1B6T

PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE IN COMPLEX WITH 3'-DEPHOSPHO-COA FROM ESCHERICHIA COLI

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)
A	d1b6ta_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	Adenylyltransferase	Phosphopantetheine adenylyltransferase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1b6tb_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	Adenylyltransferase	Phosphopantetheine adenylyltransferase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Nucleotidylyl transferase	8034591	3001541	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Nucleotidylyl transferase	8034591	3001541	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)
A	CTP_transf_like_1	e1b6tA1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: CTP_transf_like_1	ECOD (1.6)
B	CTP_transf_like_1	e1b6tB1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: CTP_transf_like_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
B	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01467	Cytidylyltransferase-like (CTP_transf_like)	Cytidylyltransferase-like	This family includes: Cholinephosphate cytidylyltransferase Swiss:P49585; glycerol-3-phosphate cytidylyltransferase Swiss:P27623. It also includes putative adenylyltransferases, and FAD synthases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROTEIN (PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE)	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pantetheine-phosphate adenylyltransferase activity adenylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups identical protein binding protein binding	coenzyme A biosynthetic process cellular biosynthetic process nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process small molecule metabolic process sulfur compound metabolic process amide metabolic process phosphorus metabolic process coenzyme A metabolic process nucleoside phosphate metabolic process cellular metabolic process primary metabolic process coenzyme A biosynthetic process cellular biosynthetic process nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process small molecule metabolic process sulfur compound metabolic process amide metabolic process phosphorus metabolic process coenzyme A metabolic process nucleoside phosphate metabolic process cellular metabolic process primary metabolic process amide biosynthetic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process sulfur compound biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004821	Cytidyltransferase-like domain	Domain
A, B	IPR001980	Phosphopantetheine adenylyltransferase	Family
A, B	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	pantetheine-phosphate adenylyltransferase M-CSA #299	Phosphopantetheine adenylyltransferase (PPAT), isolated from Escherichia coli, catalyses the magnesium-dependent adenylyl transfer from ATP to 4'-phosphopantetheine (Ppant or PhP) to form dephospho-CoA (dPCoA). This reaction is the penultimate step in the synthesis of CoA. PPAT belongs to the nucleotidyltransferase alpha/beta phosphodiesterase superfamily, whose members catalyse the transfer of a nucleotide monophosphate to a substrate by stabilising the transition state of the reaction. PPAT is a hexamer consisting of two trimers. While each subunit possesses an active site, it appears that only the subunits of one trimer will catalyse the reaction at a given time. The reaction proceeds via a random bi-bi mechanism in that the order of the binding of ATP and Ppant is not fixed, nor is the release of dPCoA and pyrophosphate. CoA can regulate the activity of PPAT by binding to the PPAT.PPi complex, thus preventing the binding of a new Ppant substrate molecule.	Defined by 4 residues: HIS:A-18LYS:A-42ARG:A-91SER:A-129 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.7.7.3 (PDB Primary Data) Search M-CSA Motif + EC 2.7.7.3

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.