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NCPP_PYRAE
ID   NCPP_PYRAE              Reviewed;         178 AA.
AC   Q8ZUF6;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Probable 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=PAE2808;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64451.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZUF6; -.
DR   SMR; Q8ZUF6; -.
DR   STRING; 178306.PAE2808; -.
DR   EnsemblBacteria; AAL64451; AAL64451; PAE2808.
DR   KEGG; pai:PAE2808; -.
DR   PATRIC; fig|178306.9.peg.2094; -.
DR   eggNOG; arCOG01221; Archaea.
DR   HOGENOM; CLU_087417_0_1_2; -.
DR   InParanoid; Q8ZUF6; -.
DR   OMA; ADYWVGI; -.
DR   Proteomes; UP000002439; Chromosome.
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   GO; GO:0006772; P:thiamine metabolic process; IBA:GO_Central.
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.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..178
FT                   /note="Probable inosine/xanthosine triphosphatase"
FT                   /id="PRO_0000156362"
SQ   SEQUENCE   178 AA;  18870 MW;  F0F18BD23F0A9982 CRC64;
     MIVAVGTKNP NKIRAVEDAY RLFGIPARIV PAPRPLTTPP QPVGLEAVLK GAVERAKAAL
     QAVEKAEHGV GIEAGVVEAG GVHLDITIAA IVDAGGRTTI GFGPAFQIPP PFLSQVLSGV
     EMGAVAEQYF KRPSIGYREG LIGVLTKRRV TRYHLNLAAV AMALTPRLPH NSQLYLKP
 
 
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