ID N6VJT5_9HYPH Unreviewed; 214 AA. AC N6VJT5; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 19-JAN-2022, entry version 42. DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_01405}; GN ORFNames=m02_00460 {ECO:0000313|EMBL:ENN94120.1}; OS Bartonella bovis m02. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=1094492 {ECO:0000313|EMBL:ENN94120.1, ECO:0000313|Proteomes:UP000014026}; RN [1] {ECO:0000313|EMBL:ENN94120.1, ECO:0000313|Proteomes:UP000014026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=m02 {ECO:0000313|Proteomes:UP000014026}; RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393; RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C., RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.; RT "A gene transfer agent and a dynamic repertoire of secretion systems hold RT the keys to the explosive radiation of the emerging pathogen Bartonella."; RL PLoS Genet. 9:E1003393-E1003393(2013). 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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01405}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|RuleBase:RU003781}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01405}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ENN94120.1}. 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; AGWB01000001; ENN94120.1; -; Genomic_DNA. DR RefSeq; WP_010701874.1; NZ_KB915624.1. DR STRING; 1094492.m02_00460; -. DR EnsemblBacteria; ENN94120; ENN94120; m02_00460. DR PATRIC; fig|1094492.3.peg.52; -. DR HOGENOM; CLU_082080_0_0_5; -. DR Proteomes; UP000014026; Unassembled WGS sequence. DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:RHEA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0034404; P:nucleobase-containing small molecule biosynthetic process; IEA:UniProt. 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; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01405}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01405}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01405}; KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP- KW Rule:MF_01405}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01405}. FT REGION 13..18 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT REGION 163..166 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT REGION 199..200 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT ACT_SITE 74 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT METAL 74 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 75 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" FT BINDING 186 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405" SQ SEQUENCE 214 AA; 23822 MW; C954FC206F13393C CRC64; MRRIVNKKLV IATHNTGKLH EINALIAPFG LTTLSAKELS LPEPKETGTT FEENAYIKAF AAAKTTQLPA LSDDSGLEID ALGGAPGVYT ADWAIQPNGT YNFLKAMQKI EDELQKIGAL EKSQRKCRFI SVICVAWPNG YADYFRGSIE GTFIWPPRGD KGFGFDPIFL PDGYENTFGE MSTEQKHGWK LNDKTPLSHR SRAFKLFVEN FLVS //