Annotations: 7N8E

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ACPS	e7n8eA1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: 4'-phosphopantetheinyl transferase (From Topology)	T: 4'-phosphopantetheinyl transferase	F: ACPS	ECOD (1.6)
A	EntD	e7n8eA2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: 4'-phosphopantetheinyl transferase (From Topology)	T: 4'-phosphopantetheinyl transferase	F: EntD	ECOD (1.6)
B	ACPS	e7n8eB1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: 4'-phosphopantetheinyl transferase (From Topology)	T: 4'-phosphopantetheinyl transferase	F: ACPS	ECOD (1.6)
B	EntD	e7n8eB2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: 4'-phosphopantetheinyl transferase (From Topology)	T: 4'-phosphopantetheinyl transferase	F: EntD	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF17837	4'-phosphopantetheinyl transferase N-terminal domain (4PPT_N)	4'-phosphopantetheinyl transferase N-terminal domain	This entry represents the N-terminal domain from 4'- phosphopantetheinyl transferase enzymes. This domain is structurally related to the Pfam:PF01648 domain with which it forms a pseudodimeric arrangement [2].	Domain
A, B	PF01648	4'-phosphopantetheinyl transferase superfamily (ACPS)	4'-phosphopantetheinyl transferase superfamily	Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of Pfam:PF00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of ...	Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of Pfam:PF00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP [1]. This superfamily consists of two subtypes: The ACPS type such as Swiss:P24224 and the Sfp type such as Swiss:P39135. The structure of the Sfp type is known [3], which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	4'-phosphopantetheinyl transferase PptT	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding holo-[acyl-carrier-protein] synthase activity transferase activity catalytic activity phosphotransferase activity, for other substituted phosphate groups transferase activity, transferring phosphorus-containing groups	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 secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process catechol-containing compound biosynthetic process catechol-containing siderophore biosynthetic process enterobactin metabolic 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 secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process catechol-containing compound biosynthetic process catechol-containing siderophore biosynthetic process enterobactin metabolic process macrolide biosynthetic process macrolide metabolic process biosynthetic process peptide biosynthetic process polyketide biosynthetic process lactone metabolic process organic hydroxy compound biosynthetic process phenol-containing compound metabolic process phenol-containing compound biosynthetic process metabolic process nonribosomal peptide biosynthetic process peptide metabolic process	cell periphery plasma membrane membrane cellular anatomical entity protein-containing complex catalytic complex enterobactin synthetase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR037143	4'-phosphopantetheinyl transferase domain superfamily	Homologous Superfamily
A, B	IPR003542	Enterobactin synthetase-like, component D	Family
A, B	IPR041354	4'-phosphopantetheinyl transferase, N-terminal domain	Domain
A, B	IPR008278	4'-phosphopantetheinyl transferase domain	Domain

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.