ID   DUT_HALSA               Reviewed;         165 AA.
AC   Q9HMF3;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=VNG_2570G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG20618.1; -; Genomic_DNA.
DR   PIR; F84406; F84406.
DR   RefSeq; WP_010903920.1; NC_002607.1.
DR   AlphaFoldDB; Q9HMF3; -.
DR   SMR; Q9HMF3; -.
DR   STRING; 64091.VNG_2570G; -.
DR   PaxDb; Q9HMF3; -.
DR   EnsemblBacteria; AAG20618; AAG20618; VNG_2570G.
DR   GeneID; 5953444; -.
DR   GeneID; 62887858; -.
DR   KEGG; hal:VNG_2570G; -.
DR   PATRIC; fig|64091.14.peg.1990; -.
DR   HOGENOM; CLU_103451_1_0_2; -.
DR   InParanoid; Q9HMF3; -.
DR   OMA; WDAGYEG; -.
DR   OrthoDB; 94658at2157; -.
DR   PhylomeDB; Q9HMF3; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000000554; 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; Reference proteome.
FT   CHAIN           1..165
FT                   /note="Probable deoxyuridine 5'-triphosphate
FT                   nucleotidohydrolase"
FT                   /id="PRO_0000153636"
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