##gff-version 3
O54754	UniProtKB	Chain	1	1333	.	.	.	ID=PRO_0000166106;Note=Aldehyde oxidase 1	
O54754	UniProtKB	Domain	4	91	.	.	.	Note=2Fe-2S ferredoxin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465	
O54754	UniProtKB	Domain	235	420	.	.	.	Note=FAD-binding PCMH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00718	
O54754	UniProtKB	Active site	1265	1265	.	.	.	Note=Proton acceptor%3B for azaheterocycle hydroxylase activity;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19401776;Dbxref=PMID:19401776	
O54754	UniProtKB	Binding site	43	43	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	48	48	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	51	51	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	73	73	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	112	112	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	113	113	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	116	116	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	148	148	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	150	150	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	150	150	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	263	270	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	344	344	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	353	353	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	357	357	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	366	366	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	410	410	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	801	802	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	1042	1042	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	1083	1086	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	1198	1198	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Binding site	1263	1263	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Modified residue	1063	1063	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06278	
O54754	UniProtKB	Natural variant	109	109	.	.	.	Note=In strain: 129/Sv. H->Q	
O54754	UniProtKB	Natural variant	168	168	.	.	.	Note=In strain: C57BL/6 XCBA and 129/Sv. A->G	
O54754	UniProtKB	Natural variant	449	449	.	.	.	Note=In strain: C57BL/6 XCBA. R->T	
O54754	UniProtKB	Natural variant	492	492	.	.	.	Note=In strain: C57BL/6 XCBA%3B requires 2 nucleotide substitutions. R->A	
O54754	UniProtKB	Natural variant	686	687	.	.	.	Note=In strain: 129/Sv. KQ->NE	
O54754	UniProtKB	Natural variant	857	857	.	.	.	Note=In strain: 129/Sv. E->D	
O54754	UniProtKB	Natural variant	983	983	.	.	.	Note=In strain: C57BL/6 XCBA. E->D	
O54754	UniProtKB	Natural variant	1169	1169	.	.	.	Note=In strain: C57BL/6 XCBA and 129/Sv. N->D	
O54754	UniProtKB	Natural variant	1329	1329	.	.	.	Note=In strain: C57BL/6 XCBA and 129/Sv. C->W	
O54754	UniProtKB	Mutagenesis	806	806	.	.	.	Note=Decreases substrate affinity and activity on benzaldehyde%2C phthalazine and acetaldehyde%2C while increases affinity for more hydrophobic aldehydes like retinal. Abolishes catalytic activity%3B when associated with R-884. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19401776;Dbxref=PMID:19401776	
O54754	UniProtKB	Mutagenesis	884	884	.	.	.	Note=Abolishes catalytic activity on phthalazine and acetaldehyde. Decreases catalytic efficiency on benzaldehyde and retinal. Abolishes catalytic activity%3B when associated with E-806. M->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19401776;Dbxref=PMID:19401776	
O54754	UniProtKB	Mutagenesis	1265	1265	.	.	.	Note=Abolishes catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19401776;Dbxref=PMID:19401776