Conserved Site

NUDIX hydrolase, NudL, conserved site (IPR000059)

Short name: NUDIX_hydrolase_NudL_CS


Nudix hydrolases, which are commonly found in all kingdoms of life, are pyrophosphohydrolases predominantly acting on substrates that contain a nucleotide diphosphate linked to another moiety X [PMID: 8810257, PMID: 16378245]. These substrates include nucleoside triphosphates, nucleotide sugars, dinucleoside polyphosphates, dinucleotide coenzymes and capped RNAs. In some cases, phosphohydrolase activity has been observed with nucleoside diphopshates and some non-nucletoide substrates. These enzymes posses an almost universally conserved, charateristic twenty-three-amino acid motif, Gx(5)Ex(5)[UA]xREx(2)EExGU (where U is an aliphatic, hydrophobic amino acid residue), necessary for catalytic activity. Some members of this family protect cells by degrading potentially mutagenic oxidised nucleotides, while others control the levels of metabolic intermediates and signalling compounds.

This entry represents a number of proteins which contain the characteristic Nudix domain. One of the characterised protein in this entry, PCD1, is a peroxisomal coenzyme A (CoA) diphosphatase catalysing the cleavage of coenzyme A into ADP and phosphopantetheine, with a strong preference for oxidised CoA disulphide as its substrate [PMID: 10922370]. PCD1 may function, therefore, to maintain the capacity for beta-oxidation of fatty acids. It has also been shown to degrade oxo-dGTP and so may also be involved in protecting the cell from mutagenic oxidised nucleotides [PMID: 15475388].

GO terms

Biological Process

GO:0009132 nucleoside diphosphate metabolic process

Molecular Function

GO:0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
GO:0000287 magnesium ion binding
GO:0030145 manganese ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns