Annotations: 5HUB

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	CM_2	e5hubA1	A: alpha bundles	X: Chorismate mutase II (From Topology)	H: Chorismate mutase II (From Topology)	T: Chorismate mutase II	F: CM_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.59.10	Mainly Alpha	Up-down Bundle	Chorismate Mutase Domain, subunit A	Chorismate mutase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01817	Chorismate mutase type II (CM_2)	Chorismate mutase type II	Chorismate mutase EC:5.4.99.5 catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine [2,3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Chorismate mutase	isomerase activity chorismate mutase activity catalytic activity intramolecular transferase activity	oxoacid metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process small molecule metabolic process metabolic process cellular process organic acid metabolic process chorismate metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036979	Chorismate mutase domain superfamily	Homologous Superfamily
A	IPR010958	Chorismate mutase, high GC Gram-positive bacteria/archaeal	Domain
A	IPR051331	Chorismate mutase-related enzymes	Family
A	IPR002701	Chorismate mutase II, prokaryotic-type	Domain
A	IPR036263	Chorismate mutase type II superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.