2FQ1

Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PP-binding	e2fq1A2	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PP-binding	ECOD (1.6)
A	Isochorismatase	e2fq1A1	A: a/b three-layered sandwiches	X: Isochorismatase-like hydrolases (From Topology)	H: Isochorismatase-like hydrolases (From Topology)	T: Isochorismatase-like hydrolases	F: Isochorismatase	ECOD (1.6)
B	PP-binding	e2fq1B4	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PP-binding	ECOD (1.6)
B	Isochorismatase	e2fq1B3	A: a/b three-layered sandwiches	X: Isochorismatase-like hydrolases (From Topology)	H: Isochorismatase-like hydrolases (From Topology)	T: Isochorismatase-like hydrolases	F: Isochorismatase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.850	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Isochorismatase-like	CATH (4.3.0)
A	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
B	3.40.50.850	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Isochorismatase-like	CATH (4.3.0)
B	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00857	Isochorismatase family (Isochorismatase)	Isochorismatase family	-	Family
A, B	PF00550	Phosphopantetheine attachment site (PP-binding)	Phosphopantetheine attachment site	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes memb ...	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Isochorismatase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding 2,3-dihydroxybenzoate-serine ligase activity acid-amino acid ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity vitamin binding amide binding modified amino acid binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding 2,3-dihydroxybenzoate-serine ligase activity acid-amino acid ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity vitamin binding amide binding modified amino acid binding phosphopantetheine binding transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups identical protein binding protein binding isochorismatase activity leukotriene-A4 hydrolase activity ether hydrolase activity hydrolase activity, acting on ether bonds hydrolase activity	enterobactin biosynthetic process polyketide metabolic process organic hydroxy compound metabolic process catechol-containing compound metabolic process secondary metabolic process antibiotic biosynthetic process siderophore biosynthetic process antibiotic metabolic process organic substance metabolic process secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process organic substance biosynthetic process catechol-containing compound biosynthetic process enterobactin biosynthetic process polyketide metabolic process organic hydroxy compound metabolic process catechol-containing compound metabolic process secondary metabolic process antibiotic biosynthetic process siderophore biosynthetic process antibiotic metabolic process organic substance metabolic process secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process organic substance biosynthetic process catechol-containing compound biosynthetic process catechol-containing siderophore biosynthetic process enterobactin metabolic process macrolide biosynthetic process macrolide metabolic process organic cyclic compound metabolic process biosynthetic process peptide biosynthetic process polyketide biosynthetic process lactone metabolic process organic hydroxy compound biosynthetic process phenol-containing compound metabolic process organic cyclic compound biosynthetic process phenol-containing compound biosynthetic process metabolic process nonribosomal peptide biosynthetic process peptide metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol cell periphery plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR009081	Phosphopantetheine binding ACP domain	Domain
A, B	IPR000868	Isochorismatase-like	Domain
A, B	IPR036380	Isochorismatase-like superfamily	Homologous Superfamily
A, B	IPR036736	ACP-like superfamily	Homologous Superfamily
A, B	IPR016291	Isochorismatase	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.