|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-259 |
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: 558.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 6 QTVLLNDGHFIPILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKV 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 86 WQTFHRPELVQ---------------------------PGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGV 138
Cdd:cd19108 81 WCTFHRPELVRpalekslkklqldyvdlylihfpvalkPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 139 CNFNRRQLEKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR--------------------VDKSFPVLLDDPVLGSMA 198
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKskdivlvaysalgsqrdkewVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720374595 199 KKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYI 259
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-272 |
3.05e-138 |
|
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: 391.85 E-value: 3.05e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 13 GHFIPILGFGT-SAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHR 91
Cdd:cd19109 1 GNSIPIIGLGTySEPKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 92 PELV---------------------------QPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRR 144
Cdd:cd19109 81 PELVrptlertlkvlqldyvdlyiiempmafKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 145 QLEKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR--------------------VDKSFPVLLDDPVLGSMAKKYNRT 204
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQqhdivivaysplgtcrdpiwVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720374595 205 PALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYIGSSISEDHPDFPF 272
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-276 |
7.59e-109 |
|
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: 317.05 E-value: 7.59e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRPELV 95
Cdd:cd19107 4 MPILGLGT---WKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 96 ---------------------------QPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEK 148
Cdd:cd19107 81 kgacqktlsdlkldyldlylihwptgfKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 149 ILSKPGLKYKPVCNQVECHPYLNQRKLLDFCRV--------------DKSF-----PVLLDDPVLGSMAKKYNRTPALIA 209
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSkgivvtaysplgspDRPWakpedPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720374595 210 LRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYIGSSISEDHPDFPFLDEY 276
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-266 |
3.43e-107 |
|
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: 312.78 E-value: 3.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGT-VKREDIFCTSKVW 86
Cdd:cd19106 1 LHTGQKMPLIGLGTwkSKPGQV-----KAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 QTFHRPELVQP---------------------------GENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVC 139
Cdd:cd19106 76 NTKHHPEDVEPalrktlkdlqldyldlylihwpyaferGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 140 NFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-------------------VDKSFPVLLDDPVLGSMAKK 200
Cdd:cd19106 156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKarglvvtaysplgspdrpwAKPDEPVLLEEPKVKALAKK 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720374595 201 YNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYIGSSISED 266
Cdd:cd19106 234 YNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVPMITVD 299
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-276 |
9.97e-101 |
|
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: 296.48 E-value: 9.97e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRPE 93
Cdd:cd19110 4 IPAVGLGTwkASPGEV-----TEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 94 LVQ---------------------------PGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQL 146
Cdd:cd19110 79 LVKtactrslkalklnyldlylihwpmgfkPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 147 EKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV--------LLDDPVLGSMAKKYNRTPALIALRYQ 213
Cdd:cd19110 159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQsrnvsVTAYRPLggscegvdLIDDPVIQRIAKKHGKSPAQILIRFQ 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720374595 214 VQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYIGSSISEDHPDFPFLDEY 276
Cdd:cd19110 239 IQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-259 |
2.09e-97 |
|
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: 287.64 E-value: 2.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 7 TVLLNDGHFIPILGFGTSapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVW 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTW--KLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 QTFHRPELVQP---------GENY-------FP--------KDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFN 142
Cdd:cd19116 80 NSYHEREQVEPalreslkrlGLDYvdlylihWPvafkenndSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 143 RRQLEKILSkpGLKYKPVCNQVECHPYLNQRKLLDFC--------------RVDKSF----PVLLDDPVLGSMAKKYNRT 204
Cdd:cd19116 160 SEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCqsngivvmayspfgRLVPRGqtnpPPRLDDPTLVAIAKKYGKT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1720374595 205 PALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYI 259
Cdd:cd19116 238 TAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-250 |
1.57e-94 |
|
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: 278.60 E-value: 1.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVdgtvKREDIFCTSKVWQTFHRPELV 95
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGV----PREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 96 QP---------GENY-------FPKDenGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPglKYKP 159
Cdd:cd19071 74 REaleeslkdlGLDYldlylihWPVP--GKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAA--RIKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 160 VCNQVECHPYLNQRKLLDFCR-----------VDKSFPVLLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEK 228
Cdd:cd19071 150 AVNQIELHPYLQQKELVEFCKehgivvqayspLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPE 229
|
250 260
....*....|....*....|..
gi 1720374595 229 RIKENMQVFEFQLTSVDMKVLD 250
Cdd:cd19071 230 RIKENLDVFDFELSEEDMAAID 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-258 |
2.19e-87 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 260.76 E-value: 2.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 12 DGHFIPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVWQTFHR 91
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 92 PELVQP---------GENYF-------PKDengkfiydaVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPGl 155
Cdd:COG0656 74 YDDTLAafeeslerlGLDYLdlylihwPGP---------GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 156 kYKPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSF 225
Cdd:COG0656 144 -VKPAVNQVELHPYLQQRELLAFCR-EHGIVVeaysplgrgkLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSV 221
|
250 260 270
....*....|....*....|....*....|...
gi 1720374595 226 IEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:COG0656 222 TPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
7-259 |
1.43e-85 |
|
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: 257.72 E-value: 1.43e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 7 TVLLNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSK 84
Cdd:cd19123 3 TLPLSNGDLIPALGLGTwkSKPGEV-----GQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 85 VWQTFHRPELVQP---------GENY-----------------FPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGV 138
Cdd:cd19123 78 LWNNSHAPEDVLPalektladlQLDYldlylmhwpvalkkgvgFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 139 CNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR---------------------VDKSFPVLLDDPVLGSM 197
Cdd:cd19123 158 SNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRdngihltaysplgsgdrpaamKAEGEPVLLEDPVINKI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720374595 198 AKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYI 259
Cdd:cd19123 236 AEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
10-257 |
1.26e-81 |
|
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: 247.71 E-value: 1.26e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQ 87
Cdd:cd19154 6 LSNGVKMPLIGLGTwqSKGAEG-----ITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 88 TFHRPELVQPG---------------------------ENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCN 140
Cdd:cd19154 81 HEHAPEDVEEAlreslkklqleyvdlylihapaafkddEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 141 FNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-------------------VDKSF-----PVLLDDPVLGS 196
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKkhnisvtsyatlgspgranFTKSTgvspaPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720374595 197 MAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIR 257
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
10-252 |
9.29e-77 |
|
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: 234.93 E-value: 9.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGT--SAPqevprSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQ 87
Cdd:cd19125 5 LNTGAKIPAVGLGTwqADP-----GVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 88 TFHRPELVQPGEN-------------YF-----------PKDENGKFIydAVDICDTWEAMEKCKDAGLAKSIGVCNFNR 143
Cdd:cd19125 80 TDHAPEDVPPALEktlkdlqldyldlYLihwpvrlkkgaHMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVSNFSV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 144 RQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV-----------LLDDPVLGSMAKKYNRTPAL 207
Cdd:cd19125 158 KKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKskgihLSAYSPLgspgttwvkknVLKDPIVTKVAEKLGKTPAQ 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720374595 208 IALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 252
Cdd:cd19125 236 VALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-257 |
3.37e-73 |
|
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: 226.64 E-value: 3.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 5 QQTVLLNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCT 82
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTwqSSPEEI-----ETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 83 SKVWQTFHRPELVQP----------------------------GENYFPKDENGKFIYD-AVDICDTWEAMEKCKDAGLA 133
Cdd:cd19155 76 TKLPPGGNRREKVEKfllksleklqldyvdlylihfpvgslskEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 134 KSIGVCNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR--------------------------VDKSFPV 187
Cdd:cd19155 156 RSIGLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSthsitvtayaplgspgaahfspgtgsPSGSSPD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 188 LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIR 257
Cdd:cd19155 234 LLQDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-258 |
4.02e-70 |
|
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: 217.75 E-value: 4.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 13 GHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFH 90
Cdd:cd19111 1 GFPMPVIGLGTyqSPPEEV-----RAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 91 RPELVQPG-----EN-----------YFP-----KDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKI 149
Cdd:cd19111 76 EFKDTEKSlekslENlklpyvdlyliHHPcgfvnKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 150 LSKPglKYKPVCNQVECHPYLNQRKLLDFC-----------------RVDKSF----PVLLDDPVLGSMAKKYNRTPALI 208
Cdd:cd19111 156 LAYA--KVKPSNLQLECHAYLQQRELRKFCnkknivvtayaplgspgRANQSLwpdqPDLLEDPTVLAIAKELDKTPAQV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720374595 209 ALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:cd19111 234 LLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-258 |
1.88e-68 |
|
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: 213.02 E-value: 1.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 7 TVLLNDGHFIPILGFGTSAPQEvpRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDgtvkREDIFCTSKVW 86
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEE--GSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIP----REELFITSKVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 QTFHRPE---------LVQPGENY-------FPKDENGKfiydavdicDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKIL 150
Cdd:cd19157 75 NADQGYDstlkafeasLERLGLDYldlylihWPVKGKYK---------ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 151 SKPglKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV----LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVL 221
Cdd:cd19157 146 ADA--EIVPMVNQVEFHPRLTQKELRDYCKkqgiqLEAWSPLmqgqLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTI 223
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720374595 222 AKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:cd19157 224 PKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-253 |
2.02e-68 |
|
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: 212.62 E-value: 2.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 7 TVLLNDGHFIPILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVW 86
Cdd:cd19131 1 TITLNDGNTIPQLGLGV---WQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 QTFHRPE---------LVQPGENY-------FPKDENGKFIydavdicDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKIL 150
Cdd:cd19131 74 NSDQGYDstlrafdesLRKLGLDYvdlylihWPVPAQDKYV-------ETWKALIELKKEGRVKSIGVSNFTIEHLQRLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 151 SKPGLKykPVCNQVECHPYLNQRKLLDFC-----RVDKSFPV----LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVL 221
Cdd:cd19131 147 DETGVV--PVVNQIELHPRFQQRELRAFHakhgiQTESWSPLgqggLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVI 224
|
250 260 270
....*....|....*....|....*....|..
gi 1720374595 222 AKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 253
Cdd:cd19131 225 PKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-250 |
5.26e-68 |
|
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: 210.98 E-value: 5.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVWQTFHRPELV 95
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIA----ESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 96 QP---------GENYF-------PKDEngkfiydaVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPGLkyKP 159
Cdd:cd19073 74 KKsvdrsleklGTDYVdlllihwPNPT--------VPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL--PI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 160 VCNQVECHPYLNQRKLLDFCR-----VDKSFPV----LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRI 230
Cdd:cd19073 144 AVNQVEFHPFLYQAELLEYCRendivITAYSPLargeVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHL 223
|
250 260
....*....|....*....|
gi 1720374595 231 KENMQVFEFQLTSVDMKVLD 250
Cdd:cd19073 224 KENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-238 |
7.99e-68 |
|
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: 211.89 E-value: 7.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIR-SKIVDGTVKREDIFCTSKVW 86
Cdd:cd19118 1 LNTGNKIPAIGLGTwqAEPGEV-----GAAVKIALKAGYRHLDLAKVYQNQHEVGQALKeLLKEEPGVKREDLFITSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 QTFHRPELVQPG------------------------------ENYFPKDENGKFIY--DAVDICDTWEAMEKCKDAGLAK 134
Cdd:cd19118 76 NNSHRPEYVEPAlddtlkelgldyldlylihwpvafkptgdlNPLTAVPTNGGEVDldLSVSLVDTWKAMVELKKTGKVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 135 SIGVCNFNRRQLEKILSKPGLkyKPVCNQVECHPYLNQRKLLDFCRVDK--------------SFPVLLDDPVLGSMAKK 200
Cdd:cd19118 156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNihitaysplgnnlaGLPLLVQHPEVKAIAAK 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720374595 201 YNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFE 238
Cdd:cd19118 234 LGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE 271
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-236 |
8.56e-68 |
|
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: 212.32 E-value: 8.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 11 NDGHFIPILGFGTSAPQEvprSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFH 90
Cdd:cd19129 1 NGSGAIPALGFGTLIPDP---SATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 91 RPELV---------------------------QPGENYFPKDENGKFIYD-AVDICDTWEAMEKCKDAGLAKSIGVCNFN 142
Cdd:cd19129 78 RPERVkpafeaslkrlqldyldlylihtpfafQPGDEQDPRDANGNVIYDdGVTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 143 RRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR----VDKSF--------PVLLDDPVLGSMAKKYNRTPALIAL 210
Cdd:cd19129 158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKnhgiVLQAFaplghgmePKLLEDPVITAIARRVNKTPAQVLL 235
|
250 260
....*....|....*....|....*.
gi 1720374595 211 RYQVQRGVVVLAKSFIEKRIKENMQV 236
Cdd:cd19129 236 AWAIQRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-253 |
2.62e-66 |
|
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: 206.90 E-value: 2.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 8 VLLNDGHFIPILGFGTSapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSkivdGTVKREDIFCTSKVWQ 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVF--QTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 88 TFHRPElvqPGENYFPKDENgKFIYDAVD-----------ICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPglK 156
Cdd:cd19126 75 DDQRAR---RTEDAFQESLD-RLGLDYVDlylihwpgkdkFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHA--D 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 157 YKPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFI 226
Cdd:cd19126 149 VVPAVNQVEFHPYLTQKELRGYCK-SKGIVVeawsplgqggLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVH 227
|
250 260
....*....|....*....|....*..
gi 1720374595 227 EKRIKENMQVFEFQLTSVDMKVLDGLN 253
Cdd:cd19126 228 ASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-254 |
3.40e-66 |
|
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: 207.74 E-value: 3.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 5 QQTVLLNDGHFIPILGFGT--SAPQEVprSKATEAtkiAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCT 82
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTwqSKPNEV--AKAVEA---ALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 83 SKVWQTFHR-------------------------PELVQPG--ENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKS 135
Cdd:cd19117 74 TKLWCTWHRrveealdqslkklgldyvdlylmhwPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 136 IGVCNFNRRQLEKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV------LLDDPVLGSMAKKYNRT 204
Cdd:cd19117 154 IGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKskgihATAYSPLgstnapLLKEPVIIKIAKKHGKT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720374595 205 PALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEfqLTSVDMKVLDGLNK 254
Cdd:cd19117 234 PAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHK 281
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
6-258 |
2.79e-64 |
|
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: 203.81 E-value: 2.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 6 QTVLLNDGHFIPILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKV 85
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGL---WKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 86 WQTFHRPELVQP---------GENY-------FP----------------KDENGKFIYDAVDICDTWEAMEKCKDAGLA 133
Cdd:cd19115 80 WNTFHDGERVEPicrkqladwGIDYfdlflihFPialkyvdpavryppgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 134 KSIGVCNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCRVDK------------SF-----------PVLLD 190
Cdd:cd19115 160 RSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGiavtayssfgpqSFleldlpgakdtPPLFE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720374595 191 DPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:cd19115 238 HDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-252 |
2.50e-63 |
|
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: 200.19 E-value: 2.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 12 DGHFIPILGFGTSAPQEVPrSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVK-REDIFCTSKVWQTFH 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSP-EDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 91 RPELV---------------------------QPGENYFPKDENgkfIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNR 143
Cdd:cd19124 80 HPDLVlpalkkslrnlqleyvdlylihwpvslKPGKFSFPIEEE---DFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 144 RQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR----VDKSFPVL------------LDDPVLGSMAKKYNRTPAL 207
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKangiHVTAYSPLgapgtkwgsnavMESDVLKEIAAAKGKTVAQ 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720374595 208 IALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 252
Cdd:cd19124 235 VSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-253 |
1.94e-62 |
|
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: 197.03 E-value: 1.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 8 VLLNDGHFIPILGFGTSapqEVPRSKATE-ATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVW 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 ----------QTFHRP---------ELV---QPGENYFpkdengkfiydavdicDTWEAMEKCKDAGLAKSIGVCNFNRR 144
Cdd:cd19133 74 iqdagyekakKAFERSlkrlgldylDLYlihQPFGDVY----------------GAWRAMEELYKEGKIRAIGVSNFYPD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 145 QLEKILskPGLKYKPVCNQVECHPYLNQRKLLDFcrvDKSFPV--------------LLDDPVLGSMAKKYNRTPALIAL 210
Cdd:cd19133 138 RLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEF---LKKYGVqieawgpfaegrnnLFENPVLTEIAEKYGKSVAQVIL 212
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720374595 211 RYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 253
Cdd:cd19133 213 RWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
7-258 |
5.98e-62 |
|
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: 197.71 E-value: 5.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 7 TVLLNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSK 84
Cdd:cd19112 2 TITLNSGHKMPVIGLGVwrMEPGEI-----KELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 85 VWQTFH-------RPELVQPGENY-------FP--------------KDENGKFIYDA-VDICDTWEAMEKCKDAGLAKS 135
Cdd:cd19112 77 LWNSDHghvieacKDSLKKLQLDYldlylvhFPvatkhtgvgttgsaLGEDGVLDIDVtISLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 136 IGVCNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV--------------LLDDPVLGS 196
Cdd:cd19112 157 IGISNYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQkhgisVTAHTPLggaaanaewfgsvsPLDDPVLKD 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720374595 197 MAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:cd19112 235 LAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-252 |
8.44e-62 |
|
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: 195.56 E-value: 8.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 13 GHFIPILGFGTSapQEVPRsKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVWQTFHRP 92
Cdd:cd19140 5 GVRIPALGLGTY--PLTGE-ECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIA----ASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 93 ELVQP---------GENY-------FPKDEngkfiydaVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKI--LSKPG 154
Cdd:cd19140 78 DDFLAsveeslrklRTDYvdllllhWPNKD--------VPLAETLGALNEAQEAGLARHIGVSNFTVALLREAveLSEAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 155 LkykpVCNQVECHPYLNQRKLLDFCR-----VDKSFPV----LLDDPVLGSMAKKYNRTPALIALRYQVQR-GVVVLAKS 224
Cdd:cd19140 150 L----FTNQVEYHPYLDQRKLLDAARehgiaLTAYSPLargeVLKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAIPKA 225
|
250 260
....*....|....*....|....*...
gi 1720374595 225 FIEKRIKENMQVFEFQLTSVDMKVLDGL 252
Cdd:cd19140 226 TNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
10-252 |
4.02e-61 |
|
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: 194.67 E-value: 4.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIvDGTVKREDIFCTSKVWQ 87
Cdd:cd19121 6 LNTGASIPAVGLGTwqAKAGEV-----KAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 88 TFHR-------------------------PELVQPGENY--FPKDENGK--FIYDAvDICDTWEAMEKCKDAGLAKSIGV 138
Cdd:cd19121 80 TYHRrvelcldrslkslgldyvdlylvhwPVLLNPNGNHdlFPTLPDGSrdLDWDW-NHVDTWKQMEKVLKTGKTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 139 CNFNRRQLEKILskPGLKYKPVCNQVECHPYLNQRKLLDFCRV------------DKSFPVLLDDPVLgSMAKKYNRTPA 206
Cdd:cd19121 159 SNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEkgilieaysplgSTGSPLISDEPVV-EIAKKHNVGPG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720374595 207 LIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFqlTSVDMKVLDGL 252
Cdd:cd19121 236 TVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-258 |
7.81e-61 |
|
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: 193.50 E-value: 7.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 8 VLLNDGHFIPILGFGTSAPQEvpRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKivdgTVKREDIFCTSKVW- 86
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQD--GAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWn 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 ---------QTFHRpELVQPGENY-------FPKdeNGKFIydavdicDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKIL 150
Cdd:cd19156 75 sdqgyestlAAFEE-SLEKLGLDYvdlylihWPV--KGKFK-------DTWKAFEKLYKEKKVRAIGVSNFHEHHLEELL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 151 SKpgLKYKPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVV 220
Cdd:cd19156 145 KS--CKVAPMVNQIELHPLLTQEPLRKFCK-EKNIAVeawsplgqgkLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIIT 221
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720374595 221 LAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:cd19156 222 IPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-258 |
2.12e-60 |
|
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: 192.45 E-value: 2.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 13 GHFIPILGFGT-----SAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVW- 86
Cdd:cd19120 1 GSKIPAIAFGTgtawyKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 ------QTFHRpELVQPGENYF-------PKDENGKfiydAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKP 153
Cdd:cd19120 77 gikdprEALRK-SLAKLGVDYVdlylihsPFFAKEG----GPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 154 glKYKPVCNQVECHPYLN--QRKLLDFCR----VDKSF----PVLLD-----DPVLGSMAKKYNRTPALIALRYQVQRGV 218
Cdd:cd19120 152 --KIKPAVNQIEFHPYLYpqQPALLEYCRehgiVVSAYsplsPLTRDaggplDPVLEKIAEKYGVTPAQVLLRWALQKGI 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720374595 219 VVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:cd19120 230 VVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-253 |
2.39e-60 |
|
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: 191.71 E-value: 2.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGTSApqeVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSkivdGTVKREDIFCTSKVWQTF 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYP---LKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 90 HRPELVQP---------GENYF-------PKDENGKFIydavdicDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKP 153
Cdd:cd19132 74 HGYEEALRtieeslyrlGLDYVdlylihwPNPSRDLYV-------EAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDET 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 154 GLKykPVCNQVECHPYLNQRKLLDFCR----VDKSF-PV-----LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAK 223
Cdd:cd19132 147 GVT--PAVNQIELHPYFPQAEQRAYHRehgiVTQSWsPLgrgsgLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPK 224
|
250 260 270
....*....|....*....|....*....|
gi 1720374595 224 SFIEKRIKENMQVFEFQLTSVDMKVLDGLN 253
Cdd:cd19132 225 SANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-252 |
2.55e-60 |
|
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: 192.08 E-value: 2.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGT---SAPQEVprSKATEAtkiAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRP 92
Cdd:cd19136 1 MPILGLGTfrlRGEEEV--RQAVDA---ALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 93 ELVQ----------------------PGENYFPKDENGKFIYDAvdicDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKIL 150
Cdd:cd19136 76 EKARaaclgslerlgtdyldlylihwPGVQGLKPSDPRNAELRR----ESWRALEDLYKEGKLRAIGVSNYTVRHLEELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 151 SKPglKYKPVCNQVECHPYLNQRKLLDFCRVDKSF-----------PVLLDDPVLGSMAKKYNRTPALIALRYQVQRGVV 219
Cdd:cd19136 152 KYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHlqaysslgsgdLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIG 229
|
250 260 270
....*....|....*....|....*....|...
gi 1720374595 220 VLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 252
Cdd:cd19136 230 VIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-252 |
2.67e-60 |
|
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: 192.35 E-value: 2.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 17 PILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRPELVQ 96
Cdd:cd19128 2 PRLGFGT---YKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 97 ---------------------------PGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKI 149
Cdd:cd19128 79 eqllitlqdlqleyldlflihwplafdMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 150 LSKpgLKYKPVCNQVECHPYLNQRKLLDFC---------------RVDKSFPVLLDDPVLGSMAKKYNRTPALIALRYQV 214
Cdd:cd19128 159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCiennihvtayrplggSYGDGNLTFLNDSELKALATKYNTTPPQVIIAWHL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720374595 215 QR---GVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 252
Cdd:cd19128 237 QKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-258 |
9.21e-60 |
|
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: 192.28 E-value: 9.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 6 QTVLLNDGHFIPILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKV 85
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGC---WKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 86 WQTFHRPELVQ-----------------------------PGENYFPK-----DENgKFIYDAVDICDTWEAMEKCKDAG 131
Cdd:cd19113 78 WNNFHDPKNVEtalnktlsdlkldyvdlflihfpiafkfvPIEEKYPPgfycgDGD-NFVYEDVPILDTWKALEKLVDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 132 LAKSIGVCNFNRRQLEKILSkpGLKYKPVCNQVECHPYLNQRKLLDFCRVD------------KSF-----------PVL 188
Cdd:cd19113 157 KIKSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAgititayssfgpQSFvelnqgralntPTL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 189 LDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:cd19113 235 FEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
10-259 |
3.86e-57 |
|
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: 185.01 E-value: 3.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGTSAPQEvPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTF 89
Cdd:cd19119 6 LNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 90 HRP-----------------ELV-------------QPGENYFPKDENGKFIYDA-VDICDTWEAMEKCKDAGLAKSIGV 138
Cdd:cd19119 85 YDEversldeslkalgldyvDLLlvhwpvcfekdsdDSGKPFTPVNDDGKTRYAAsGDHITTYKQLEKIYLDGRAKAIGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 139 CNFNRRQLEKILSKpgLKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV------LLDDPVLGSMAKKYNRTPAL 207
Cdd:cd19119 165 SNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFkhgilVTAYSPLgshgapNLKNPLVKKIAEKYNVSTGD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1720374595 208 IALRYQVQRGVVVLAKSFIEKRIKENMQVfeFQLTSVDMKVLD--GLNKNIRYI 259
Cdd:cd19119 243 ILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDdiGEKYPVRFI 294
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
7-258 |
7.87e-56 |
|
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: 180.44 E-value: 7.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 7 TVLLNDGHFIPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKivdgTVKREDIFCTSKVW 86
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVG---ELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 QTFH---------RPELVQPGENY-------FPKDENGKFIydavdicDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKIL 150
Cdd:cd19134 75 TPDQgftasqaacRASLERLGLDYvdlylihWPAGREGKYV-------DSWGGLMKLREEGLARSIGVSNFTAEHLENLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 151 SKPGlkYKPVCNQVECHPYLNQRKLLDFCR----VDKSF-PV----LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVL 221
Cdd:cd19134 148 DLTF--FTPAVNQIELHPLLNQAELRKVNAqhgiVTQAYsPLgvgrLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVI 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720374595 222 AKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:cd19134 226 SRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
7-252 |
3.37e-53 |
|
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: 173.66 E-value: 3.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 7 TVLLNDGHFIPILGFGTSapqevpRS--KATEATKIAI-DAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTS 83
Cdd:cd19135 4 TVRLSNGVEMPILGLGTS------HSggYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIK----ESGVPREDLFLTT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 84 KVWQT---------------------------FHRPELVQPGENyfPKDEngkfiydavdICDTWEAMEKCKDAGLAKSI 136
Cdd:cd19135 74 KLWPSdygyestkqafeaslkrlgvdyldlylLHWPDCPSSGKN--VKET----------RAETWRALEELYDEGLCRAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 137 GVCNFNRRQLEKILSKPGLKykPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPA 206
Cdd:cd19135 142 GVSNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCR-DNNIVFegycplakgkALEEPTVTELAKKYQKTPA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720374595 207 LIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 252
Cdd:cd19135 219 QILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-258 |
6.40e-53 |
|
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: 174.28 E-value: 6.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 13 GHFIPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRP 92
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 93 E------------------------------LVQPGENYFP---KDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVC 139
Cdd:cd19114 78 DhvreafdrqlkdygldyidlylihfpipaaYVDPAENYPFlwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 140 NFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLD----------------------FCRVDKSFPVLLDDPVLGSM 197
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDwakkqgiqitayssfgnavytkVTKHLKHFTNLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720374595 198 AKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 258
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-253 |
2.47e-50 |
|
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: 166.24 E-value: 2.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKivdgTVKREDIFCTSKVWQTF 89
Cdd:cd19130 4 LNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAAS----GIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 90 HRPELVQPGENyfpkDENGKFIYDAVDI-------------CDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPGLK 156
Cdd:cd19130 77 HDGDEPAAAFA----ESLAKLGLDQVDLylvhwptpaagnyVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 157 ykPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV----LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIE 227
Cdd:cd19130 153 --PAVNQIELHPAYQQRTIRDWAQahdvkIEAWSPLgqgkLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRR 230
|
250 260
....*....|....*....|....*.
gi 1720374595 228 KRIKENMQVFEFQLTSVDMKVLDGLN 253
Cdd:cd19130 231 ERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-253 |
3.88e-50 |
|
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: 166.04 E-value: 3.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGTSApqeVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDgtvkREDIFCTSKVWQT- 88
Cdd:cd19127 3 LNNGVEMPALGLGVFQ---TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVD----RSDIFVTTKLWISd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 89 ---------FHRpELVQPGENY-------FPKdengKFIYDavDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSK 152
Cdd:cd19127 76 ygydkalrgFDA-SLRRLGLDYvdlyllhWPV----PNDFD--RTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 153 PGLKykPVCNQVECHPYLNQRKLLDF-----------------CRVDKSFPV----LLDDPVLGSMAKKYNRTPALIALR 211
Cdd:cd19127 149 TTVV--PAVNQVELHPYFSQKDLRAFhrrlgivtqawspiggvMRYGASGPTgpgdVLQDPTITGLAEKYGKTPAQIVLR 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720374595 212 YQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 253
Cdd:cd19127 227 WHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-252 |
1.13e-48 |
|
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: 161.75 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGTS--APQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVW-QTFHRP 92
Cdd:cd19139 1 IPAFGLGTFrlKDDVV-----IDSVRTALELGYRHIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWiDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 93 ELVQPGENYFPKDENGKF---------IYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPGlKYKPVCNQ 163
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVdltlihwpsPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVG-AGAIATNQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 164 VECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKEN 233
Cdd:cd19139 151 IELSPYLQNRKLVAHCK-QHGIHVtsymtlaygkVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSN 229
|
250
....*....|....*....
gi 1720374595 234 MQVFEFQLTSVDMKVLDGL 252
Cdd:cd19139 230 LLALDLTLDADDMAAIAAL 248
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
5-241 |
5.51e-46 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 155.62 E-value: 5.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 5 QQTVL-LNDGHFIPILGFGT-SAPQEVPRSKATEAtkiaIDAGFRHIDCAAVYQNEKEVGLAIRSkivdGTVKREDIFCT 82
Cdd:PRK11565 3 NPTVIkLQDGNVMPQLGLGVwQASNEEVITAIHKA----LEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 83 SKVWQTFHRpelvQPGENYfpKDENGKFIYDAVDI-------------CDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKI 149
Cdd:PRK11565 75 TKLWNDDHK----RPREAL--EESLKKLQLDYVDLylmhwpvpaidhyVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 150 LSKPGLkyKPVCNQVECHPYLNQRKLLDFCRVDK----SFPVL-------LDDPVLGSMAKKYNRTPALIALRYQVQRGV 218
Cdd:PRK11565 149 IDETGV--TPVINQIELHPLMQQRQLHAWNATHKiqteSWSPLaqggkgvFDQKVIRDLADKYGKTPAQIVIRWHLDSGL 226
|
250 260
....*....|....*....|...
gi 1720374595 219 VVLAKSFIEKRIKENMQVFEFQL 241
Cdd:PRK11565 227 VVIPKSVTPSRIAENFDVFDFRL 249
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-239 |
4.68e-43 |
|
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: 148.54 E-value: 4.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 10 LNDGHFIPILGFGTSApQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDG-TVKREDIFCTSKVWQT 88
Cdd:cd19122 3 LNNGVKIPAVGFGTFA-NEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 89 FHRPELV---------QPGENYF------------------PK-DENGKFIYDAvDICD----TWEAMEKCKDAGLAKSI 136
Cdd:cd19122 82 LHEPEDVkwsidnslkNLKLDYIdlflvhwpiaaekndqrsPKlGPDGKYVILK-DLTEnpepTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 137 GVCNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCRVDKSFPV-----------------LLDDPVLGSMAK 199
Cdd:cd19122 161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEaysplgsqnqvpstgerVSENPTLNEVAE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720374595 200 KYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEF 239
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIEL 278
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
16-250 |
3.21e-42 |
|
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: 145.45 E-value: 3.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGTSA---PQEVP---RSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRskivdgTVKREDIFCTSKVW 86
Cdd:cd19072 4 VPVLGLGTWGiggGMSKDysdDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 QT-FHRPELVQPGENYFpKDENGKFI--Y------DAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPGlKY 157
Cdd:cd19072 78 PDhLKYDDVIKAAKESL-KRLGTDYIdlYlihwpnPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLK-KG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 158 KPVCNQVECHpYLNQR---KLLDFCRvDKSFPVL----LD---------DPVLGSMAKKYNRTPALIALRYQVQR-GVVV 220
Cdd:cd19072 156 PIVANQVEYN-LFDREeesGLLPYCQ-KNGIAIIayspLEkgklsnakgSPLLDEIAKKYGKTPAQIALNWLISKpNVIA 233
|
250 260 270
....*....|....*....|....*....|
gi 1720374595 221 LAKSFIEKRIKENMQVFEFQLTSVDMKVLD 250
Cdd:cd19072 234 IPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-253 |
5.56e-40 |
|
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: 140.14 E-value: 5.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 19 LGFGTSA----PQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgTVKREDIFCTSKV------ 85
Cdd:pfam00248 1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 86 WQTFHRPELVQPGENYFPKDENGKFIyD---------AVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPglK 156
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYI-DlyylhwpdpDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKG--K 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 157 YKPVCNQVECHPY--LNQRKLLDFCRvDKSFPV-------------------------------------LLDDPVLGSM 197
Cdd:pfam00248 154 IPIVAVQVEYNLLrrRQEEELLEYCK-KNGIPLiaysplggglltgkytrdpdkgpgerrrllkkgtplnLEALEALEEI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720374595 198 AKKYNRTPALIALRY--QVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 253
Cdd:pfam00248 233 AKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-257 |
2.91e-33 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 122.05 E-value: 2.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGTSAPQEVPrskATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVWQTFHRPELV 95
Cdd:PRK11172 3 IPAFGLGTFRLKDQV---VIDSVKTALELGYRAIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLAKDKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 96 QP---------GENY-------FPKDENGkfiydaVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPGlKYKP 159
Cdd:PRK11172 76 IPslkeslqklRTDYvdltlihWPSPNDE------VSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVG-AENI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 160 VCNQVECHPYLNQRKLLDFCRVD----KSFPVL-----LDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRI 230
Cdd:PRK11172 149 ATNQIELSPYLQNRKVVAFAKEHgihvTSYMTLaygkvLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENL 228
|
250 260
....*....|....*....|....*..
gi 1720374595 231 KENMQVFEFQLTSVDMKVLDGLNKNIR 257
Cdd:PRK11172 229 ASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-250 |
4.31e-29 |
|
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: 111.19 E-value: 4.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 6 QTVLLNDGHFIPILGFGTSAPQEVPRSKATE--ATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIF 80
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAQEieALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 81 CTSKVWQTFHRPELVQP---------GENYFpkDengkfIY-----DAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQL 146
Cdd:cd19138 74 LVSKVLPSNASRQGTVRacerslrrlGTDYL--D-----LYllhwrGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 147 EKILSKPGLKyKPVCNQVECHpyLNQR----KLLDFCRvDKSFPV---------------LLDDPVLGSMAKKYNRTPAL 207
Cdd:cd19138 147 EELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCR-EHGVPVmaysplaqggllrrgLLENPTLKEIAARHGATPAQ 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720374595 208 IALRYQV-QRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLD 250
Cdd:cd19138 223 VALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-250 |
2.62e-28 |
|
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: 108.81 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 13 GHFIPILGFGT------SAPQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSkivdgtVKREDIFCTS 83
Cdd:cd19137 1 GEKIPALGLGTwgiggfLTPDYSRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 84 KVWQT-FHRPELVQPGENYFPKDENgkfiyDAVDIC------------DTWEAMEKCKDAGLAKSIGVCNFNRRQLEKIL 150
Cdd:cd19137 75 KVWPTnLRYDDLLRSLQNSLRRLDT-----DYIDLYlihwpnpnipleETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 151 SKpgLKYKPVCNQVECHPY---LNQRKLLDFCR-----VDKSFP----VLLDDPVLGSMAKKYNRTPALIALRYQVQR-G 217
Cdd:cd19137 150 SK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQkngitVVAYSPlrrgLEKTNRTLEEIAKNYGKTIAQIALAWLIQKpN 227
|
250 260 270
....*....|....*....|....*....|...
gi 1720374595 218 VVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLD 250
Cdd:cd19137 228 VVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
34-250 |
9.77e-22 |
|
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: 91.91 E-value: 9.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 34 ATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRskivdGTVKREDIFCTSKVWQTFHR------------------- 91
Cdd:cd19093 28 LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIATKFAPLPWRltrrsvvkalkaslerlgl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 92 --PELVQ---PGENYFPkdengkfiydavdICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKI---LSKPGlkYKPVCNQ 163
Cdd:cd19093 103 dsIDLYQlhwPGPWYSQ-------------IEALMDGLADAVEEGLVRAVGVSNYSADQLRRAhkaLKERG--VPLASNQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 164 VE---CHPYLNQRKLLDFC-------------------------------RVDKSFPVLLD--DPV---LGSMAKKYNRT 204
Cdd:cd19093 168 VEyslLYRDPEQNGLLPACdelgitliaysplaqglltgkyspenpppggRRRLFGRKNLEkvQPLldaLEEIAEKYGKT 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720374595 205 PALIALRYQVQRGVVVL--AKSfiEKRIKENMQVFEFQLTSVDMKVLD 250
Cdd:cd19093 248 PAQVALNWLIAKGVVPIpgAKN--AEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-250 |
3.14e-18 |
|
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: 82.19 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 13 GHFIPILGFGTSA-----PQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSK 84
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 85 VwqtFHRPElvqpGENYFPKDENGKFIYDAVD------------------------ICDTWEAMEKCKDAGLAKSIGVCN 140
Cdd:cd19084 74 C---GLRWD----GGKGVTKDLSPESIRKEVEqslrrlqtdyidlyqihwpdpntpIEETAEALEKLKKEGKIRYIGVSN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 141 FNRRQLEKIlskpgLKY-KPVCNQVechPY--LNQ---RKLLDFCR----------------------VDKSFP------ 186
Cdd:cd19084 147 FSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRengigvlpygplaqglltgkykKEPTFPpddrrs 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 187 --VLLDDP----------VLGSMAKKYNRTPALIALRYQVQR----GVVVLAKSfiEKRIKENMQVFEFQLTSVDMKVLD 250
Cdd:cd19084 219 rfPFFRGEnfeknleivdKLKEIAEKYGKSLAQLAIAWTLAQpgvtSAIVGAKN--PEQLEENAGALDWELTEEELKEID 296
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
5-250 |
2.18e-17 |
|
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: 80.22 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 5 QQTVLLNDGHFIPILGFGT----SAPQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtvKRE 77
Cdd:COG0667 2 EYRRLGRSGLKVSRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 78 DIFCTSKVWQTFHrpelvqPGENyfPKDENGKFIYDAVD------------------------ICDTWEAMEKCKDAGLA 133
Cdd:COG0667 76 DVVIATKVGRRMG------PGPN--GRGLSREHIRRAVEaslrrlgtdyidlyqlhrpdpdtpIEETLGALDELVREGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 134 KSIGVCNFNRRQLEKILSKPGLKYKPVCNQVEchpY--LNQR---KLLDFC----------------------------- 179
Cdd:COG0667 148 RYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAArelgvgvlaysplagglltgkyrrgatfp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 180 ---RVDKSFPVLLDDP-------VLGSMAKKYNRTPALIALRYQVQRGVVVL----AKSfiEKRIKENMQVFEFQLTSVD 245
Cdd:COG0667 225 egdRAATNFVQGYLTErnlalvdALRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENLAAADLELSAED 302
|
....*
gi 1720374595 246 MKVLD 250
Cdd:COG0667 303 LAALD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-256 |
2.52e-15 |
|
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: 74.16 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGTSA--------PQEVPRSKATeaTKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSK 84
Cdd:cd19085 1 VSRLGLGCWQfgggywwgDQDDEESIAT--IHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 85 VW-QTFHRPELVQPGEN------------YF---PKDEngkfiydaVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEK 148
Cdd:cd19085 72 VSpDNLTPEDVRKSCERslkrlgtdyidlYQihwPSSD--------VPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 149 ILsKPGlkyKPVCNQVechPY-LNQR----KLLDFCR----------------------VDKSFP--------VLLDDP- 192
Cdd:cd19085 144 AL-DAG---RIDSNQL---PYnLLWRaieyEILPFCRehgigvlaysplaqglltgkfsSAEDFPpgdartrlFRHFEPg 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720374595 193 ----------VLGSMAKKYNRTPALIALRYQVQR----GVVVLAKSfiEKRIKENMQVFEFQLTSVDMKVLDGLNKNI 256
Cdd:cd19085 217 aeeetfealeKLKEIADELGVTMAQLALAWVLQQpgvtSVIVGARN--PEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
19-222 |
1.19e-14 |
|
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: 71.40 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 19 LGFGTSA-PQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtVKREDIFCTSKVWqtfHRPEL 94
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGG---HPPGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 95 VQPGENYFPKD---------ENGKFiyDAVDIC------------DTWEAMEKCKDAGLAKSIGVCNFNRRQLEKIL--S 151
Cdd:cd06660 75 DPSRSRLSPEHirrdleeslRRLGT--DYIDLYylhrddpstpveETLEALNELVREGKIRYIGVSNWSAERLAEALayA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720374595 152 KPGLKYKPVCNQVE---CHPYLNQRKLLDFCRvDKSFPVLlddpVLGSMAkkynRTPALIALRYQVQRGVVVLA 222
Cdd:cd06660 153 KAHGLPGFAAVQPQyslLDRSPMEEELLDWAE-ENGLPLL----AYSPLA----RGPAQLALAWLLSQPFVTVP 217
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-138 |
2.62e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 56.34 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 13 GHFIPILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQN-EKEVGLAIRSkivdgtvKREDIFCTSK------- 84
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATKtgardye 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720374595 85 -VWQTFHRpELVQPGENYF----------PKDENGKFIYDAVdicdtWEAMEKCKDAGLAKSIGV 138
Cdd:cd19100 81 gAKRDLER-SLKRLGTDYIdlyqlhavdtEEDLDQVFGPGGA-----LEALLEAKEEGKIRFIGI 139
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-138 |
7.80e-09 |
|
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: 55.25 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 17 PILGFGTS----APQEVPRSKATEATKIAIDAGFRHIDCAAVYQN-EKEVGLAIRskivdgTVKREDIFCTSKVwQTFHR 91
Cdd:cd19090 1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA------ELPREPLVLSTKV-GRLPE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720374595 92 PElvqpgenyfpKDENGKFIY------------DAVDIC-------DTW----------EAMEKCKDAGLAKSIGV 138
Cdd:cd19090 74 DT----------ADYSADRVRrsveeslerlgrDRIDLLmihdperVPWvdilapggalEALLELKEEGLIKHIGL 139
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-85 |
8.25e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 55.40 E-value: 8.25e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720374595 19 LGFGTS--APQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKIVDGTVKREDIFCTSKV 85
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKA 77
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
16-242 |
2.03e-08 |
|
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: 53.76 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGT---SAPQEV----PRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtvkREDIFCTSKV 85
Cdd:cd19088 1 VSRLGYGAmrlTGPGIWgppaDREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPY-------PDDVVIATKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 86 wqtfhrpELVQPGENYFPKDENGKFIYDA------------------------VDICDTWEAMEKCKDAGLAKSIGVCNF 141
Cdd:cd19088 74 -------GLVRTGPGWWGPDGSPEYLRQAveaslrrlgldridlyqlhridpkVPFEEQLGALAELQDEGLIRHIGLSNV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 142 NRRQLEKILSKPGLkykpVCNQVECHPYlNQR--KLLDFCRVD----------KSFPVLLDDPVLGSMAKKYNRTPALIA 209
Cdd:cd19088 147 TVAQIEEARAIVRI----VSVQNRYNLA-NRDdeGVLDYCEAAgiafipwfplGGGDLAQPGGLLAEVAARLGATPAQVA 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720374595 210 LRYQVQRGVVVLA---KSFIEkRIKENMQVFEFQLT 242
Cdd:cd19088 222 LAWLLARSPVMLPipgTSSVE-HLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
119-250 |
2.41e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 53.75 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 119 DTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPglkYKPVCNQVEcHPYLNQR---KLLDFCR--------------- 180
Cdd:cd19101 123 DAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---VPIVSNQVQ-YSLLDRRpenGMAALCEdhgikllaygtlagg 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 181 --------VDKSFPVLLDDP-----------------------VLGSMAKKYNRTPALIALRYQVQR----GVVVLAKSf 225
Cdd:cd19101 199 llsekylgVPEPTGPALETRslqkyklmidewggwdlfqellrTLKAIADKHGVSIANVAVRWVLDQpgvaGVIVGARN- 277
|
170 180
....*....|....*....|....*
gi 1720374595 226 iEKRIKENMQVFEFQLTSVDMKVLD 250
Cdd:cd19101 278 -SEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
11-250 |
5.42e-08 |
|
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: 53.00 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 11 NDGHFIPILGFGT-------SAPQEVPRSKATEAT---KIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtvkRE 77
Cdd:cd19091 8 RSGLKVSELALGTmtfggggGFFGAWGGVDQEEADrlvDIALDAGINFFDTADVYsegESEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 78 DIFCTSKVwqTFhrpelvQPGENyfpKDENG---KFIYDAVD------------------------ICDTWEAMEKCKDA 130
Cdd:cd19091 81 DVLIATKV--RG------RMGEG---PNDVGlsrHHIIRAVEaslkrlgtdyidlyqlhgfdaltpLEETLRALDDLVRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 131 GLAKSIGVCNFNRRQLEKILS---KPGLKyKPVCNQV-----------ECHPYLNQRKL--------------------- 175
Cdd:cd19091 150 GKVRYIGVSNFSAWQIMKALGiseRRGLA-RFVALQAyysllgrdlehELMPLALDQGVgllvwsplaggllsgkyrrgq 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 176 ------------LDFCRVD--KSFPVLlddPVLGSMAKKYNRTPALIALRYQVQR----GVVVLAKSfiEKRIKENMQVF 237
Cdd:cd19091 229 papegsrlrrtgFDFPPVDreRGYDVV---DALREIAKETGATPAQVALAWLLSRptvsSVIIGARN--EEQLEDNLGAA 303
|
330
....*....|...
gi 1720374595 238 EFQLTSVDMKVLD 250
Cdd:cd19091 304 GLSLTPEEIARLD 316
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-142 |
7.02e-08 |
|
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: 52.24 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 17 PILGFGTS----APQEVPRSKATEATKIAIDAGFRHIDCAAVYQN-EKEVGLAIRskivdgTVKREDIFCTSKVWQTFHR 91
Cdd:cd19095 1 SVLGLGTSgigrVWGVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVGTHGEG 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720374595 92 PELVqpgenyfpKDENGKFIY------------DAVDI-----CDTW-------EAMEKCKDAGLAKSIGVCNFN 142
Cdd:cd19095 75 GRDR--------KDFSPAAIRasierslrrlgtDYIDLlqlhgPSDDeltgevlETLEDLKAAGKVRYIGVSGDG 141
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-138 |
1.78e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 51.05 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 5 QQTVLLNDGHFIPILGFGTSAPQevprSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRskivdgTVKREDIFC 81
Cdd:cd19105 2 PYRTLGKTGLKVSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 82 TSKVwqtfhrpelvqpgenYFPKDENGK--FI-----------YDAVDIC--------DTW-------EAMEKCKDAGLA 133
Cdd:cd19105 72 ATKA---------------SPRLDKKDKaeLLksveeslkrlqTDYIDIYqlhgvdtpEERllneellEALEKLKKEGKV 136
|
....*
gi 1720374595 134 KSIGV 138
Cdd:cd19105 137 RFIGF 141
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-151 |
3.91e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 50.36 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGTSA-----------PQEVPRSKAteATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSkivdgtVKREDIFC 81
Cdd:cd19102 1 LTTIGLGTWAiggggwgggwgPQDDRDSIA--AIRAALDLGINWIDTAAVYglgHSEEVVGRALKG------LRDRPIVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 82 T--SKVW------QTFHRPE-------------------LVQ---PGENyfpkdengkfiydaVDICDTWEAMEKCKDAG 131
Cdd:cd19102 73 TkcGLLWdeegriRRSLKPAsiraeceaslrrlgvdvidLYQihwPDPD--------------EPIEEAWGALAELKEEG 138
|
170 180
....*....|....*....|
gi 1720374595 132 LAKSIGVCNFNRRQLEKILS 151
Cdd:cd19102 139 KVRAIGVSNFSVDQMKRCQA 158
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-238 |
6.21e-07 |
|
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: 49.48 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 17 PILGFGT-----SAPQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRskivdgTVKREDIFCTSKV-WQ 87
Cdd:cd19096 1 SVLGFGTmrlpeSDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALK------EGPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 88 TFHRPELVqpgENYFpkDE------------------NGKFIYDAVDICDTWEAMEKCKDAGLAKSIGvcnF----NRRQ 145
Cdd:cd19096 75 SVKSAEDF---RRIL--EEslkrlgvdyidfyllhglNSPEWLEKARKGGLLEFLEKAKKEGLIRHIG---FsfhdSPEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 146 LEKILSkpglkykpvCNQVEC----HPYLNQ-----RKLLDFCRvDKSFPVLLDDPVLGSM-----------AKKYNRTP 205
Cdd:cd19096 147 LKEILD---------SYDFDFvqlqYNYLDQenqagRPGIEYAA-KKGMGVIIMEPLKGGGlannppealaiLCGAPLSP 216
|
250 260 270
....*....|....*....|....*....|....*
gi 1720374595 206 ALIALRYQV-QRGV-VVLAKSFIEKRIKENMQVFE 238
Cdd:cd19096 217 AEWALRFLLsHPEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-222 |
7.40e-07 |
|
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: 49.48 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 18 ILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAI------RSKIV--------------DGTV 74
Cdd:cd19092 10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALalnpglREKIEiqtkcgirlgddprPGRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 75 KREDifcTSK---VW---------QT-------FHRPE-LVQPGEnyfpkdengkfiydavdicdTWEAMEKCKDAGLAK 134
Cdd:cd19092 90 KHYD---TSKehiLAsvegslkrlGTdyldlllLHRPDpLMDPEE--------------------VAEAFDELVKSGKVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 135 SIGVCNFNRRQLEkiLSKPGLKYKPVCNQVEC---HPYLNQRKLLDFCRVDKSFP----VLLDDPVLGSMAKKYNRTPAL 207
Cdd:cd19092 147 YFGVSNFTPSQIE--LLQSYLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPmawsPLGGGRLFGGFDERFQRLRAA 224
|
250
....*....|....*...
gi 1720374595 208 ---IALRYQVQRGVVVLA 222
Cdd:cd19092 225 leeLAEEYGVTIEAIALA 242
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-148 |
1.44e-06 |
|
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: 48.81 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 16 IPILGFGT------SAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSKVW 86
Cdd:cd19149 11 ASVIGLGTwaigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATKCG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 87 QTFHRpelvqpGENYFPKDENGKFIY---------------------DAVD------------ICDTWEAMEKCKDAGLA 133
Cdd:cd19149 84 LRWDR------EGGSFFFVRDGVTVYknlspesireeveqslkrlgtDYIDlyqthwqdvetpIEETMEALEELKRQGKI 157
|
170
....*....|....*
gi 1720374595 134 KSIGVCNFNRRQLEK 148
Cdd:cd19149 158 RAIGASNVSVEQIKE 172
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
20-139 |
8.80e-05 |
|
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: 42.85 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 20 GFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSKVwqtFHRPELVQ 96
Cdd:cd19086 12 GLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKF---GNRFDGGP 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720374595 97 PGENYFPKDengkFIYDAV------------DIC-------------DTWEAMEKCKDAGLAKSIGVC 139
Cdd:cd19086 82 ERPQDFSPE----YIREAVeaslkrlgtdyiDLYqlhnppdevldndELFEALEKLKQEGKIRAYGVS 145
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-85 |
1.99e-04 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 42.11 E-value: 1.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720374595 16 IPILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVY-QNEKEVGLAIRSkivdgtvKREDIFCTSKV 85
Cdd:COG1453 13 VSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKG-------PRDKVILATKL 76
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-113 |
2.99e-04 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 41.44 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720374595 17 PILGFGTSAP----QEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvKREDIFCTSKVWQTF 89
Cdd:cd19152 1 PKLGFGTAPLgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVGRLL 74
|
90 100
....*....|....*....|....*
gi 1720374595 90 H-RPELVQPGENYFPKDENGKFIYD 113
Cdd:cd19152 75 VpLQEVEPTFEPGFWNPLPFDAVFD 99
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
19-88 |
2.44e-03 |
|
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: 38.73 E-value: 2.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720374595 19 LGFGT--SAPQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRskivdgTVKREDIFCTSKV-WQT 88
Cdd:cd19074 7 LSLGTwlTFGGQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALK------GWPRESYVISTKVfWPT 76
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
19-85 |
4.23e-03 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 38.08 E-value: 4.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720374595 19 LGFGTsAP-----QEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvKREDIFCTSKV 85
Cdd:cd19161 3 LGLGT-AGlgnlyTAVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREK------PRDEFVLSTKV 70
|
|
| |
