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InterPro: IPR000086 NUDIX hydrolase domain

Protein matches Help

UniProtKB

Matches:

18928 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

IPR000086 NUDIX_hydrolase_dom

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.90.79.10	NUDIX_hydrolase	17857
Pfam	PF00293	NUDIX	17770
Signatures in BioMart

InterPro Relationships Help

Parent

IPR015797 NUDIX hydrolase domain-like

Children

IPR003293 Nudix hydrolase 6-like
IPR003561 Mutator MutT protein
IPR003562 Mutator MutX protein
IPR003563 7,8-dihydro-8-oxoguanine triphosphatase
IPR003564 DATP pyrophosphohydrolase
IPR003565 Bis(5'-nucleosyl)-tetraphosphatase
IPR004385 Nucleoside diphosphate pyrophosphatase
IPR011876 Isopentenyl-diphosphate delta-isomerase, type 1
IPR014078 Nucleoside triphosphatase YtkD
IPR017397 NUDIX hydrolase, AtNUDT22

Found in

IPR003300 Viral protein D9
IPR003301 Viral protein D10

Contains

IPR000059 NUDIX hydrolase, NudL, conserved site
IPR020084 NUDIX hydrolase, conserved site
IPR020476 NUDIX hydrolase

GO Term annotation Help

Function

GO:0016787 hydrolase activity

InterPro annotation

Entry Details in BioMart

Abstract

MutT is a small bacterial protein (~12-15Kd) involved in the GO system [1] responsible for removing an oxidatively damaged form of guanine (8-hydroxy- guanine or 7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with near equal efficiency, leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate, with the concomitant release of pyrophosphate. A short conserved N-terminal region of mutT (designated the MutT domain) is also found in a variety of other prokaryotic, viral and eukaryotic proteins [2, 3, 4, 5].

The generic name `NUDIX hydrolases' (NUcleoside DIphosphate linked to some other moiety X) has been coined for this domain family [6]. The family can be divided into a number of subgroups, of which MutT anti- mutagenic activity represents only one type; most of the rest hydrolyse diverse nucleoside diphosphate derivatives (including ADP-ribose, GDP- mannose, TDP-glucose, NADH, UDP-sugars, dNTP and NTP).

Structural links Help

PDB - click here

SCOP: a.242.1.1 , d.113.1.1 , d.113.1.2 , d.113.1.3 , d.113.1.4 , d.113.1.5 , d.113.1.6 , d.113.1.7

CATH: 3.90.79.10

Database links Help

PDBe-motif: PS00893

Enzyme: EC:3.6

PROSITE doc: PDOC00695

PANDIT: PF00293

Blocks: IPB000086

Pfam Clan: CL0261.3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000086

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O22951 Nudix hydrolase 22, chloroplastic

O43809 Cleavage and polyadenylation specificity factor subunit 5

P53550 mRNA-decapping enzyme subunit 2

Q8R2U6 Diphosphoinositol polyphosphate phosphohydrolase 2

Q9U2M7 Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR015797	NUDIX hydrolase domain-like
IPR007722	Dcp2, box A
IPR003565	Bis(5'-nucleosyl)-tetraphosphatase
IPR016706	Cleavage/polyadenylation specificity factor, 25kDa subunit
IPR017397	NUDIX hydrolase, AtNUDT22
IPR020084	NUDIX hydrolase, conserved site
IPR000086	NUDIX hydrolase domain
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Michaels ML, Miller JH. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 174 6321-5 1992 [PubMed: 1328155] http://jb.asm.org/cgi/content/abstract/174/20/6321
2.	Koonin EV. A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses. Nucleic Acids Res. 21 4847 1993 [PubMed: 8233837] http://dx.doi.org/10.1093/nar/21.20.4847
3.	Mejean V, Salles C, Bullions LC, Bessman MJ, Claverys JP. Characterization of the mutX gene of Streptococcus pneumoniae as a homologue of Escherichia coli mutT, and tentative definition of a catalytic domain of the dGTP pyrophosphohydrolases. Mol. Microbiol. 11 323-30 1994 [PubMed: 8170394] http://dx.doi.org/10.1111/j.1365-2958.1994.tb00312.x
4.	Sakumi K, Furuichi M, Tsuzuki T, Kakuma T, Kawabata S, Maki H, Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 268 23524-30 1993 [PubMed: 8226881] http://intl.jbc.org/cgi/content/abstract/268/31/23524
5.	McLennan AG. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int. J. Mol. Med. 4 79-89 1999 [PubMed: 10373642]
6.	Bessman MJ, Frick DN, O'Handley SF. The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes. J. Biol. Chem. 271 25059-62 1996 [PubMed: 8810257] http://dx.doi.org/10.1074/jbc.271.41.25059

Additional Reading Open in usermanual
	de Ruyck J, Oudjama Y, Wouters J. Monoclinic form of isopentenyl diphosphate isomerase: a case of polymorphism in biomolecular crystals. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 2008 239-42 [PubMed: 18391416]
	She M, Decker CJ, Chen N, Tumati S, Parker R, Song H. Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. Nat. Struct. Mol. Biol. 13 2006 63-70 [PubMed: 16341225] http://dx.doi.org/10.1038/nsmb1033
	Thorsell AG, Persson C, Graslund S, Hammarstrom M, Busam RD, Hallberg BM. Crystal structure of human diphosphoinositol phosphatase 1. Proteins 77 2009 242-6 [PubMed: 19585659] http://dx.doi.org/10.1002/prot.22489
	She M, Decker CJ, Svergun DI, Round A, Chen N, Muhlrad D, Parker R, Song H. Structural basis of dcp2 recognition and activation by dcp1. Mol. Cell 29 2008 337-49 [PubMed: 18280239] http://dx.doi.org/10.1016/j.molcel.2008.01.002
	Buchko GW, Litvinova O, Robinson H, Yakunin AF, Kennedy MA. Functional and Structural Characterization of DR_0079 from Deinococcus radiodurans, a Novel Nudix Hydrolase with a Preference for Cytosine (Deoxy)ribonucleoside 5'-Di- and Triphosphates. Biochemistry 2008 [PubMed: 18512963]

InterPro 23.1