NCPP_YERPS
ID NCPP_YERPS Reviewed; 180 AA.
AC Q66EU4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=YPTB0597;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19837.1; -; Genomic_DNA.
DR RefSeq; WP_011191695.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66EU4; -.
DR SMR; Q66EU4; -.
DR EnsemblBacteria; CAH19837; CAH19837; YPTB0597.
DR GeneID; 66842982; -.
DR KEGG; ypo:BZ17_1963; -.
DR KEGG; yps:YPTB0597; -.
DR PATRIC; fig|273123.14.peg.2088; -.
DR OMA; ADYWVGI; -.
DR Proteomes; UP000001011; 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 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..180
FT /note="Inosine/xanthosine triphosphatase"
FT /id="PRO_0000156356"
FT BINDING 8..13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00648"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00648"
FT BINDING 68..69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00648"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00648"
SQ SEQUENCE 180 AA; 19709 MW; 72CE88BCC9E16D93 CRC64;
MYHVIAATTN PAKINAITLA FDDVYGPGQY RIEGVNVDSG VPLQPIGSTE TRIGARQRVK
NARQVRPEAD FWVGIEAGIE DNMTFAWMVI EHLQARGESR SASLMLPDII LQGIRQGREL
GDEMAVLSGI SNVKQQGGAI GIFTQGKLTR TSVYHQALLL ALVPFHNEIY QRPSPSKPAI
