ID   DUT_PBCV1               Reviewed;         141 AA.
AC   O41033;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   OrderedLocusNames=A551L;
OS   Paramecium bursaria Chlorella virus 1 (PBCV-1).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Chlorovirus.
OX   NCBI_TaxID=10506;
OH   NCBI_TaxID=114055; Chlorella.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9356347; DOI=10.1006/viro.1997.8805;
RA   Li Y., Lu Z., Sun L., Ropp S., Kutish G.F., Rock D.L., van Etten J.L.;
RT   "Analysis of 74 kb of DNA located at the right end of the 330-kb chlorella
RT   virus PBCV-1 genome.";
RL   Virology 237:360-377(1997).
CC   -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces
CC       dUMP, the immediate precursor of thymidine nucleotides and it decreases
CC       the intracellular concentration of dUTP so that uracil cannot be
CC       incorporated into DNA. {ECO:0000250}.
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   -!- 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   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; JF411744; AAC96912.1; -; Genomic_DNA.
DR   PIR; T18053; T18053.
DR   RefSeq; NP_048907.1; NC_000852.5.
DR   SMR; O41033; -.
DR   GeneID; 918013; -.
DR   KEGG; vg:918013; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000000862; Genome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..141
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182969"
SQ   SEQUENCE   141 AA;  14879 MW;  3D0734C9C9BD70B8 CRC64;
     MSSLLVKKLV ESATTPMRGS EGAAGYDISS VEDVVVPAMG RIAVSTGISI RVPNGTYGRI
     APRSGLAYKY GIDVLAGVID SDYRGELKAI LYNTTERDYI IKKGDRIAQL ILEQIVTPDV
     AVVLELEDTA RGGGGFGSTG I