NCPP_ECOLI
ID NCPP_ECOLI Reviewed; 170 AA.
AC P39411; Q2M5S3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Inosine/xanthosine triphosphatase {ECO:0000255|HAMAP-Rule:MF_00648, ECO:0000303|PubMed:16216582};
DE Short=ITPase/XTPase {ECO:0000255|HAMAP-Rule:MF_00648, ECO:0000303|PubMed:16216582};
DE EC=3.6.1.73 {ECO:0000255|HAMAP-Rule:MF_00648, ECO:0000269|PubMed:16216582};
DE AltName: Full=Non-canonical purine NTP phosphatase;
DE AltName: Full=Non-standard purine NTP phosphatase;
DE AltName: Full=Nucleoside-triphosphate phosphatase;
DE Short=NTPase;
GN Name=yjjX; OrderedLocusNames=b4394, JW5801;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-170.
RX PubMed=7001368; DOI=10.1093/nar/8.7.1551;
RA Singleton C.K., Roeder W.D., Bogosian G., Somerville R.L., Weith H.L.;
RT "DNA sequence of the E. coli trpR gene and prediction of the amino acid
RT sequence of Trp repressor.";
RL Nucleic Acids Res. 8:1551-1560(1980).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-170.
RX PubMed=7841459; DOI=10.3109/10425179409010185;
RA Skrypka I., Somerville R.L.;
RT "Nucleotide sequence of the Salmonella typhimurium trpR gene.";
RL DNA Seq. 4:355-360(1994).
RN [6]
RP ANTIBIOTIC RESISTANCE.
RX PubMed=15292217; DOI=10.1074/jbc.m404284200;
RA Lawhorn B.G., Gerdes S.Y., Begley T.P.;
RT "A genetic screen for the identification of thiamin metabolic genes.";
RL J. Biol. Chem. 279:43555-43559(2004).
RN [7] {ECO:0007744|PDB:1U5W}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=16216582; DOI=10.1016/j.str.2005.07.007;
RA Zheng J., Singh V.K., Jia Z.;
RT "Identification of an ITPase/XTPase in Escherichia coli by structural and
RT biochemical analysis.";
RL Structure 13:1511-1520(2005).
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. ITP and XTP are the best substrates, followed by
CC GDP and dITP. Is not active on dATP and dGTP, and exhibits no
CC phosphatase activity toward pyrimidines (CTP, TTP, UTP, dCTP, and dTTP)
CC (PubMed:16216582). Seems also implicated in the resistance against the
CC thiamine metabolism inhibitors bacimethrin and CF3-HMP
CC (PubMed:15292217). {ECO:0000269|PubMed:16216582,
CC ECO:0000305|PubMed:15292217}.
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 ECO:0000269|PubMed:16216582};
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 ECO:0000269|PubMed:16216582};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16216582};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16216582};
CC Note=Binds 1 divalent cation per subunit. Activity is maximal in the
CC presence of Mg(2+), while Mn(2+) decreases the activity by 20%.
CC {ECO:0000269|PubMed:16216582};
CC -!- ACTIVITY REGULATION: Competitively inhibited by ATP, GTP and TTP.
CC {ECO:0000269|PubMed:16216582}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for ITP {ECO:0000269|PubMed:16216582};
CC KM=1.17 mM for XTP {ECO:0000269|PubMed:16216582};
CC KM=0.58 mM for GDP {ECO:0000269|PubMed:16216582};
CC KM=4.51 mM for dITP {ECO:0000269|PubMed:16216582};
CC KM=1.24 mM for GTP {ECO:0000269|PubMed:16216582};
CC KM=0.91 mM for magnesium ions {ECO:0000269|PubMed:16216582};
CC KM=1.39 mM for manganese ions {ECO:0000269|PubMed:16216582};
CC KM=2.44 mM for zinc ions {ECO:0000269|PubMed:16216582};
CC Vmax=1720 umol/min/mg enzyme with ITP as substrate
CC {ECO:0000269|PubMed:16216582};
CC Vmax=7876 umol/min/mg enzyme with XTP as substrate
CC {ECO:0000269|PubMed:16216582};
CC Vmax=358 umol/min/mg enzyme with GDP as substrate
CC {ECO:0000269|PubMed:16216582};
CC Vmax=1849 umol/min/mg enzyme with dITP as substrate
CC {ECO:0000269|PubMed:16216582};
CC Vmax=67 umol/min/mg enzyme with GTP as substrate
CC {ECO:0000269|PubMed:16216582};
CC Vmax=1264 umol/min/mg enzyme with ITP as substrate and magnesium ions
CC as cofactor (at 25 degrees Celsius and pH 6.75)
CC {ECO:0000269|PubMed:16216582};
CC Vmax=571 umol/min/mg enzyme with ITP as substrate and manganese ions
CC as cofactor (at 25 degrees Celsius and pH 6.75)
CC {ECO:0000269|PubMed:16216582};
CC Vmax=439 umol/min/mg enzyme with ITP as substrate and zinc ions as
CC cofactor (at 25 degrees Celsius and pH 6.75)
CC {ECO:0000269|PubMed:16216582};
CC Note=kcat is 573.3 sec(-1) with ITP as substrate. kcat is 2625 sec(-
CC 1) with XTP as substrate. kcat is 119 sec(-1) with GDP as substrate.
CC kcat is 616.5 sec(-1) with dITP as substrate. kcat is 22.3 sec(-1)
CC with GTP as substrate. {ECO:0000269|PubMed:16216582};
CC pH dependence:
CC Optimum pH is 6.75. {ECO:0000269|PubMed:16216582};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00648,
CC ECO:0000269|PubMed:16216582}.
CC -!- SIMILARITY: Belongs to the YjjX NTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00648, ECO:0000305}.
CC -!- CAUTION: PubMed:7841459 sequence was originally thought to originate
CC from S.typhimurium, but seems to come from an unknown E.coli strain.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97290.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97290.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77347.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78383.1; -; Genomic_DNA.
DR EMBL; J01715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L13768; AAA72135.1; -; Genomic_DNA.
DR PIR; S56618; S56618.
DR RefSeq; NP_418811.2; NC_000913.3.
DR RefSeq; WP_001338221.1; NZ_LN832404.1.
DR PDB; 1U5W; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-170.
DR PDBsum; 1U5W; -.
DR AlphaFoldDB; P39411; -.
DR SMR; P39411; -.
DR BioGRID; 4262781; 5.
DR DIP; DIP-12663N; -.
DR STRING; 511145.b4394; -.
DR jPOST; P39411; -.
DR PaxDb; P39411; -.
DR PRIDE; P39411; -.
DR EnsemblBacteria; AAC77347; AAC77347; b4394.
DR EnsemblBacteria; BAE78383; BAE78383; BAE78383.
DR GeneID; 948919; -.
DR KEGG; ecj:JW5801; -.
DR KEGG; eco:b4394; -.
DR PATRIC; fig|1411691.4.peg.2290; -.
DR EchoBASE; EB2485; -.
DR eggNOG; COG1986; Bacteria.
DR HOGENOM; CLU_087417_1_0_6; -.
DR InParanoid; P39411; -.
DR OMA; ADYWVGI; -.
DR PhylomeDB; P39411; -.
DR BioCyc; EcoCyc:EG12600-MON; -.
DR BioCyc; MetaCyc:EG12600-MON; -.
DR BRENDA; 3.6.1.73; 2026.
DR EvolutionaryTrace; P39411; -.
DR PRO; PR:P39411; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0103023; F:ITPase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:EcoCyc.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006772; P:thiamine metabolic process; EXP:EcoliWiki.
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; Antibiotic resistance; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..170
FT /note="Inosine/xanthosine triphosphatase"
FT /id="PRO_0000156337"
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"
FT CONFLICT 146..152
FT /note="GKLTRAS -> ETHSRH (in Ref. 5; AAA72135)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1U5W"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:1U5W"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1U5W"
FT HELIX 48..65
FT /evidence="ECO:0007829|PDB:1U5W"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:1U5W"
FT STRAND 81..94
FT /evidence="ECO:0007829|PDB:1U5W"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1U5W"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:1U5W"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1U5W"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:1U5W"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1U5W"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:1U5W"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1U5W"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:1U5W"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:1U5W"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1U5W"
SQ SEQUENCE 170 AA; 18213 MW; 60F87FEB6344E597 CRC64;
MHQVVCATTN PAKIQAILQA FHEIFGEGSC HIASVAVESG VPEQPFGSEE TRAGARNRVA
NARRLLPEAD FWVAIEAGID GDSTFSWVVI ENASQRGEAR SATLPLPAVI LEKVREGEAL
GPVMSRYTGI DEIGRKEGAI GVFTAGKLTR ASVYHQAVIL ALSPFHNAVY
