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InterPro: IPR008162 Inorganic pyrophosphatase

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1765 proteins

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Accession

IPR008162 Pyrophosphatase

Secondary

IPR001596 , IPR008163

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.90.80.10	Pyrophosphatase	1654
Pfam	PF00719	Pyrophosphatase	1674
PROSITE pattern	PS00387	PPASE	1488
PANTHER	PTHR10286	Pyrophosphatase	1663
SuperFamily	SSF50324	Pyrophosphatase	1726
Signatures in BioMart

GO Term annotation Help

Process

GO:0006796 phosphate metabolic process

Function

GO:0000287 magnesium ion binding
GO:0004427 inorganic diphosphatase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

Inorganic pyrophosphatase (EC:3.6.1.1) (PPase) [1, 2] is the enzyme responsible for the hydrolysis of pyrophosphate (PPi) which is formed principally as the product of the many biosynthetic reactions that utilise ATP. All known PPases require the presence of divalent metal cations, with magnesium conferring the highest activity. Among other residues, a lysine has been postulated to be part of or close to the active site. PPases have been sequenced from bacteria such as Escherichia coli (homohexamer), Bacillus PS3 (Thermophilic bacterium PS-3) and Thermus thermophilus, from the archaebacteria Thermoplasma acidophilum, from fungi (homodimer), from a plant, and from bovine retina. In yeast, a mitochondrial isoform of PPase has been characterised which seems to be involved in energy production and whose activity is stimulated by uncouplers of ATP synthesis.

The sequences of PPases share some regions of similarities, among which is a region that contains three conserved aspartates that are involved in the binding of cations.

Structural links Help

PDB - click here

SCOP: b.40.5.1

CATH: 3.90.80.10

Database links Help

PDBe-motif: PS00387

Enzyme: EC:3.6.1.1

PROSITE doc: PDOC00325

PANDIT: PF00719

Blocks: IPB008162

Taxonomic coverage Help

Example proteins Help

O77460 Inorganic pyrophosphatase

P00817 Inorganic pyrophosphatase

Q15181 Inorganic pyrophosphatase

Q18680 Probable inorganic pyrophosphatase 1

Q91VM9 Inorganic pyrophosphatase 2, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008162	Inorganic pyrophosphatase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Lahti R, Kolakowski LF Jr, Heinonen J, Vihinen M, Pohjanoksa K, Cooperman BS. Conservation of functional residues between yeast and E. coli inorganic pyrophosphatases. Biochim. Biophys. Acta 1038 338-45 1990 [PubMed: 2160278] http://dx.doi.org/10.1016/0167-4838(90)90246-C
2.	Cooperman BS, Baykov AA, Lahti R. Evolutionary conservation of the active site of soluble inorganic pyrophosphatase. Trends Biochem. Sci. 17 262-6 1992 [PubMed: 1323891] http://dx.doi.org/10.1016/0968-0004(92)90406-Y

Additional Reading Open in usermanual
	Samygina VR, Moiseev VM, Rodina EV, Vorobyeva NN, Popov AN, Kurilova SA, Nazarova TI, Avaeva SM, Bartunik HD. Reversible inhibition of Escherichia coli inorganic pyrophosphatase by fluoride: trapped catalytic intermediates in cryo-crystallographic studies. J. Mol. Biol. 366 2007 1305-17 [PubMed: 17196979] http://dx.doi.org/10.1016/j.jmb.2006.11.082
	Wu CA, Lokanath NK, Kim DY, Park HJ, Hwang HY, Kim ST, Suh SW, Kim KK. Structure of inorganic pyrophosphatase from Helicobacter pylori. Acta Crystallogr. D Biol. Crystallogr. 61 2005 1459-64 [PubMed: 16239722] http://dx.doi.org/10.1107/S0907444905025667
	Chao TC, Huang H, Tsai JY, Huang CY, Sun YJ. Kinetic and structural properties of inorganic pyrophosphatase from the pathogenic bacterium Helicobacter pylori. Proteins 65 2006 670-80 [PubMed: 16988955] http://dx.doi.org/10.1002/prot.21093
	Oksanen E, Ahonen AK, Tuominen H, Tuominen V, Lahti R, Goldman A, Heikinheimo P. A complete structural description of the catalytic cycle of yeast pyrophosphatase. Biochemistry 46 2007 1228-39 [PubMed: 17260952] http://dx.doi.org/10.1021/bi0619977
	Liu B, Bartlam M, Gao R, Zhou W, Pang H, Liu Y, Feng Y, Rao Z. Crystal structure of the hyperthermophilic inorganic pyrophosphatase from the archaeon Pyrococcus horikoshii. Biophys. J. 86 2004 420-7 [PubMed: 14695284] http://www.biophysj.org/cgi/content/abstract/86/1/420

InterPro 23.1