NUDI_ECOLC
ID NUDI_ECOLC Reviewed; 141 AA.
AC B1IXT6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=EcolC_1398;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA77062.1; -; Genomic_DNA.
DR RefSeq; WP_001300564.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IXT6; -.
DR SMR; B1IXT6; -.
DR KEGG; ecl:EcolC_1398; -.
DR HOGENOM; CLU_037162_31_0_6; -.
DR OMA; RTTKWRG; -.
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_0000342124"
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; 6AD2A51D276F13AB CRC64;
MRQRTIVCPL IQNDGAYLLC KMADDRGVFP GQWAISGGGV EPGERIEEAL RREIREELGE
QLLLTEITPW TFSDDIRTKT YADGRKEEIY MIYLIFDCVS ANREVKINEE FQDYAWVKPE
DLVHYDLNVA TRKTLRLKGL L
