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InterPro: IPR004385 Nucleoside diphosphate pyrophosphatase

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UniProtKB

Matches:

770 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

IPR004385 NDP_pyrophosphatase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR00052	NDP_pyrophos	770
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000086 NUDIX hydrolase domain

Contains

IPR020084 NUDIX hydrolase, conserved site

GO Term annotation Help

Function

GO:0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
GO:0046872 metal ion binding

InterPro annotation

Entry Details in BioMart

Abstract

This entry describes a family of proteins which appear to catalyse the hydrolysis of phosphorus-containing acid anhydrides such as nucleoside diphosphate, for example ADP-mannose and UDP-glucose [1]. Some of these enzymes play a key role in glycogen biosynthesis.

Structural links Help

PDB - click here

SCOP: d.113.1.1

CATH: 3.90.79.10

Database links Help

Enzyme: EC:3.6.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004385

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O95848 Uridine diphosphate glucose pyrophosphatase

P37128 GDP-mannose pyrophosphatase nudK

Q05B60 Uridine diphosphate glucose pyrophosphatase

Q9D142 Uridine diphosphate glucose pyrophosphatase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR015797	NUDIX hydrolase domain-like
IPR000086	NUDIX hydrolase domain
IPR004385	Nucleoside diphosphate pyrophosphatase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Yagi T, Baroja-Fernandez E, Yamamoto R, Munoz FJ, Akazawa T, Hong KS, Pozueta-Romero J. Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose. Biochem. J. 370 409-15 2003 [PubMed: 12429023] http://dx.doi.org/10.1042/BJ20021140

Additional Reading Open in usermanual
	Xu W, Dunn CA, O'handley SF, Smith DL, Bessman MJ. Three new Nudix hydrolases from Escherichia coli. J. Biol. Chem. 281 2006 22794-8 [PubMed: 16766526] http://dx.doi.org/10.1074/jbc.M603407200
	Gabelli SB, Bianchet MA, Bessman MJ, Amzel LM. The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family. Nat. Struct. Biol. 8 2001 467-72 [PubMed: 11323725] http://dx.doi.org/10.1038/87647
	Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ. Structural analysis of a set of proteins resulting from a bacterial genomics project. Proteins 60 2005 787-96 [PubMed: 16021622] http://dx.doi.org/10.1002/prot.20541
	Gabelli SB, Bianchet MA, Ohnishi Y, Ichikawa Y, Bessman MJ, Amzel LM. Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase. Biochemistry 41 2002 9279-85 [PubMed: 12135348] http://dx.doi.org/10.1021/bi0259296

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