2FN0

Crystal structure of Yersinia enterocolitica salicylate synthase (Irp9)

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2fn0a1	Alpha and beta proteins (a+b)	ADC synthase	ADC synthase	ADC synthase	Salicylate synthetase Irp9	(Yersinia enterocolitica ) [TaxId: 630 ],	SCOPe (2.08)
A	d2fn0a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Yersinia enterocolitica ) [TaxId: 630 ],	SCOPe (2.08)
B	d2fn0b2	Alpha and beta proteins (a+b)	ADC synthase	ADC synthase	ADC synthase	Salicylate synthetase Irp9	(Yersinia enterocolitica ) [TaxId: 630 ],	SCOPe (2.08)
B	d2fn0b3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Yersinia enterocolitica ) [TaxId: 630 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ADC synthase	8041163	3001093	SCOP2B (2022-06-29)
B	SCOP2 Family	ADC synthase	8028784	4002317	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	ADC synthase	8041163	3001093	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	Chorismate_bind	e2fn0A1	A: a+b duplicates or obligate multimers	X: ADC synthase (From Topology)	H: ADC synthase (From Topology)	T: ADC synthase	F: Chorismate_bind	ECOD (1.6)
B	Chorismate_bind	e2fn0B1	A: a+b duplicates or obligate multimers	X: ADC synthase (From Topology)	H: ADC synthase (From Topology)	T: ADC synthase	F: Chorismate_bind	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.60.120.10	Alpha Beta	4-Layer Sandwich	Anthranilate synthase	Anthranilate synthase	CATH (4.3.0)
B	3.60.120.10	Alpha Beta	4-Layer Sandwich	Anthranilate synthase	Anthranilate synthase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00425	chorismate binding enzyme (Chorismate_bind)	chorismate binding enzyme	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	salicylate synthetase, Irp9	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding isomerase activity isochorismate synthase activity intramolecular hydroxytransferase activity catalytic activity intramolecular transferase activity lyase activity carbon-oxygen lyase activity oxo-acid-lyase activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding isomerase activity isochorismate synthase activity intramolecular hydroxytransferase activity catalytic activity intramolecular transferase activity lyase activity carbon-oxygen lyase activity oxo-acid-lyase activity carbon-carbon lyase activity	siderophore biosynthetic process peptide biosynthetic process biosynthetic process secondary metabolite biosynthetic process siderophore metabolic process metabolic process cellular process nonribosomal peptide biosynthetic process peptide metabolic process secondary metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR019999	Anthranilate synthase component I-like	Family
A, B	IPR019996	Salicylate synthase	Family
A, B	IPR015890	Chorismate-utilising enzyme, C-terminal	Domain
A, B	IPR005801	ADC synthase	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.