ID   NCPP_ALIFM              Reviewed;         170 AA.
AC   B5FAQ4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Inosine/xanthosine triphosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE            Short=ITPase/XTPase {ECO:0000255|HAMAP-Rule:MF_00648};
DE            EC=3.6.1.73 {ECO:0000255|HAMAP-Rule:MF_00648};
DE   AltName: Full=Non-canonical purine NTP phosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE   AltName: Full=Non-standard purine NTP phosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE   AltName: Full=Nucleoside-triphosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE            Short=NTPase {ECO:0000255|HAMAP-Rule:MF_00648};
GN   OrderedLocusNames=VFMJ11_0572;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphatase that hydrolyzes non-canonical purine nucleotides
CC       such as XTP and ITP to their respective diphosphate derivatives.
CC       Probably excludes non-canonical purines from DNA/RNA precursor pool,
CC       thus preventing their incorporation into DNA/RNA and avoiding
CC       chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_00648}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + XTP = H(+) + phosphate + XDP; Xref=Rhea:RHEA:28406,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:59884, ChEBI:CHEBI:61314; EC=3.6.1.73;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + ITP = H(+) + IDP + phosphate; Xref=Rhea:RHEA:28330,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58280, ChEBI:CHEBI:61402; EC=3.6.1.73;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC       Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC       or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00648};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00648}.
CC   -!- SIMILARITY: Belongs to the YjjX NTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00648}.
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DR   EMBL; CP001139; ACH67147.1; -; Genomic_DNA.
DR   RefSeq; WP_012534229.1; NC_011184.1.
DR   AlphaFoldDB; B5FAQ4; -.
DR   SMR; B5FAQ4; -.
DR   EnsemblBacteria; ACH67147; ACH67147; VFMJ11_0572.
DR   KEGG; vfm:VFMJ11_0572; -.
DR   HOGENOM; CLU_087417_1_0_6; -.
DR   OMA; ADYWVGI; -.
DR   Proteomes; UP000001857; Chromosome I.
DR   GO; GO:0103023; F:ITPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_00648; Non_canon_purine_NTPase_YjjX; 1.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR002786; Non_canon_purine_NTPase.
DR   InterPro; IPR026533; NTPase/PRRC1.
DR   Pfam; PF01931; NTPase_I-T; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00258; TIGR00258; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding.
FT   CHAIN           1..170
FT                   /note="Inosine/xanthosine triphosphatase"
FT                   /id="PRO_1000130951"
SQ   SEQUENCE   170 AA;  18444 MW;  72E15498E9442BB5 CRC64;
     MKVIIASQNP AKIAAVESAF NLAFPNDTFS FEGVSVKSGV PDQPMSCEET KQGAINRVNN
     AKIKLPNCDY YVGLEAGIEG NSTFAWMIID NGLTVGESRS SSLPLPPQVI DEVKKGKELG
     DVMDEQFNTD NIKQKGGAIG LLTNNLLTRT SVYQQALILA LIPFLHPTRF