ID IXTPA_CAMJR Reviewed; 200 AA. AC Q5HT36; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 02-SEP-2026, entry version 97. 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=CJE1566; OS Campylobacter jejuni (strain RM1221). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=195099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM1221; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms from RT the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(2005). 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; CP000025; AAW36001.1; -; Genomic_DNA. DR RefSeq; WP_002855675.1; NC_003912.7. DR AlphaFoldDB; Q5HT36; -. DR SMR; Q5HT36; -. DR KEGG; cjr:CJE1566; -. 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_0000178146" 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; 22349 MW; 1E82869A8EAC8BA1 CRC64; MKIILATSNK HKVLELKEIL KDFEIYAFDE VLMPFEIEEN GKTFKENALI KARAVFNALD EKQKKDFIAL SDDSGICVDV LEGNPGIYSA RFSGKGDDKS NRDKLVNEMI KKGFKQSKAH YVAAIAMVGL MGEFSTHGTM HGKVIDTEKG ENGFGYDSLF IPKGFDKTLA QLSVDEKNNI SHRFKALELA KIILKILNKG //