EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR000842 Phosphoribosyl pyrophosphate synthetase, conserved site

Protein matches Help

UniProtKB

Matches:

1953 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000842 PRib-PP_synthetase_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00114	PRPP_SYNTHETASE	1953
Signatures in BioMart

InterPro Relationships Help

Found in

IPR005946 Phosphoribosyl pyrophosphokinase

GO Term annotation Help

Process

GO:0009156 ribonucleoside monophosphate biosynthetic process
GO:0044249 cellular biosynthetic process

Function

GO:0000287 magnesium ion binding
GO:0004749 ribose phosphate diphosphokinase activity

InterPro annotation

Entry Details in BioMart

Abstract

Phosphoribosyl pyrophosphate synthetase (EC:2.7.6.1) (PRib-PP synthetase) catalyses the formation of PRib-PP from ATP and ribose 5-phosphate. PRib-PP is then used in various biosynthetic pathways, for example in the formation of purines, pyrimidines, histidine and tryptophan. PRib-PP synthetase requires inorganic phosphate and magnesium ions for its stability and activity. In mammals, three isozymes of PRib-PP synthetase are found, while in yeast there are at least four isozymes. A very conserved region containing two conserved aspartic acid residues as well as a histidine has been suggested to be involved in binding divalent cations [1]. These residues are all potential ligands for a cation such as magnesium.

Structural links Help

PDB - click here

SCOP: c.61.1.2

CATH: 3.40.50.2020

Database links Help

PDBe-motif: PS00114

Enzyme: EC:2.7.6.1

PROSITE doc: PDOC00105

Blocks: IPB000842

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000842

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O64888 Ribose-phosphate pyrophosphokinase 5

P32895 Ribose-phosphate pyrophosphokinase 1

P60891 Ribose-phosphate pyrophosphokinase 1

Q69XQ6 Ribose-phosphate pyrophosphokinase 2

Q9CS42 Ribose-phosphate pyrophosphokinase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005946	Phosphoribosyl pyrophosphokinase
IPR000836	Phosphoribosyltransferase
IPR000842	Phosphoribosyl pyrophosphate synthetase, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Bower SG, Harlow KW, Switzer RL, Hove-Jensen B. Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site. J. Biol. Chem. 264 10287-91 1989 [PubMed: 2542328] http://intl.jbc.org/cgi/content/abstract/264/17/10287

Additional Reading Open in usermanual
	Eriksen TA, Kadziola A, Larsen S. Binding of cations in Bacillus subtilis phosphoribosyldiphosphate synthetase and their role in catalysis. Protein Sci. 11 2002 271-9 [PubMed: 11790837] http://dx.doi.org/10.1110/ps.28502
	Li S, Lu Y, Peng B, Ding J. Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site. Biochem. J. 401 2007 39-47 [PubMed: 16939420] http://dx.doi.org/10.1042/BJ20061066
	Eriksen TA, Kadziola A, Bentsen AK, Harlow KW, Larsen S. Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase. Nat. Struct. Biol. 7 2000 303-8 [PubMed: 10742175] http://dx.doi.org/10.1038/74069

InterPro 23.1