ID   DUT_BPT5                Reviewed;         148 AA.
AC   O48500; Q66LT4;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23 {ECO:0000305};
DE   AltName: Full=dUTP pyrophosphatase;
GN   Name=DUT;
GN   ORFNames=T5.131 {ECO:0000312|EMBL:AAS77177.1},
GN   T5p129 {ECO:0000312|EMBL:AAU05268.1};
OS   Escherichia phage T5 (Enterobacteria phage T5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX   NCBI_TaxID=2695836;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
RX   PubMed=8988373; DOI=10.3109/10425179609047573;
RA   Kaliman A.V.;
RT   "Identification of the bacteriophage T5 dUTPase by protein sequence
RT   comparisons.";
RL   DNA Seq. 6:347-350(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT   "Bacteriophage T5 complete genome.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 11303-B5;
RX   PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA   Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA   Hu S.;
RT   "Complete genome sequence of bacteriophage T5.";
RL   Virology 332:45-65(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St0 deletion mutant;
RX   PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA   Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA   Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA   Boulanger P.;
RT   "Insights into bacteriophage T5 structure from analysis of its
RT   morphogenesis genes and protein components.";
RL   J. Virol. 88:1162-1174(2014).
RN   [5]
RP   IDENTIFICATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=381286; DOI=10.1016/s0021-9258(18)35977-5;
RA   Warner H.R., Thompson R.B., Mozer T.J., Duncan B.K.;
RT   "The properties of a bacteriophage T5 mutant unable to induce deoxyuridine
RT   5'-triphosphate nucleotidohydrolase. Synthesis of uracil-containing T5
RT   deoxyribonucleic acid.";
RL   J. Biol. Chem. 254:7534-7539(1979).
CC   -!- FUNCTION: This enzyme decreases the intracellular concentration of dUTP
CC       so that uracil cannot be incorporated into viral progeny DNA. This
CC       activity is sufficient to exclude uracil from the DNA during phage
CC       replication. In the case of dUTPase mutant phages, the host dUTPase
CC       activity is not sufficient to exclude uracil from T5 DNA and uracil are
CC       incorporated, leading to decreased phage viability.
CC       {ECO:0000269|PubMed:381286}.
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:381286};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000305|PubMed:15661140}.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; AY543070; AAS77177.1; -; Genomic_DNA.
DR   EMBL; AY692264; AAU05268.1; -; Genomic_DNA.
DR   EMBL; AY587007; AAX12059.1; -; Genomic_DNA.
DR   RefSeq; YP_006959.1; NC_005859.1.
DR   SMR; O48500; -.
DR   GeneID; 2777637; -.
DR   KEGG; vg:2777637; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000002107; Genome.
DR   Proteomes; UP000002141; Genome.
DR   Proteomes; UP000002503; Genome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   InterPro; IPR008181; dUTPase.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   PANTHER; PTHR11241; PTHR11241; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR00576; dut; 1.
PE   1: Evidence at protein level;
KW   Early protein; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..148
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182970"
SQ   SEQUENCE   148 AA;  16204 MW;  4BD56DB1456EF430 CRC64;
     MIKIKLTHPD CMPKIGSEDA AGMDLRAFFG TNPAADLRAI APGKSLMIDT GVAVEIPRGW
     FGLVVPRSSL GKRHLMIANT AGVIDSDYRG TIKMNLYNYG SEMQTLENFE RLCQLVVLPH
     YSTHNFKIVD ELEETIRGEG GFGSSGSK