3ZO8

Wild-type chorismate mutase of Bacillus subtilis at 1.6 A resolution

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d3zo8c_	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	YjgF-like	Chorismate mutase	Chorismate mutase	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
A	d3zo8a_	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	YjgF-like	Chorismate mutase	Chorismate mutase	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
B	d3zo8b_	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	YjgF-like	Chorismate mutase	Chorismate mutase	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
D	d3zo8d_	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	YjgF-like	Chorismate mutase	Chorismate mutase	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
E	d3zo8e_	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	YjgF-like	Chorismate mutase	Chorismate mutase	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
F	d3zo8f_	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	YjgF-like	Chorismate mutase	Chorismate mutase	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	YjgF-like	8035953	3001733	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	YjgF-like	8035953	3001733	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	YjgF-like	8035953	3001733	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	YjgF-like	8035953	3001733	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	YjgF-like	8035953	3001733	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	YjgF-like	8035953	3001733	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C	CM_1	e3zo8C1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: YjgF-like (From Topology)	T: YjgF-like	F: CM_1	ECOD (1.6)
A	CM_1	e3zo8A1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: YjgF-like (From Topology)	T: YjgF-like	F: CM_1	ECOD (1.6)
B	CM_1	e3zo8B1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: YjgF-like (From Topology)	T: YjgF-like	F: CM_1	ECOD (1.6)
D	CM_1	e3zo8D1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: YjgF-like (From Topology)	T: YjgF-like	F: CM_1	ECOD (1.6)
E	CM_1	e3zo8E1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: YjgF-like (From Topology)	T: YjgF-like	F: CM_1	ECOD (1.6)
F	CM_1	e3zo8F1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: YjgF-like (From Topology)	T: YjgF-like	F: CM_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.30.1330.40	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
A	3.30.1330.40	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
B	3.30.1330.40	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
D	3.30.1330.40	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
E	3.30.1330.40	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
F	3.30.1330.40	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF07736	Chorismate mutase type I (CM_1)	Chorismate mutase type I	Chorismate mutase (CM) EC:5.4.99.5 catalyses the the conversion of chorismate to prephenate in the shikimate pathway of tyrosine and phenylalanine biosynthesis in bacteria, fungi and plants [1,2]. The three types of CM are AroH class, AroQ class, ...	Chorismate mutase (CM) EC:5.4.99.5 catalyses the the conversion of chorismate to prephenate in the shikimate pathway of tyrosine and phenylalanine biosynthesis in bacteria, fungi and plants [1,2]. The three types of CM are AroH class, AroQ class, prokaryotic type and AroQ class, eukaryotic type. Structurally CMs can be divided into two main groups: type I (AroH) class and type II (AroQ). Type I (AroH) CMs include CMs characterised by a trimeric pseudo alpha/beta barrel structure [2]. The two types of the AroQ structural class (the Escherichia coli CM dimer and the yeast CM monomer) can be structurally superimposed, and the topology of the four-helix bundle forming the active site is conserved [3]. CMs can be monofunctional or bifunctional (generally fused to another shikimate pathway member). Despite the structural differences, all CMs perform the same basic reaction [2]. This entry represents chorismate mutases of the AroH class predominantly from Terrabacteria.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	CHORISMATE MUTASE AROH	isomerase activity chorismate mutase activity catalytic activity intramolecular transferase activity	amino acid biosynthetic process biosynthetic process amino acid metabolic process primary metabolic process metabolic process cellular process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process amino acid biosynthetic process biosynthetic process amino acid metabolic process primary metabolic process metabolic process cellular process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process dicarboxylic acid metabolic process chorismate metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR008243	Chorismate mutase, AroH class	Family
A, B, C, D, E A, B, C, D, E, F	IPR035959	RutC-like superfamily	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
D, F	chorismate mutase (AroH) M-CSA #474	Chorismate mutase (CM; EC:5.4.99.5) catalyses the rearrangement of chorismate to prephenat, the reaction at the branch point of the biosynthetic pathway leading to the three aromatic amino acids, phenylalanine, tryptophan and tyrosine (chorismic acid is the last common intermediate, and CM leads to the L-phenylalanine/L-tyrosine branch). It is part of the shikimate pathway, which is present only in bacteria, fungi and plants. This entry represents a family of monofunctional (non-fused) chorismate mutases from Gram-positive bacteria (Firmicutes) and cyanobacteria. They are monofunctional, homotrimeric, non-allosteric enzymes and are not regulated by the end-product aromatic amino acids (unlike those CMs of the AroQ-type).	Defined by 7 residues: ARG:D-7GLU:D-78ARG:D-90TYR:D-108ARG:D-116ARG:F-63CYS:F-75 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.4.99.5 (PDB Primary Data) Search M-CSA Motif + EC 5.4.99.5

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.