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InterPro: IPR005946 Phosphoribosyl pyrophosphokinase

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2650 proteins

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

Accession

IPR005946 PRPP_kinase

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01251	ribP_PPkin	2650
Signatures in BioMart

InterPro Relationships Help

Contains

IPR000836 Phosphoribosyltransferase
IPR000842 Phosphoribosyl pyrophosphate synthetase, conserved site

GO Term annotation Help

Process

GO:0009165 nucleotide biosynthetic process

Function

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

InterPro annotation

Entry Details in BioMart

Abstract

Synonyms: phosphoribosylpyrophosphate synthetase

Phosphoribosyldiphosphate synthetase (PRPPsase, EC:2.7.6.1) catalyzes the transfer of an intact diphosphate (PP) group from ATP to ribose-5-phosphate (R-5-P), which results in the formation of AMP and 5-phospho-D-ribosyl--1-diphosphate (PRPP).

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate

PRPP is an essential precursor for purine and pyrimidine nucleotides, both in the de novo synthesis and in the salvage pathway as well as in the synthesis of pyridine nucleotide coenzymes. The activity of PRPPsase is highly regulated. Besides competitive inhibition at the substrate binding sites, most PRPPsases are regulated in an allosteric manner, in which ADP generally acts as the most potent inhibitor. In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions.

Structural links Help

PDB - click here

SCOP: c.61.1.2

CATH: 3.40.50.2020

Database links Help

Enzyme: EC:2.7.6.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005946

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O60256 Phosphoribosyl pyrophosphate synthetase-associated protein 2

O64888 Ribose-phosphate pyrophosphokinase 5

P32895 Ribose-phosphate pyrophosphokinase 1

Q69XQ6 Ribose-phosphate pyrophosphokinase 2

Q8R574 Phosphoribosyl pyrophosphate synthetase-associated protein 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005946	Phosphoribosyl pyrophosphokinase
IPR007337	RelB antitoxin
IPR000836	Phosphoribosyltransferase
IPR000842	Phosphoribosyl pyrophosphate synthetase, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Help

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
	Kadziola A, Jepsen CH, Johansson E, McGuire J, Larsen S, Hove-Jensen B. Novel class III phosphoribosyl diphosphate synthase: structure and properties of the tetrameric, phosphate-activated, non-allosterically inhibited enzyme from Methanocaldococcus jannaschii. J. Mol. Biol. 354 2005 815-28 [PubMed: 16288921] http://dx.doi.org/10.1016/j.jmb.2005.10.001
	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
	Kita K, Ishizuka T, Ishijima S, Sonoda T, Tatibana M. A novel 39-kDa phosphoribosylpyrophosphate synthetase-associated protein of rat liver. Cloning, high sequence similarity to the catalytic subunits, and a negative regulatory role. J. Biol. Chem. 269 1994 8334-40 [PubMed: 8132556] http://intl.jbc.org/cgi/reprint/269/11/8334.pdf

InterPro 23.1