(data stored in SCRATCH3701 zone)

SWISSPROT: NCPP_VIBVY

ID   NCPP_VIBVY              Reviewed;         183 AA.
AC   Q7MNK7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 85.
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.- {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=VV0708;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; Evidence={ECO:0000255|HAMAP-
CC         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; Evidence={ECO:0000255|HAMAP-
CC         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}.
DR   EMBL; BA000037; BAC93472.1; -; Genomic_DNA.
DR   SMR; Q7MNK7; -.
DR   STRING; 672.VV93_v1c06450; -.
DR   EnsemblBacteria; BAC93472; BAC93472; BAC93472.
DR   KEGG; vvy:VV0708; -.
DR   HOGENOM; HOG000098033; -.
DR   KO; K01529; -.
DR   OMA; PFHNPVY; -.
DR   BioCyc; VVUL196600:GJ9W-728-MONOMER; -.
DR   Proteomes; UP000002675; Chromosome I.
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;
DR   PRODOM; Q7MNK7.
DR   SWISS-2DPAGE; Q7MNK7.
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..183
FT                   /note="Inosine/xanthosine triphosphatase"
FT                   /id="PRO_0000156354"
FT   REGION          75..76
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00648"
FT   METAL           75
FT                   /note="Manganese or magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00648"
SQ   SEQUENCE   183 AA;  19654 MW;  AE4556C452051B5E CRC64;
     MSKKIMATQK VIIASLNPAK ITAVESAFTS AFPDGTFEFV GVNVPSEVAD QPMSDSETHL
     GALNRVRNAK ACRADGAFYV GLEAGIDGNV TFAWMVIESH THRGESRSAS LMLPPNVIAK
     LPNANELGDV MDEVFGTENI KQKGGAISLL TQNQLTRSSV YHQALILALI PFTNPEHFPA
     NLS
//

If you have problems or comments...

PBIL Back to PBIL home page