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InterPro: IPR008179 Phosphoribosyl-ATP pyrophosphohydrolase

Protein matches Help

UniProtKB

Matches:

1455 proteins

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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

IPR008179 PRib-ATP_pyrophosphohydrolase

Secondary

IPR002497 , IPR008178

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01503	PRA-PH	1455
TIGRFAMs	TIGR03188	histidine_hisI	1426
Signatures in BioMart

InterPro Relationships Help

Found in

IPR016298 Histidine biosynthesis trifunctional-protein

GO Term annotation Help

Process

GO:0000105 histidine biosynthetic process

Function

GO:0004636 phosphoribosyl-ATP diphosphatase activity

InterPro annotation

Entry Details in BioMart

Abstract

Phosphoribosyl-ATP pyrophosphatase, EC:3.6.1.31 catalyses the second step in the histidine biosynthetic pathway:

5-phosphoribosyl-ATP + H2O = 5-phosphoribosyl-AMP + PPi

The Neurospora crassa enzyme also catalyzes the reactions of histidinol dehydrogenase (EC:1.1.1.23) and phosphoribosyl-AMP cyclohydrolase (EC:3.5.4.19).

Structural links Help

PDB - click here

SCOP: a.204.1.4

Database links Help

Enzyme: EC:3.6.1.31

PANDIT: PF01503

Blocks: IPB008179

Pfam Clan: CL0231.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008179

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A1RTU9 Phosphoribosyl-ATP pyrophosphatase

O82768 Histidine biosynthesis bifunctional protein hisIE, chloroplastic

P00815 Histidine biosynthesis trifunctional protein

P0A5B1 Phosphoribosyl-ATP pyrophosphatase

P74755 Histidine biosynthesis bifunctional protein hisIE

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR016298	Histidine biosynthesis trifunctional-protein
IPR008179	Phosphoribosyl-ATP pyrophosphohydrolase
IPR002496	Phosphoribosyl-AMP cyclohydrolase
IPR012131	Histidinol dehydrogenase, prokaryotic-type
IPR016161	Aldehyde/histidinol dehydrogenase
IPR001692	Histidinol dehydrogenase, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Javid-Majd F, Yang D, Ioerger TR, Sacchettini JC. The 1.25 A resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis. Acta Crystallogr. D Biol. Crystallogr. 64 2008 627-35 [PubMed: 18560150] http://dx.doi.org/10.1107/S0907444908007105
	Keesey JK Jr, Bigelis R, Fink GR. The product of the his4 gene cluster in Saccharomyces cerevisiae. A trifunctional polypeptide. J. Biol. Chem. 254 1979 7427-33 [PubMed: 379004] http://intl.jbc.org/cgi/content/abstract/254/15/7427
	Bruni CB, Carlomagno MS, Formisano S, Paolella G. Primary and secondary structural homologies between the HIS4 gene product of Saccharomyces cerevisiae and the hisIE and hisD gene products of Escherichia coli and Salmonella typhimurium. Mol. Gen. Genet. 203 1986 389-96 [PubMed: 3528746] http://dx.doi.org/10.1007/BF00422062

InterPro 23.1