##gff-version 3
Q9SI64	UniProtKB	Transit peptide	1	52	.	.	.	Note=Chloroplast;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9SI64	UniProtKB	Chain	53	702	.	.	.	ID=PRO_0000149946;Note=Arginine decarboxylase 1%2C chloroplastic	
Q9SI64	UniProtKB	Active site	524	524	.	.	.	Note=Proton donor%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
Q9SI64	UniProtKB	Binding site	288	288	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
Q9SI64	UniProtKB	Binding site	320	330	.	.	.	Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9SI64	UniProtKB	Binding site	325	325	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
Q9SI64	UniProtKB	Binding site	374	377	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
Q9SI64	UniProtKB	Binding site	436	437	.	.	.	Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07805	
Q9SI64	UniProtKB	Binding site	525	525	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07805	
Q9SI64	UniProtKB	Binding site	565	565	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
Q9SI64	UniProtKB	Site	285	285	.	.	.	Note=Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00860	
Q9SI64	UniProtKB	Modified residue	136	136	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
Q9SI64	UniProtKB	Mutagenesis	136	136	.	.	.	Note=Loss of decarboxylase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11576438;Dbxref=PMID:11576438	
Q9SI64	UniProtKB	Mutagenesis	524	524	.	.	.	Note=Loss of decarboxylase activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11576438;Dbxref=PMID:11576438	
Q9SI64	UniProtKB	Sequence conflict	452	452	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305