The domain within your query sequence starts at position 553 and ends at position 707; the E-value for the ACOX domain shown below is 1.4e-45.

YGCRPLALAFMELTVMQRFHEHIHSSGLSPSLRTVLGRLSTLYGLWCLSQHMALLYRGGY
ISGEQTGRAMEDAILTLCEQLKDDAVALVDVIAPSDFVLNSPIAKADGEVSDLARYDLDL
PPAWHPFRLPLRN

ACOX

ACOX
PFAM accession number:PF01756
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