##gff-version 3
Q8N4T8	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000319878;Note=3-oxoacyl-[acyl-carrier-protein] reductase	
Q8N4T8	UniProtKB	Active site	148	148	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
Q8N4T8	UniProtKB	Binding site	11	14	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25203508,ECO:0007744|PDB:4CQM;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Binding site	34	35	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25203508,ECO:0007744|PDB:4CQM;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Binding site	56	56	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25203508,ECO:0007744|PDB:4CQM;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Binding site	83	85	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25203508,ECO:0007744|PDB:4CQM;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Binding site	135	135	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Binding site	148	148	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25203508,ECO:0007744|PDB:4CQM;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Binding site	152	152	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25203508,ECO:0007744|PDB:4CQM;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Binding site	181	183	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25203508,ECO:0007744|PDB:4CQM;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Site	169	169	.	.	.	Note=Important for interaction with acyl carrier protein (ACP);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
Q8N4T8	UniProtKB	Modified residue	40	40	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91VT4	
Q8N4T8	UniProtKB	Modified residue	96	96	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91VT4	
Q8N4T8	UniProtKB	Modified residue	195	195	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91VT4	
Q8N4T8	UniProtKB	Alternative sequence	180	237	.	.	.	ID=VSP_031527;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q8N4T8	UniProtKB	Natural variant	70	70	.	.	.	ID=VAR_039049;Note=L->M;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:17974005,ECO:0007744|PubMed:21269460;Dbxref=dbSNP:rs2877380,PMID:14702039,PMID:15489334,PMID:17974005,PMID:21269460	
Q8N4T8	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Unable to restore growth of an OAR1-deficient yeast mutant. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Mutagenesis	12	12	.	.	.	Note=Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Mutagenesis	34	34	.	.	.	Note=Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Strongly reduces NADPH-dependent reductase activity with acetoacetyl-CoA and 9%2C10-phenanthrene quinone. No effect on NADH-dependent reductase activities. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Mutagenesis	135	135	.	.	.	Note=Unable to restore growth of an OAR1-deficient yeast mutant. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Mutagenesis	148	148	.	.	.	Note=Unable to restore growth of an OAR1-deficient yeast mutant. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Mutagenesis	152	152	.	.	.	Note=Unable to restore growth of an OAR1-deficient yeast mutant. Abolishes NADPH-dependent reductase activity with acetoacetyl-CoA. Strongly reduces NADPH-dependent reductase activity with 9%2C10-phenanthrene quinone. No effect on NADH-dependent reductase activities. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9%2C10-phenanthrene quinone. No effect on NADH-dependent reductase activities. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Unable to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9%2C10-phenanthrene quinone. No effect on NADH-dependent reductase activities. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25203508;Dbxref=PMID:25203508	
Q8N4T8	UniProtKB	Beta strand	4	8	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Turn	9	11	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Helix	14	23	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Turn	24	26	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Beta strand	28	34	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Helix	36	45	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Helix	60	69	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Turn	70	74	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Beta strand	77	82	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Turn	92	94	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQL	
Q8N4T8	UniProtKB	Helix	97	107	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Helix	109	124	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Beta strand	128	133	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Helix	136	138	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Helix	146	165	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Beta strand	171	178	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Helix	190	193	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQL	
Q8N4T8	UniProtKB	Helix	206	218	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Beta strand	226	232	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM	
Q8N4T8	UniProtKB	Helix	233	235	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CQM