ID N6VJT5_9RHIZ Unreviewed; 214 AA. AC N6VJT5; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 13-NOV-2013, entry version 4. DE RecName: Full=Non-canonical purine NTP pyrophosphatase; DE EC=3.6.1.19; DE AltName: Full=Non-standard purine NTP pyrophosphatase; DE AltName: Full=Nucleoside-triphosphate diphosphatase; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase; GN ORFNames=m02_00460; OS Bartonella bovis m02. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=1094492; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M02; RX PubMed=23555299; 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 RT hold the keys to the explosive radiation of the emerging pathogen RT bartonella."; RL PLoS Genet. 9:E1003393-E1003393(2013). CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine CC nucleotides such as XTP and ITP/dITP to their respective CC monophosphate derivatives. Might exclude non-canonical purines CC from DNA precursor pool, thus preventing their incorporation into CC DNA and avoiding chromosomal lesions (By similarity). CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. CC -!- COFACTOR: Binds 1 divalent metal cation ion per subunit; can use CC either magnesium or manganese (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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 EnsemblBacteria; ENN94120; ENN94120; m02_00460. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro. DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1; -. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR020922; NTPase. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding. FT REGION 13 18 Substrate binding (By similarity). FT REGION 74 75 Substrate binding (By similarity). FT METAL 74 74 Magnesium or manganese (By similarity). FT BINDING 166 166 Substrate (By similarity). FT BINDING 186 186 Substrate (By similarity). FT BINDING 200 200 Substrate (By similarity). 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 //