NCPP_ENTCL
ID NCPP_ENTCL Reviewed; 67 AA.
AC P39431;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 65.
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 Enterobacter cloacae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
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; L26583; AAA20184.1; -; Unassigned_DNA.
DR PIR; S45258; S45258.
DR AlphaFoldDB; P39431; -.
DR SMR; P39431; -.
DR STRING; 1399774.JDWH01000001_gene2464; -.
DR eggNOG; COG1986; Bacteria.
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..67
FT /note="Inosine/xanthosine triphosphatase"
FT /id="PRO_0000156341"
FT NON_TER 1
SQ SEQUENCE 67 AA; 7278 MW; 926E6E8DDB375D03 CRC64;
PLPEIILNKV REGEALGPVM SQYTGIDEIG RKEGAIGVFT KGVLTRSGVY HQAVVLALSP
FHNAIYR
