NCPP_SALTY
ID NCPP_SALTY Reviewed; 171 AA.
AC P39432;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 122.
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 Name=yjjX; OrderedLocusNames=STM4584;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "The crystal structure of hypothetical upf0244 protein yjjx at resolution
RT 1.68 angstrom.";
RL Submitted (FEB-2009) to the PDB data bank.
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; AE006468; AAL23399.1; -; Genomic_DNA.
DR RefSeq; NP_463440.1; NC_003197.2.
DR RefSeq; WP_000554311.1; NC_003197.2.
DR PDB; 1U14; X-ray; 1.68 A; A=1-171.
DR PDBsum; 1U14; -.
DR AlphaFoldDB; P39432; -.
DR SMR; P39432; -.
DR STRING; 99287.STM4584; -.
DR PaxDb; P39432; -.
DR DNASU; 1256110; -.
DR EnsemblBacteria; AAL23399; AAL23399; STM4584.
DR GeneID; 1256110; -.
DR KEGG; stm:STM4584; -.
DR PATRIC; fig|99287.12.peg.4827; -.
DR HOGENOM; CLU_087417_1_0_6; -.
DR OMA; ADYWVGI; -.
DR PhylomeDB; P39432; -.
DR BioCyc; SENT99287:STM4584-MON; -.
DR EvolutionaryTrace; P39432; -.
DR Proteomes; UP000001014; 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.
DR TIGRFAMs; TIGR00258; TIGR00258; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..171
FT /note="Inosine/xanthosine triphosphatase"
FT /id="PRO_0000156348"
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
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00648"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1U14"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:1U14"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1U14"
FT HELIX 48..65
FT /evidence="ECO:0007829|PDB:1U14"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:1U14"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:1U14"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1U14"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:1U14"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1U14"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:1U14"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1U14"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:1U14"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1U14"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:1U14"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1U14"
SQ SEQUENCE 171 AA; 18519 MW; F7FCA0E10765B416 CRC64;
MHQVISATTN PAKIQAILQA FEEIFGEGSC HITPVAVESG VPEQPFGSEE TRAGARNRVD
NARRLHPQAD FWVAIEAGID DDATFSWVVI DNGVQRGEAR SATLPLPAVI LDRVRQGEAL
GPVMSQYTGI DEIGRKEGAI GVFTAGKLTR SSVYYQAVIL ALSPFHNAVY R
