ID   DUT_HALS3               Reviewed;         165 AA.
AC   B0R858;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_00635};
DE            Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00635};
DE            EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00635};
DE   AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00635};
GN   Name=dut {ECO:0000255|HAMAP-Rule:MF_00635}; OrderedLocusNames=OE_4610R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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:0000255|HAMAP-Rule:MF_00635}.
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_00635};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00635}.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family. Archaeal dUTPase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00635}.
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DR   EMBL; AM774415; CAP14927.1; -; Genomic_DNA.
DR   RefSeq; WP_010903920.1; NC_010364.1.
DR   AlphaFoldDB; B0R858; -.
DR   SMR; B0R858; -.
DR   EnsemblBacteria; CAP14927; CAP14927; OE_4610R.
DR   GeneID; 5953444; -.
DR   GeneID; 62887858; -.
DR   KEGG; hsl:OE_4610R; -.
DR   HOGENOM; CLU_103451_1_0_2; -.
DR   OMA; WDAGYEG; -.
DR   PhylomeDB; B0R858; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   HAMAP; MF_00635; dUTPase_arch; 1.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR023537; dUTPase_archaeal.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotide metabolism.
FT   CHAIN           1..165
FT                   /note="Probable deoxyuridine 5'-triphosphate
FT                   nucleotidohydrolase"
FT                   /id="PRO_1000130718"
FT   REGION          39..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   165 AA;  18118 MW;  AA5039B5964D4F77 CRC64;
     MYERGAFVAD HVEPVADDQI QPNGVDLTVD AVLEQTEPGR IDTDGKTIGD RSPVTPTADE
     DSTDTTVTIQ PGTYILQYAE TITIPENHVG FVYPRSSLMR NSCMLHSAVW DAGYTGRGEG
     LFEVHHEITI ARGARVAQLV LATGDHENTY DGSYQHERTD TRPGE