##gff-version 3
P12378	UniProtKB	Chain	1	494	.	.	.	ID=PRO_0000074059;Note=UDP-glucose 6-dehydrogenase	
P12378	UniProtKB	Region	88	110	.	.	.	Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Region	129	135	.	.	.	Note=Allosteric switch region;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Region	321	325	.	.	.	Note=Important for formation of active hexamer structure;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Region	466	494	.	.	.	Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Active site	161	161	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Active site	220	220	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Active site	276	276	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	11	16	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	36	36	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	41	41	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	89	93	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	130	132	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	161	165	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	165	165	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	220	224	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	260	260	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	267	273	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	276	279	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	338	339	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	346	346	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Binding site	442	442	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Modified residue	107	107	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Modified residue	476	476	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
P12378	UniProtKB	Sequence conflict	157	157	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P12378	UniProtKB	Sequence conflict	278	281	.	.	.	Note=QKDV->ZZGK;Ontology_term=ECO:0000305;evidence=ECO:0000305