Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna26458.1-v1.0-hybrid |
Family | GT47 |
Protein Properties | Length: 1296 Molecular Weight: 146244 Isoelectric Point: 6.8567 |
Chromosome | Chromosome/Scaffold: 7 Start: 16492911 End: 16501666 |
Description | exostosin family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT47 | 333 | 686 | 0 |
KKRPLIYVYDLPPDFNSLLLEGRHFKFECVNRIYDDLNSTVWTDMLYGSQMALYESILASPYRTLNGEEADFFFVPVLDSCIITRADDAPHLSMQEHKGL RSSLTLEYYKKAYDHIVEQYPFWNHSSGRDHIWFFSWDEGACYAPKEIWNSMMLIHWGNTNSKHKHSTTAYWGDNWNDISSDRRGNHPCFDPEKDLVLPA WKSPDVNSLSSKLWARPHEMRKTLFYFNGNLGPAYPNGRPENTYSMGIRQKLAEEFGSSPNKEGKLGKQHAEDVIVTPLRSENYHEDIASSIFCGVFPGD GWSGRMEDSILQGCIPVVIQDGIFLPYENVLNYESFAVRIREDEISNLINILRA |
Full Sequence |
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Protein Sequence Length: 1296 Download |
MIATIASIVG LISLALASIV HLFFFPLVPS FNYFSQAQNS CVPINGSAEA ITDHIKGIDL 60 EYQFPSDLHK AVVYRGAPWK AEIGRWLAGC LSITNEVNIV ELIGGSGCKN DCSGQGVCNR 120 ELGQCRCFHG YSGEGCSETL QLECNYPGSP DQPYGRWVVS ICSAHCDTKK AMCFCGEGTK 180 YPNRPVAEAC GFQVKPPSKP GAPKLTDWEK ADLDNLLTTN SSKPGWCNVD PAEAYALKVQ 240 FKQECDCKYD CLLGRFCEVP VLCTCINQCS GHGHCRGGFC QCNNGWYGID CSIPSVASSV 300 REWPQWLRPA QVNIPDNSHL TGKVVNLNAV VKKKRPLIYV YDLPPDFNSL LLEGRHFKFE 360 CVNRIYDDLN STVWTDMLYG SQMALYESIL ASPYRTLNGE EADFFFVPVL DSCIITRADD 420 APHLSMQEHK GLRSSLTLEY YKKAYDHIVE QYPFWNHSSG RDHIWFFSWD EGACYAPKEI 480 WNSMMLIHWG NTNSKHKHST TAYWGDNWND ISSDRRGNHP CFDPEKDLVL PAWKSPDVNS 540 LSSKLWARPH EMRKTLFYFN GNLGPAYPNG RPENTYSMGI RQKLAEEFGS SPNKEGKLGK 600 QHAEDVIVTP LRSENYHEDI ASSIFCGVFP GDGWSGRMED SILQGCIPVV IQDGIFLPYE 660 NVLNYESFAV RIREDEISNL INILRAFNET EIKFRLANVQ QIWQRFLYRD SILLEAERQK 720 TSFGRMGDWA VQFSQLIEDD VFQTFVQTAL EAKIIICVGH RSYPGYLIAP NIGHENCMKG 780 FVLSLKNMEG IMDHLVHERS KAQSNVEEMK VIWAGRSCLK VRALRKAAYV WKRIHELGLY 840 EEEASWLRFY VDEFTYAYVH WGMFAPAIKG SATEDQQQQW LPLANKMQII GTYAQTELGH 900 GSNIQGLETT VTFDPETDEF TIHSPTLTSS KWWPGGLGKV ATHAVVYALL ITNNQDYGVH 960 GFLVQIRSLD DHFPLPGVTV GDIGMKFGSG AFDSMDNGVL IFDQVRIPRN QMLMRFSRVT 1020 RQGKHIESNV LKQLLYGAMV CVRQIIVADT SIALSRLKSS AVRRQFRSPQ NQDSVETQVI 1080 EYKTQQSTLP FAGFYLCFQI CRRVVEMPIH RMTELIQKLE ANNFSMLPKA HACTAGLKAL 1140 TTSAAVDNVE ECRKLCGGHG YLFLMKTISQ LQTGEKPNGT TTYMGHAEHF IRCHCKVQKA 1200 EDWFHPTVIL EAFEARAIRL SKNLGDFLST RSISPKQASL ASDQVRNLYS KLRPNVIVLV 1260 DAYNYTHHFL GSILGCYDGN VYPKLYEEGM ERSTQ* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PTZ00460 | PTZ00460 | 1.0e-5 | 1233 | 1287 | 55 | + acyl-CoA dehydrogenase; Provisional | ||
cd01150 | AXO | 9.0e-10 | 1186 | 1290 | 108 | + Peroxisomal acyl-CoA oxidase. Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment. | ||
PTZ00460 | PTZ00460 | 7.0e-77 | 855 | 1161 | 315 | + acyl-CoA dehydrogenase; Provisional | ||
cd01150 | AXO | 2.0e-111 | 794 | 1220 | 486 | + Peroxisomal acyl-CoA oxidase. Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment. | ||
PLN02443 | PLN02443 | 0 | 788 | 1291 | 641 | + acyl-coenzyme A oxidase |
Gene Ontology | |
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GO Term | Description |
GO:0003995 | acyl-CoA dehydrogenase activity |
GO:0003997 | acyl-CoA oxidase activity |
GO:0005777 | peroxisome |
GO:0006635 | fatty acid beta-oxidation |
GO:0016020 | membrane |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2fon_C | 0 | 785 | 1227 | 17 | 524 | A Chain A, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa Oxidase From Lycopersicon Esculentum (Tomato) |
PDB | 2fon_C | 2e-21 | 1220 | 1287 | 583 | 650 | A Chain A, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa Oxidase From Lycopersicon Esculentum (Tomato) |
PDB | 2fon_B | 0 | 785 | 1227 | 17 | 524 | A Chain A, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa Oxidase From Lycopersicon Esculentum (Tomato) |
PDB | 2fon_B | 2e-21 | 1220 | 1287 | 583 | 650 | A Chain A, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa Oxidase From Lycopersicon Esculentum (Tomato) |
PDB | 2fon_A | 0 | 785 | 1227 | 17 | 524 | A Chain A, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa Oxidase From Lycopersicon Esculentum (Tomato) |