##gff-version 3
Q99J39	UniProtKB	Transit peptide	1	38	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99J39	UniProtKB	Chain	39	492	.	.	.	ID=PRO_0000021090;Note=Malonyl-CoA decarboxylase%2C mitochondrial	
Q99J39	UniProtKB	Region	1	28	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99J39	UniProtKB	Region	39	189	.	.	.	Note=Alpha-helical domain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99J39	UniProtKB	Region	190	492	.	.	.	Note=Catalytic domain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99J39	UniProtKB	Motif	490	492	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99J39	UniProtKB	Active site	328	328	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99J39	UniProtKB	Active site	422	422	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99J39	UniProtKB	Binding site	298	304	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99J39	UniProtKB	Binding site	328	328	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99J39	UniProtKB	Binding site	422	422	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99J39	UniProtKB	Site	210	210	.	.	.	Note=Essential for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99J39	UniProtKB	Modified residue	58	58	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23746352;Dbxref=PMID:23746352	
Q99J39	UniProtKB	Modified residue	167	167	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23746352;Dbxref=PMID:23746352	
Q99J39	UniProtKB	Modified residue	167	167	.	.	.	Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
Q99J39	UniProtKB	Modified residue	210	210	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23746352;Dbxref=PMID:23746352	
Q99J39	UniProtKB	Modified residue	221	221	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
Q99J39	UniProtKB	Modified residue	316	316	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23746352;Dbxref=PMID:23746352	
Q99J39	UniProtKB	Modified residue	385	385	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23576753;Dbxref=PMID:23576753	
Q99J39	UniProtKB	Modified residue	385	385	.	.	.	Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
Q99J39	UniProtKB	Modified residue	388	388	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23746352;Dbxref=PMID:23746352	
Q99J39	UniProtKB	Modified residue	441	441	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23746352;Dbxref=PMID:23746352	
Q99J39	UniProtKB	Modified residue	471	471	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23746352;Dbxref=PMID:23746352	
Q99J39	UniProtKB	Disulfide bond	205	205	.	.	.	Note=Interchain;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99J39	UniProtKB	Alternative sequence	1	38	.	.	.	ID=VSP_018817;Note=In isoform Cytoplasmic+peroxisomal. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q99J39	UniProtKB	Mutagenesis	471	471	.	.	.	Note=Mimicks constitutive acetylation%2C leading to increased malonyl-CoA decarboxylase activity. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23746352;Dbxref=PMID:23746352	
Q99J39	UniProtKB	Mutagenesis	471	471	.	.	.	Note=Decreased acetylation%2C leading to reduced malonyl-CoA decarboxylase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23746352;Dbxref=PMID:23746352