ID N6VJT5_9RHIZ Unreviewed; 214 AA. AC N6VJT5; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 06-JUL-2016, entry version 22. DE RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00020486}; DE EC=3.6.1.19 {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00020468}; 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}; GN ORFNames=m02_00460 {ECO:0000313|EMBL:ENN94120.1}; OS Bartonella bovis m02. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; 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 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. {ECO:0000256|HAMAP- CC Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00020483}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01405}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01405}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00608136}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00020467}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP- CC Rule:MF_01405, ECO:0000256|RuleBase:RU003781, CC ECO:0000256|SAAS:SAAS00542593}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; ENN94120; ENN94120; m02_00460. DR Proteomes; UP000014026; Unassembled WGS sequence. 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 Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR020922; NTPase. 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 Complete proteome {ECO:0000313|Proteomes:UP000014026}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00425982}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425988}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00426004}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425941}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425996}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425966}. FT REGION 13 18 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 74 75 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT METAL 74 74 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 166 166 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 186 186 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01405}. FT BINDING 200 200 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //