3DAH

2.3 A crystal structure of ribose-phosphate pyrophosphokinase from Burkholderia pseudomallei

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d3daha1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	automated matches	automated matches	(Burkholderia pseudomallei 1710b ) [TaxId: 320372 ],	SCOPe (2.08)
B	d3dahb1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	automated matches	automated matches	(Burkholderia pseudomallei 1710b ) [TaxId: 320372 ],	SCOPe (2.08)
C	d3dahc1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	automated matches	automated matches	(Burkholderia pseudomallei 1710b ) [TaxId: 320372 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF13793	e3dahA1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: PF13793	ECOD (1.6)
A	PF14572	e3dahA4	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: PF14572	ECOD (1.6)
B	PF13793	e3dahB3	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: PF13793	ECOD (1.6)
B	PF14572	e3dahB4	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: PF14572	ECOD (1.6)
C	PF13793	e3dahC1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: PF13793	ECOD (1.6)
C	PF14572	e3dahC2	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: PF14572	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF14572	Phosphoribosyl synthetase-associated domain (Pribosyl_synth)	Phosphoribosyl synthetase-associated domain	This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.	Domain
A, B, C	PF13793	N-terminal domain of ribose phosphate pyrophosphokinase (Pribosyltran_N)	N-terminal domain of ribose phosphate pyrophosphokinase	This family is frequently found N-terminal to the Pribosyltran, Pfam:PF00156.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Ribose-phosphate pyrophosphokinase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding kinase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups ribose phosphate diphosphokinase activity diphosphotransferase activity	nucleobase-containing compound metabolic process organic substance metabolic process ribonucleoside monophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process organic substance biosynthetic process small molecule metabolic process nucleoside monophosphate metabolic process phosphorus metabolic process nucleoside phosphate metabolic process cellular metabolic process primary metabolic process nucleobase-containing compound biosynthetic process nucleoside monophosphate biosynthetic process nucleobase-containing compound metabolic process organic substance metabolic process ribonucleoside monophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process organic substance biosynthetic process small molecule metabolic process nucleoside monophosphate metabolic process phosphorus metabolic process nucleoside phosphate metabolic process cellular metabolic process primary metabolic process nucleobase-containing compound biosynthetic process nucleoside monophosphate biosynthetic process organic cyclic compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process organic cyclic compound biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process ribonucleoside monophosphate biosynthetic process 5-phosphoribose 1-diphosphate biosynthetic process ribose phosphate metabolic process carbohydrate derivative biosynthetic process carbohydrate derivative metabolic process 5-phosphoribose 1-diphosphate metabolic process ribose phosphate biosynthetic process phosphorylation nucleotide biosynthetic process nucleotide metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR000842	Phosphoribosyl pyrophosphate synthetase, conserved site	Conserved Site
A, B, C	IPR000836	Phosphoribosyltransferase domain	Domain
A, B, C	IPR037515	Ribose-phosphate pyrophosphokinase, bacterial-type	Family
A, B, C	IPR029057	Phosphoribosyltransferase-like	Homologous Superfamily
A, B, C	IPR029099	Ribose-phosphate pyrophosphokinase, N-terminal domain	Domain
A, B, C	IPR005946	Ribose-phosphate pyrophosphokinase	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.