ID   DUT_ARCFU               Reviewed;         168 AA.
AC   O29157;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=AF_1108;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(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: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; AE000782; AAB90130.1; -; Genomic_DNA.
DR   PIR; C69388; C69388.
DR   RefSeq; WP_010878604.1; NC_000917.1.
DR   AlphaFoldDB; O29157; -.
DR   SMR; O29157; -.
DR   STRING; 224325.AF_1108; -.
DR   EnsemblBacteria; AAB90130; AAB90130; AF_1108.
DR   GeneID; 24794713; -.
DR   KEGG; afu:AF_1108; -.
DR   eggNOG; arCOG04048; Archaea.
DR   HOGENOM; CLU_103451_2_0_2; -.
DR   OMA; WDAGYEG; -.
DR   OrthoDB; 94658at2157; -.
DR   PhylomeDB; O29157; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000002199; 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..168
FT                   /note="Probable deoxyuridine 5'-triphosphate
FT                   nucleotidohydrolase"
FT                   /id="PRO_0000153635"
SQ   SEQUENCE   168 AA;  19227 MW;  D99EE0FB943869D6 CRC64;
     MAVLSGDEIR KLIQKEGLIR DYVDLETQIQ PNGFDCTLRS VYRLRGCGRV DFDNSRRELP
     ELEEVEFRDW VYLPKGVYRA KLNEVVRLGN DIMAIARPRS TLIRCGANVL TAVWDAGYEG
     RSEVSIVVHN DYGIWLSRNA RIIQLVFIRL SSPTKGYEGV YKGENIDS