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Nucleoside triphosphatase NudI (EC 3.6.1.9) (Nucleotide diphosphatase NudI) (Pyrimidine deoxynucleoside triphosphate diphosphatase) (dCTP diphosphatase) (EC 3.6.1.12) (dTTP diphosphatase) (EC 3.6.1.-) (dUTP diphosphatase) (EC 3.6.1.23)

 NUDI_ECOL6              Reviewed;         141 AA.
Q8FFM5;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
07-JUN-2017, entry version 91.
RecName: Full=Nucleoside triphosphatase NudI {ECO:0000255|HAMAP-Rule:MF_01846};
EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01846};
AltName: Full=Nucleotide diphosphatase NudI {ECO:0000255|HAMAP-Rule:MF_01846};
AltName: Full=Pyrimidine deoxynucleoside triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
AltName: Full=dCTP diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
EC=3.6.1.12 {ECO:0000255|HAMAP-Rule:MF_01846};
AltName: Full=dTTP diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01846};
AltName: Full=dUTP diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_01846};
Name=nudI {ECO:0000255|HAMAP-Rule:MF_01846}; OrderedLocusNames=c2793;
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=199310;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CFT073 / ATCC 700928 / UPEC;
PubMed=12471157; DOI=10.1073/pnas.252529799;
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence
of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
-!- FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates,
with a preference for pyrimidine deoxynucleoside triphosphates
(dUTP, dTTP and dCTP). {ECO:0000255|HAMAP-Rule:MF_01846}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000255|HAMAP-Rule:MF_01846}.
-!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate.
{ECO:0000255|HAMAP-Rule:MF_01846}.
-!- CATALYTIC ACTIVITY: dTTP + H(2)O = dTMP + diphosphate.
{ECO:0000255|HAMAP-Rule:MF_01846}.
-!- CATALYTIC ACTIVITY: dCTP + H(2)O = dCMP + diphosphate.
{ECO:0000255|HAMAP-Rule:MF_01846}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01846}.
-!- SIMILARITY: Belongs to the Nudix hydrolase family. NudI subfamily.
{ECO:0000255|HAMAP-Rule:MF_01846}.
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EMBL; AE014075; AAN81247.1; -; Genomic_DNA.
RefSeq; WP_001249883.1; NC_004431.1.
ProteinModelPortal; Q8FFM5; -.
SMR; Q8FFM5; -.
STRING; 199310.c2793; -.
EnsemblBacteria; AAN81247; AAN81247; c2793.
KEGG; ecc:c2793; -.
eggNOG; ENOG4108RJ7; Bacteria.
eggNOG; COG0494; LUCA.
HOGENOM; HOG000059287; -.
KO; K12944; -.
OMA; RTTKWRG; -.
BioCyc; ECOL199310:C2793-MONOMER; -.
Proteomes; UP000001410; Chromosome.
GO; GO:0047840; F:dCTP diphosphatase activity; IEA:UniProtKB-EC.
GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
HAMAP; MF_01846; Nudix_NudI; 1.
InterPro; IPR023781; Nucleoside_triphosphatase_NudI.
InterPro; IPR020476; Nudix_hydrolase.
InterPro; IPR020084; NUDIX_hydrolase_CS.
InterPro; IPR000086; NUDIX_hydrolase_dom.
InterPro; IPR015797; NUDIX_hydrolase_dom-like.
Pfam; PF00293; NUDIX; 1.
PRINTS; PR00502; NUDIXFAMILY.
SUPFAM; SSF55811; SSF55811; 1.
PROSITE; PS51462; NUDIX; 1.
PROSITE; PS00893; NUDIX_BOX; 1.
3: Inferred from homology;
Complete proteome; Hydrolase; Magnesium.
CHAIN 1 141 Nucleoside triphosphatase NudI.
/FTId=PRO_0000342131.
DOMAIN 1 141 Nudix hydrolase. {ECO:0000255|HAMAP-
Rule:MF_01846}.
MOTIF 38 59 Nudix box.
SEQUENCE 141 AA; 16357 MW; 84BF110D627AE9F4 CRC64;
MRQRTIVCPL IQNDGAYLLC KMADDRGVFP GQWALSGGGV EPGERIEEAL RREIREELGE
QLLLTEITPW TFSDDIRTKT YADGRKEEIY MIYLIFDCVS ANRDVKINEE FQDYAWVKPE
DLVHYDLNVA TRKTLRLKGL L


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