The domain within your query sequence starts at position 510 and ends at position 690; the E-value for the ACOX domain shown below is 6.4e-53.
DSAAPLAAYRWLVCYLLQESHRRYCQEKKSRGSDFEARNNSQVYGCRPLALAFMELTVMQ RFHEHIHSSGLSPSLRTVLGRLSTLYGLWCLSQHMALLYRGGYISGEQTGRAMEDAILTL CEQLKDDAVALVDVIAPSDFVLNSPIAKADGELYKNLWAAVLQQNGVLERAAWWPEFSAN K
ACOX |
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PFAM accession number: | PF01756 |
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Interpro abstract (IPR002655): | Acyl-CoA oxidase (ACO) acts on CoA derivatives of fatty acids with chain lengths from 8 to 18. It catalyses the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids [ (PUBMED:11872165) ]. Acyl-CoA oxidase is a homodimer and the polypeptide chain of the subunit is folded into the N-terminal alpha-domain, beta-domain, and C-terminal alpha-domain [ (PUBMED:11872165) ]. Functional differences between the peroxisomal acyl-CoA oxidases and the mitochondrial acyl-CoA dehydrogenases are attributed to structural differences in the FAD environments [ (PUBMED:15581893) ]. Experimental data indicate that, in the pumpkin, the expression pattern of ACOX is very similar to that of the glyoxysomal enzyme 3-ketoacyl-CoA thiolase [ (PUBMED:9525937) ]. In humans, defects in ACOX1 are the cause of pseudoneonatal adrenoleukodystrophy, also known as peroxisomal acyl-CoA oxidase deficiency. Pseudo-NALD is a peroxisomal single-enzyme disorder. Clinical features include mental retardation, leukodystrophy, seizures, mild hepatomegaly and hearing deficit. Pseudo-NALD is characterised by increased plasma levels of very-long chain fatty acids due to a decrease in, or absence of, peroxisome acyl-CoA oxidase activity, despite the peroxisomes being intact and functioning. This entry represents the Acyl-CoA oxidase C-terminal. |
GO process: | fatty acid beta-oxidation (GO:0006635) |
GO component: | peroxisome (GO:0005777) |
GO function: | acyl-CoA oxidase activity (GO:0003997) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry ACOX