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NCPP_KLEAE
ID   NCPP_KLEAE              Reviewed;          54 AA.
AC   P39430;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Inosine/xanthosine triphosphatase {ECO:0000250|UniProtKB:P39411};
DE            Short=ITPase/XTPase {ECO:0000250|UniProtKB:P39411};
DE            EC=3.6.1.73 {ECO:0000250|UniProtKB:P39411};
DE   AltName: Full=Non-canonical purine NTP phosphatase {ECO:0000250|UniProtKB:P39411};
DE   AltName: Full=Non-standard purine NTP phosphatase {ECO:0000250|UniProtKB:P39411};
DE   AltName: Full=Nucleoside-triphosphate phosphatase {ECO:0000250|UniProtKB:P39411};
DE            Short=NTPase {ECO:0000250|UniProtKB:P39411};
DE   Flags: Fragment;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8208606; DOI=10.1093/nar/22.10.1821;
RA   Arvidson D.N., Arvidson C.G., Lawson C.L., Miner J., Adams C.,
RA   Youderian P.;
RT   "The tryptophan repressor sequence is highly conserved among the
RT   Enterobacteriaceae.";
RL   Nucleic Acids Res. 22:1821-1829(1994).
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:0000250|UniProtKB:P39411}.
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:0000250|UniProtKB:P39411};
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:0000250|UniProtKB:P39411};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P39411};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P39411};
CC       Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC       or Mn(2+). {ECO:0000250|UniProtKB:P39411};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P39411}.
CC   -!- SIMILARITY: Belongs to the YjjX NTPase family. {ECO:0000305}.
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DR   EMBL; L26582; AAC36893.1; -; Unassigned_DNA.
DR   PIR; S45255; S45255.
DR   AlphaFoldDB; P39430; -.
DR   SMR; P39430; -.
DR   STRING; 548.EAG7_03371; -.
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   InterPro; IPR029001; ITPase-like_fam.
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.
FT   CHAIN           <1..54
FT                   /note="Inosine/xanthosine triphosphatase"
FT                   /id="PRO_0000156340"
FT   NON_TER         1
SQ   SEQUENCE   54 AA;  5794 MW;  23A9E94ED9FA0FC5 CRC64;
     EALGPVMSQH TGIDQIGRKE GAIGVFTAGK LTRSSVYHQA VVLALSPFHN AIYR
 
 
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