##gff-version 3
B2HIL7	UniProtKB	Chain	1	2104	.	.	.	ID=PRO_0000406361;Note=Phenolphthiocerol synthesis polyketide synthase type I Pks15/1	
B2HIL7	UniProtKB	Domain	41	464	.	.	.	Note=Ketosynthase family 3 (KS3);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01348	
B2HIL7	UniProtKB	Domain	935	1207	.	.	.	Note=PKS/mFAS DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363	
B2HIL7	UniProtKB	Domain	2004	2079	.	.	.	Note=Carrier;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258	
B2HIL7	UniProtKB	Region	571	887	.	.	.	Note=Acyltransferase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
B2HIL7	UniProtKB	Region	935	1095	.	.	.	Note=Dehydratase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
B2HIL7	UniProtKB	Region	935	1057	.	.	.	Note=N-terminal hotdog fold;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363	
B2HIL7	UniProtKB	Region	1069	1207	.	.	.	Note=C-terminal hotdog fold;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363	
B2HIL7	UniProtKB	Region	1400	1705	.	.	.	Note=Enoylreductase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
B2HIL7	UniProtKB	Region	1718	1899	.	.	.	Note=Beta-ketoacyl reductase (KR)	
B2HIL7	UniProtKB	Region	2081	2104	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B2HIL7	UniProtKB	Active site	211	211	.	.	.	Note=For beta-ketoacyl synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01348	
B2HIL7	UniProtKB	Active site	346	346	.	.	.	Note=For beta-ketoacyl synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01348	
B2HIL7	UniProtKB	Active site	386	386	.	.	.	Note=For beta-ketoacyl synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01348	
B2HIL7	UniProtKB	Active site	662	662	.	.	.	Note=For acyltransferase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10022	
B2HIL7	UniProtKB	Active site	967	967	.	.	.	Note=Proton acceptor%3B for dehydratase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363	
B2HIL7	UniProtKB	Active site	1128	1128	.	.	.	Note=Proton donor%3B for dehydratase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01363	
B2HIL7	UniProtKB	Binding site	1530	1547	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
B2HIL7	UniProtKB	Binding site	1719	1734	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
B2HIL7	UniProtKB	Modified residue	2039	2039	.	.	.	Note=O-(pantetheine 4'-phosphoryl)serine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258	
B2HIL7	UniProtKB	Mutagenesis	211	211	.	.	.	Note=The pHBA starter unit is not loaded onto Pks15/1 and thus the pHPA intermediate is not produced. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19799378;Dbxref=PMID:19799378	
B2HIL7	UniProtKB	Mutagenesis	2039	2039	.	.	.	Note=The pHBA starter unit is loaded onto Pks15/1%2C but the pHPA intermediate is not produced. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19799378;Dbxref=PMID:19799378