ID IXTPA_CAMJ8 Reviewed; 200 AA. AC A8FN54; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 02-SEP-2026, entry version 86. DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE EC=3.6.1.66 {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_01405}; GN OrderedLocusNames=C8J_1293; OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / OS NCTC 11828). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=407148; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=81116 / NCTC 11828; RX PubMed=17873037; DOI=10.1128/jb.01404-07; RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., RA van Vliet A.H.M.; RT "The complete genome sequence of Campylobacter jejuni strain 81116 RT (NCTC11828)."; RL J. Bacteriol. 189:8402-8403(2007). CC -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside CC triphosphates to their monophosphate derivatives, with a high CC preference for the non-canonical purine nucleotides XTP (xanthosine CC triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to CC function as a house-cleaning enzyme that removes non-canonical purine CC nucleotides from the nucleotide pool, thus preventing their CC incorporation into DNA/RNA and avoiding chromosomal lesions. CC {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: CC Reaction=XTP + H2O = XMP + diphosphate + H(+); Xref=Rhea:RHEA:28610, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.66; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.66; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ITP + H2O = IMP + diphosphate + H(+); Xref=Rhea:RHEA:29399, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.66; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01405}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP- CC Rule:MF_01405}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000814; ABV52891.1; -; Genomic_DNA. DR RefSeq; WP_002866708.1; NC_009839.1. DR AlphaFoldDB; A8FN54; -. DR SMR; A8FN54; -. DR KEGG; cju:C8J_1293; -. DR HOGENOM; CLU_082080_0_2_7; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro. DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00515; HAM1; 1. DR FunFam; 3.90.950.10:FF:000001; dITP/XTP pyrophosphatase; 1. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR020922; dITP/XTP_pyrophosphatase. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR002637; RdgB/HAM1. DR NCBIfam; TIGR00042; RdgB/HAM1 family non-canonical purine NTP pyrophosphatase; 1. DR PANTHER; PTHR11067:SF9; INOSINE TRIPHOSPHATE PYROPHOSPHATASE; 1. DR PANTHER; PTHR11067; INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; ITPase-like; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding. FT CHAIN 1..200 FT /note="dITP/XTP pyrophosphatase" FT /id="PRO_1000073507" FT ACT_SITE 73 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 7..12 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 38 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 73 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 154..157 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 182..183 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" SQ SEQUENCE 200 AA; 22421 MW; EEF3029AF5BB51DC CRC64; MKIILATSNK HKVLELKEIL KDFEIYAFDE VLMPFEIEEN GKTFKENALI KARAVFNALD EKQKKDFIAL SDDSGICVDV LEGNPGIYSA RFSDKGDDKS NRDKLVNEMI KKGFNQSRAH YVAAIAMVGL MGEFSTHGTM HGKVIDTEKG ENGFGYDSLF IPKGFDKTLA QLSVDEKNNI SHRFKALELA KIILKILNKG //