##gff-version 3
P51647	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250,ECO:0000269;evidence=ECO:0000250|UniProtKB:P15437,ECO:0000269|PubMed:7832787;Dbxref=PMID:7832787	
P51647	UniProtKB	Chain	2	501	.	.	.	ID=PRO_0000056419;Note=Aldehyde dehydrogenase 1A1	
P51647	UniProtKB	Region	336	501	.	.	.	Note=Mediates interaction with PRMT3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Active site	269	269	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
P51647	UniProtKB	Active site	303	303	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
P51647	UniProtKB	Binding site	167	170	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Binding site	193	196	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Binding site	226	227	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Binding site	246	247	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Binding site	269	271	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Binding site	349	353	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Binding site	400	402	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Site	170	170	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20000	
P51647	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15437	
P51647	UniProtKB	Modified residue	91	91	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Modified residue	128	128	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Modified residue	252	252	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Modified residue	337	337	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Modified residue	353	353	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Modified residue	367	367	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Modified residue	410	410	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Modified residue	413	413	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P51647	UniProtKB	Modified residue	419	419	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Modified residue	435	435	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Modified residue	495	495	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00352	
P51647	UniProtKB	Sequence conflict	100	100	.	.	.	Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P51647	UniProtKB	Sequence conflict	106	106	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P51647	UniProtKB	Sequence conflict	170	170	.	.	.	Note=N->E;Ontology_term=ECO:0000305;evidence=ECO:0000305