEVAMRFILQKGAV 263
Cdd:cd19089 252 LNKIAAKRGQSLAQLALSWVLRDPRV 277
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
92-279 |
1.16e-09 |
|
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: 58.11 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 92 SPNLVRQGLEASLKALQLDYLDLFIMHwpfsvkpsdahsnqpLDFDDVDFCLTWEALEGCKDAGLVKSIGVSNFNRRQLE 171
Cdd:cd19752 93 SAETIEQEIDKSLRRLGTDYIDLYYAH---------------VDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 172 RL--LSKPGLKYKPVCNQvEYHVYL---------NQS----KLHEYCKCH-NIVLVAYSVL--------GTARDNTWVDP 227
Cdd:cd19752 158 RArqIARQQGWAEFSAIQ-QRHSYLrprpgadfgVQRivtdELLDYASSRpDLTLLAYSPLlsgaytrpDRPLPEQYDGP 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1785353101 228 NSPVLLEdpVLRSVAAKYNRSPAEVAMRFILQK--GAVVLAKSFNPTRLKQNLG 279
Cdd:cd19752 237 DSDARLA--VLEEVAGELGATPNQVVLAWLLHRtpAIIPLLGASTVEQLEENLA 288
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
42-298 |
1.37e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 58.06 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 42 AIDLGYRHIDCAYIYGNEVQ---IGEA---------IRSKI-----ADGTvkreeifytgklWCSFFSPNLVRQGLEASL 104
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPHVTnqlIREAlhpypddltIVTKVgarrgEDGS------------WLPAFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 105 KALQLDYLDLFIMHWPFSV-KPSDAHSNQPLdfddvdfcltwEALEGCKDAGLVKSIGVSNFNRRQLERllskpGLKYKP 183
Cdd:PRK10376 117 RNLGLDVLDVVNLRLMGDGhGPAEGSIEEPL-----------TVLAELQRQGLVRHIGLSNVTPTQVAE-----ARKIAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 184 -VCNQVEYH-VYLNQSKLHEYCKCHNIVLVAYSVLGTArdntwvdpnSPvlLEDPVLRSVAAKYNRSPAEVAMRFILQKG 261
Cdd:PRK10376 181 iVCVQNHYNlAHRADDALIDALARDGIAYVPFFPLGGF---------TP--LQSSTLSDVAASLGATPMQVALAWLLQRS 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 1785353101 262 AVVL--AKSFNPTRLKQNLGVFEFELKPEDMEMLDGLNR 298
Cdd:PRK10376 250 PNILliPGTSSVAHLRENLAAAELVLSEEVLAELDGIAR 288
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
19-175 |
1.08e-08 |
|
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: 55.36 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 19 VMGLGTYA---SAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN-EVQIGEAIrSKIADGtVKREEIFYTGKL----WCSF 90
Cdd:cd19164 17 IFGAATFSyqyTTDPESIPPVDIVRRALELGIRAFDTSPYYGPsEIILGRAL-KALRDE-FPRDTYFIITKVgrygPDDF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 91 -FSPNLVRQGLEASLKALQLDYLDLFIMHwpfsvkpsdahsnqpldfdDVDFCLTWEALEGC------KDAGLVKSIGVS 163
Cdd:cd19164 95 dYSPEWIRASVERSLRRLHTDYLDLVYLH-------------------DVEFVADEEVLEALkelfklKDEGKIRNVGIS 155
|
170
....*....|..
gi 1785353101 164 NFnrrQLERLLS 175
Cdd:cd19164 156 GY---PLPVLLR 164
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
36-120 |
1.35e-06 |
|
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: 49.13 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 36 TEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRskiaDGTVKREEIFYTGKLwcsFF-----SPN---LVR----QGL 100
Cdd:cd19143 34 KECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKI---FWggggpPPNdrgLSRkhivEGT 106
|
90 100
....*....|....*....|
gi 1785353101 101 EASLKALQLDYLDLFIMHWP 120
Cdd:cd19143 107 KASLKRLQLDYVDLVFCHRP 126
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
14-282 |
2.79e-06 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 47.92 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVmGLGTYASAEV----PKSDGTEAT-KLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgTVKREEIFYTGK 85
Cdd:cd19153 10 GNVSPV-GLGTAALGGVygdgLEQDEAVAIvAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 86 LwCSF------FSPNLVRQGLEASLKALQLDYLDLFIMHwpfsvkpsdahsnqPLDFDDVDFCL--TWEALEGCKDAGLV 157
Cdd:cd19153 85 V-GRYrdsefdYSAERVRASVATSLERLHTTYLDVVYLH--------------DIEFVDYDTLVdeALPALRTLKDEGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 158 KSIGVSNFNRRQLERLL--SKPGlkyKPVCNQVEYHVYLNQSKLHEYCKCHN----IVLVAYSVLG----TARDNTWVDP 227
Cdd:cd19153 150 KRIGIAGYPLDTLTRATrrCSPG---SLDAVLSYCHLTLQDARLESDAPGLVrgagPHVINASPLSmgllTSQGPPPWHP 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 228 NSPVLLE-DPVLRSVAAKYNRSPAEVAMRFIL----QKGAVVLAKSfNPTRLKQNLGVFE 282
Cdd:cd19153 227 ASGELRHyAAAADAVCASVEASLPDLALQYSLaahaGVGTVLLGPS-SLAQLRSMLAAVD 285
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
30-163 |
4.27e-06 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 47.47 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 30 VPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgTVKREEIFYTGKlwCS-----F-FSPNLVRQGL 100
Cdd:PLN02587 28 VSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVSTK--CGrygegFdFSAERVTKSV 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785353101 101 EASLKALQLDYLDLFIMHwpfsvkpsdahsnqPLDFDDVDFCL--TWEALEGCKDAGLVKSIGVS 163
Cdd:PLN02587 102 DESLARLQLDYVDILHCH--------------DIEFGSLDQIVneTIPALQKLKESGKVRFIGIT 152
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
14-193 |
5.53e-05 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 44.31 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 14 GNAIPVMGLGTYAS--AEVPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRSK--IADGTVKREEIFYTGKL 86
Cdd:cd19158 10 GLRVSCLGLGTWVTfgGQITDEMAEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKgwRRSSLVITTKIFWGGKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 87 WCSF-FSPNLVRQGLEASLKALQLDYLDLFimhwpFSVKPSdahSNQPLDfddvdfcLTWEALEGCKDAGLVKSIGVSNF 165
Cdd:cd19158 90 ETERgLSRKHIIEGLKASLERLQLEYVDVV-----FANRPD---PNTPME-------ETVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190
....*....|....*....|....*....|
gi 1785353101 166 NRRQLERLLS--KPGLKYKPVCNQVEYHVY 193
Cdd:cd19158 155 SSMEIMEAYSvaRQFNLIPPICEQAEYHMF 184
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
17-118 |
3.08e-03 |
|
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: 38.98 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785353101 17 IPVMGLGTYA--SAEVPKSDGTEATKLAIDLGYRHIDCAYIYGN---EVQIGEAIRSKiadgTVKREEIFYTGKLWCSF- 90
Cdd:cd19142 13 VSNVGLGTWStfSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIYWSYg 88
|
90 100 110
....*....|....*....|....*....|...
gi 1785353101 91 -----FSPNLVRQGLEASLKALQLDYLDLFIMH 118
Cdd:cd19142 89 seergLSRKHIIESVRASLRRLQLDYIDIVIIH 121
|
|
| |
