ID IXTPA_COXBU Reviewed; 200 AA. AC Q83FA3; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 104. 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=CBU_0043; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae; OC Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). 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=H2O + XTP = diphosphate + H(+) + XMP; 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=H2O + ITP = diphosphate + H(+) + IMP; 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; AE016828; AAO89612.1; -; Genomic_DNA. DR RefSeq; NP_819098.1; NC_002971.3. DR RefSeq; WP_005769347.1; NC_002971.4. DR PDB; 3TQU; X-ray; 1.90 A; A/B/C/D=1-200. DR PDBsum; 3TQU; -. DR AlphaFoldDB; Q83FA3; -. DR SMR; Q83FA3; -. DR STRING; 227377.CBU_0043; -. DR DNASU; 1207905; -. DR EnsemblBacteria; AAO89612; AAO89612; CBU_0043. DR GeneID; 1207905; -. DR KEGG; cbu:CBU_0043; -. DR PATRIC; fig|227377.7.peg.44; -. DR eggNOG; COG0127; Bacteria. DR HOGENOM; CLU_082080_0_3_6; -. DR OrthoDB; 9807456at2; -. DR Proteomes; UP000002671; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047429; F:nucleoside triphosphate diphosphatase activity; IBA:GO_Central. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro. DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IBA:GO_Central. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00515; HAM1; 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 1: Evidence at protein level; KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..200 FT /note="dITP/XTP pyrophosphatase" FT /id="PRO_0000178160" FT ACT_SITE 69 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 8..13 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405" FT BINDING 70 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" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:3TQU" FT HELIX 11..20 FT /evidence="ECO:0007829|PDB:3TQU" FT TURN 21..23 FT /evidence="ECO:0007829|PDB:3TQU" FT STRAND 24..30 FT /evidence="ECO:0007829|PDB:3TQU" FT HELIX 31..34 FT /evidence="ECO:0007829|PDB:3TQU" FT HELIX 46..61 FT /evidence="ECO:0007829|PDB:3TQU" FT STRAND 65..74 FT /evidence="ECO:0007829|PDB:3TQU" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:3TQU" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:3TQU" FT TURN 85..89 FT /evidence="ECO:0007829|PDB:3TQU" FT HELIX 95..109 FT /evidence="ECO:0007829|PDB:3TQU" FT STRAND 115..127 FT /evidence="ECO:0007829|PDB:3TQU" FT STRAND 134..144 FT /evidence="ECO:0007829|PDB:3TQU" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:3TQU" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:3TQU" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:3TQU" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:3TQU" FT TURN 169..171 FT /evidence="ECO:0007829|PDB:3TQU" FT HELIX 174..180 FT /evidence="ECO:0007829|PDB:3TQU" FT HELIX 182..196 FT /evidence="ECO:0007829|PDB:3TQU" SQ SEQUENCE 200 AA; 21777 MW; A35DF16EE7025113 CRC64; MLEIVLASQN SSKLAEMQEL LRDLEIKFIP QTEFSVPDIE ETGSTFVENA IIKARHAAKQ TGLPALADDS GLTIAALNSA PGVFSSRYAG KNATDAERIQ KVLEALEAAD DSDRSASFHC VIALMENEND PAPLICHGVW EGEIAREPRG KNGFGYDPIF YVPSHQRTAA ELDPQEKNAI SHRGQALEQL STVLTEAFLV //