##gff-version 3
O70475	UniProtKB	Chain	1	493	.	.	.	ID=PRO_0000074061;Note=UDP-glucose 6-dehydrogenase	
O70475	UniProtKB	Region	88	110	.	.	.	Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Region	129	135	.	.	.	Note=Allosteric switch region;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Region	321	325	.	.	.	Note=Important for formation of active hexamer structure;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Region	466	493	.	.	.	Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Active site	161	161	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Active site	220	220	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Active site	276	276	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	11	16	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	36	36	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	41	41	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	89	93	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	130	132	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	161	165	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	165	165	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	220	224	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	260	260	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	267	273	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	276	279	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	338	339	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	346	346	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Binding site	442	442	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60701	
O70475	UniProtKB	Modified residue	107	107	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
O70475	UniProtKB	Modified residue	474	474	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:19131326,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:19131326,PMID:21183079	
O70475	UniProtKB	Mutagenesis	302	302	.	.	.	Note=In lzme%3B causes arrest of embryonic development during gastrulation due to chondroitin sulfate and heparan sulfate deficiency%2C impaired FGF signaling and impaired migration of mesoderm and endoderm. Q->QFQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14505572;Dbxref=PMID:14505572