Annotations: 2GTV

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth X]	d2gtvx1	All alpha proteins	Chorismate mutase II	Chorismate mutase II	monomeric chorismate mutase	Chorismate mutase-like protein MJ0246	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)
A [auth X]	d2gtvx2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth X]	SCOP2 Family	Monomeric chorismate mutase	8029692	4001595	SCOP2 (2022-06-29)
A [auth X]	SCOP2 Superfamily	chorismate mutase ii	8042071	3001645	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth X]	PF01817	e2gtvX1	A: alpha bundles	X: Chorismate mutase II (From Topology)	H: Chorismate mutase II (From Topology)	T: Chorismate mutase II	F: PF01817	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth X]	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 [auth X]	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 [auth X]	chorismate mutase	isomerase activity chorismate mutase activity catalytic activity intramolecular transferase activity identical protein binding protein binding binding	oxoacid metabolic process cellular biosynthetic process organic hydroxy compound metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process monocarboxylic acid biosynthetic process benzene-containing compound metabolic process small molecule biosynthetic process salicylic acid biosynthetic process cellular metabolic process oxoacid metabolic process cellular biosynthetic process organic hydroxy compound metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process monocarboxylic acid biosynthetic process benzene-containing compound metabolic process small molecule biosynthetic process salicylic acid biosynthetic process cellular metabolic process carboxylic acid metabolic process salicylic acid metabolic process organic cyclic compound metabolic process biosynthetic process organic hydroxy compound biosynthetic process phenol-containing compound metabolic process organic cyclic compound biosynthetic process phenol-containing compound biosynthetic process metabolic process cellular process monocarboxylic acid metabolic process dicarboxylic acid metabolic process chorismate metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth X]	IPR036979	Chorismate mutase domain superfamily	Homologous Superfamily
A [auth X]	IPR010950	Chorismate mutase, archaeal	Domain
A [auth X]	IPR002701	Chorismate mutase II, prokaryotic-type	Domain
A [auth X]	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 R01GM133198.