NUDI_ECO45
ID NUDI_ECO45 Reviewed; 141 AA.
AC B7MG18;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Nucleoside triphosphatase NudI {ECO:0000255|HAMAP-Rule:MF_01846};
DE EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=Nucleotide diphosphatase NudI {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=Pyrimidine deoxynucleoside triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=dCTP diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
DE EC=3.6.1.12 {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=dTTP diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=dUTP diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_01846};
GN Name=nudI {ECO:0000255|HAMAP-Rule:MF_01846}; OrderedLocusNames=ECS88_2400;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates, with a
CC preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and
CC dCTP). {ECO:0000255|HAMAP-Rule:MF_01846}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dCTP + H2O = dCMP + diphosphate + H(+); Xref=Rhea:RHEA:22636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57566, ChEBI:CHEBI:61481; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dCTP + H2O = dCMP + diphosphate + H(+); Xref=Rhea:RHEA:22636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57566, ChEBI:CHEBI:61481; EC=3.6.1.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01846}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01846}.
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DR EMBL; CU928161; CAR03680.1; -; Genomic_DNA.
DR RefSeq; WP_001249884.1; NC_011742.1.
DR AlphaFoldDB; B7MG18; -.
DR SMR; B7MG18; -.
DR EnsemblBacteria; CAR03680; CAR03680; ECS88_2400.
DR GeneID; 58461873; -.
DR KEGG; ecz:ECS88_2400; -.
DR HOGENOM; CLU_037162_31_0_6; -.
DR OMA; RTTKWRG; -.
DR Proteomes; UP000000747; Chromosome.
DR GO; GO:0047840; F:dCTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR HAMAP; MF_01846; Nudix_NudI; 1.
DR InterPro; IPR023781; Nucleoside_triphosphatase_NudI.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium.
FT CHAIN 1..141
FT /note="Nucleoside triphosphatase NudI"
FT /id="PRO_1000188477"
FT DOMAIN 1..141
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01846"
FT MOTIF 38..59
FT /note="Nudix box"
SQ SEQUENCE 141 AA; 16371 MW; 71BF110D627B42EE CRC64;
MRQRTIVCPL IQNDGAYLLC KMADDRGVFP GQWALSGGGV EPGERIEEAL RREIREELGE
QLLLTEITPW TFSDDIRTKT YADGRKEEIY MIYLIFDCVS ANREVKINEE FQDYAWVKPE
DLVHYDLNVA TRKTLRLKGL L
