##gff-version 3
Q9LVI8	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22223895;Dbxref=PMID:22223895	
Q9LVI8	UniProtKB	Chain	2	354	.	.	.	ID=PRO_0000153168;Note=Glutamine synthetase cytosolic isozyme 1-3	
Q9LVI8	UniProtKB	Domain	19	99	.	.	.	Note=GS beta-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01330	
Q9LVI8	UniProtKB	Domain	106	354	.	.	.	Note=GS catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01331	
Q9LVI8	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22223895;Dbxref=PMID:22223895	
Q9LVI8	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8LCE1	
Q9LVI8	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q43127	
Q9LVI8	UniProtKB	Mutagenesis	49	49	.	.	.	Note=3-fold increase in affinity for ammonium and catalytic efficiency. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16338958;Dbxref=PMID:16338958	
Q9LVI8	UniProtKB	Mutagenesis	174	174	.	.	.	Note=4-fold increase in affinity for ammonium and catalytic efficiency. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16338958;Dbxref=PMID:16338958	
Q9LVI8	UniProtKB	Sequence conflict	85	85	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305