ID IXTPA_CHLMU Reviewed; 209 AA. AC Q9PJD4; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 04-NOV-2026, entry version 121. 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=TC_0895; OS Chlamydia muridarum (strain MoPn / Nigg). OC Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales; OC Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=243161; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MoPn / Nigg; RX PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., RA Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae RT AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). 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; AE002160; AAF39689.1; -; Genomic_DNA. DR PIR; H81651; H81651. DR RefSeq; WP_010231873.1; NC_002620.2. DR AlphaFoldDB; Q9PJD4; -. DR SMR; Q9PJD4; -. DR GeneID; 1246264; -. DR KEGG; cmu:TC_0895; -. DR eggNOG; COG0127; Bacteria. DR HOGENOM; CLU_082080_0_2_0; -. DR OMA; AAFVCHI; -. DR OrthoDB; 9807456at2; -. DR Proteomes; UP000000800; Chromosome. 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 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; Reference proteome. FT CHAIN 1..209 FT /note="dITP/XTP pyrophosphatase" FT /id="PRO_0000178149" FT ACT_SITE 70 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 70 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 71 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 209 AA; 23383 MW; 4EC73447310682F4 CRC64; MKILIASSHG YKVRETKAFL KKIGEFDIFS LVDYPSYTPP KETGETPEEN AIQKGVFAAQ TFRCWTIADD SMLIIPALGG LPGKLSASFS GEHASDKDHR KKLLEEMLLL ENPIDRSAYF ECCVVLVSPF GKIFKAHASC EGTIVFKERG SSGFGYDPLF SKHDYKQTYA ELPEEIKNQV SHRAKALAKL QPYVEMAFAN HLLARNESL //