NUDI_ECOLI
ID NUDI_ECOLI Reviewed; 141 AA.
AC P52006; P77305;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Nucleoside triphosphatase NudI {ECO:0000303|PubMed:16766526};
DE EC=3.6.1.9 {ECO:0000269|PubMed:16766526};
DE AltName: Full=Nucleotide diphosphatase NudI {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=Pyrimidine deoxynucleoside triphosphate diphosphatase {ECO:0000305};
DE AltName: Full=dCTP diphosphatase;
DE EC=3.6.1.12 {ECO:0000269|PubMed:16766526};
DE AltName: Full=dTTP diphosphatase;
DE EC=3.6.1.- {ECO:0000269|PubMed:16766526};
DE AltName: Full=dUTP diphosphatase;
DE EC=3.6.1.23 {ECO:0000269|PubMed:16766526};
GN Name=nudI; Synonyms=yfaO; OrderedLocusNames=b2251, JW2245;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 61-141.
RC STRAIN=K12;
RA Guzzo A., Macintyre G., Diorio C., Salmon K., Dubow M.S.;
RT "Identification, sequencing and characterization of an aluminium-inducible
RT Escherichia coli gene.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16766526; DOI=10.1074/jbc.m603407200;
RA Xu W., Dunn C.A., O'Handley S.F., Smith D.L., Bessman M.J.;
RT "Three new Nudix hydrolases from Escherichia coli.";
RL J. Biol. Chem. 281:22794-22798(2006).
RN [6]
RP CRYSTALLIZATION.
RC STRAIN=K1;
RX PubMed=17768363; DOI=10.1107/s1744309107040316;
RA Jung J., Ahn Y.-J., Kang L.-W.;
RT "Overexpression, crystallization and preliminary X-ray crystallographic
RT analysis of Nudix hydrolase Orf141 from Escherichia coli K-1.";
RL Acta Crystallogr. F 63:812-815(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates, with a
CC preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and
CC dCTP). {ECO:0000269|PubMed:16766526}.
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:0000269|PubMed:16766526};
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:0000269|PubMed:16766526};
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:0000269|PubMed:16766526};
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:0000269|PubMed:16766526};
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:0000269|PubMed:16766526};
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:0000269|PubMed:16766526};
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:0000269|PubMed:16766526};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16766526};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for dUTP {ECO:0000269|PubMed:16766526};
CC KM=1.3 mM for dTTP {ECO:0000269|PubMed:16766526};
CC Vmax=81 umol/min/mg enzyme with dUTP as substrate
CC {ECO:0000269|PubMed:16766526};
CC Vmax=56 umol/min/mg enzyme with dTTP as substrate
CC {ECO:0000269|PubMed:16766526};
CC Note=kcat is 21 sec(-1) with dUTP as substrate, and 15 sec(-1) with
CC dTTP as substrate. {ECO:0000269|PubMed:16766526};
CC pH dependence:
CC Optimum pH is about 8.5. {ECO:0000269|PubMed:16766526};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16766526}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudI subfamily.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC75311.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16074.1; -; Genomic_DNA.
DR EMBL; X83874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A64996; A64996.
DR RefSeq; NP_416754.1; NC_000913.3.
DR RefSeq; WP_001300564.1; NZ_LN832404.1.
DR AlphaFoldDB; P52006; -.
DR SMR; P52006; -.
DR BioGRID; 4261215; 13.
DR IntAct; P52006; 7.
DR STRING; 511145.b2251; -.
DR jPOST; P52006; -.
DR PaxDb; P52006; -.
DR PRIDE; P52006; -.
DR EnsemblBacteria; AAC75311; AAC75311; b2251.
DR EnsemblBacteria; BAA16074; BAA16074; BAA16074.
DR GeneID; 946740; -.
DR KEGG; ecj:JW2245; -.
DR KEGG; eco:b2251; -.
DR PATRIC; fig|511145.12.peg.2343; -.
DR EchoBASE; EB3060; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_037162_31_0_6; -.
DR InParanoid; P52006; -.
DR OMA; RTTKWRG; -.
DR PhylomeDB; P52006; -.
DR BioCyc; EcoCyc:G7164-MON; -.
DR BioCyc; MetaCyc:G7164-MON; -.
DR PRO; PR:P52006; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047840; F:dCTP diphosphatase activity; IDA:EcoCyc.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IDA:EcoCyc.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IDA:EcoCyc.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IBA:GO_Central.
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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..141
FT /note="Nucleoside triphosphatase NudI"
FT /id="PRO_0000057139"
FT DOMAIN 1..141
FT /note="Nudix hydrolase"
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
