2C43

STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE- PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ACPS	e2c43A2	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	KOG0945	e2c43A1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: 4'-phosphopantetheinyl transferase (From Topology)	T: 4'-phosphopantetheinyl transferase	F: KOG0945	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.470.20	Alpha Beta	Alpha-Beta Complex	Ribosomal Protein L22	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	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	AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE	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	organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process lysine metabolic process lysine biosynthetic process via aminoadipic acid oxoacid metabolic process aspartate family amino acid biosynthetic process organonitrogen compound biosynthetic process aspartate family amino acid metabolic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process lysine biosynthetic process small molecule metabolic process small molecule biosynthetic process carboxylic acid metabolic process L-amino acid biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process proteinogenic amino acid biosynthetic process alpha-amino acid biosynthetic process catabolic process dicarboxylic acid catabolic process organic acid catabolic process cellular catabolic process carboxylic acid catabolic process pteridine-containing compound catabolic process 10-formyltetrahydrofolate catabolic process organonitrogen compound catabolic process 10-formyltetrahydrofolate metabolic process dicarboxylic acid metabolic process cellular modified amino acid metabolic process organic cyclic compound catabolic process organic cyclic compound metabolic process folic acid-containing compound catabolic process folic acid-containing compound metabolic process small molecule catabolic process pteridine-containing compound metabolic process tetrahydrofolate metabolic process organic substance catabolic process cellular modified amino acid catabolic process pantothenate metabolic process vitamin metabolic process amide metabolic process monocarboxylic acid metabolic process water-soluble vitamin metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR037143	4'-phosphopantetheinyl transferase domain superfamily	Homologous Superfamily
A	IPR008278	4'-phosphopantetheinyl transferase domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q9NRN7	lung cancer ovarian cancer plasma cell myeloma lymphoplasmacytic lymphoma Parkinson disease psoriasis osteosarcoma pituitary cancer

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.