ID   N6VJT5_9RHIZ            Unreviewed;       214 AA.
AC   N6VJT5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   03-SEP-2014, entry version 9.
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; 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 (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.
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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   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   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
FT                                similarity){EA12}.
FT   BINDING     166    166       Substrate (By similarity){EA12}.
FT   BINDING     186    186       Substrate (By similarity){EA12}.
FT   BINDING     200    200       Substrate (By similarity){EA12}.
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
//