ID   DUT_METKA               Reviewed;         154 AA.
AC   Q8TV34;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=MK1566;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02779.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TV34; -.
DR   SMR; Q8TV34; -.
DR   STRING; 190192.MK1566; -.
DR   EnsemblBacteria; AAM02779; AAM02779; MK1566.
DR   KEGG; mka:MK1566; -.
DR   HOGENOM; CLU_103451_2_0_2; -.
DR   OMA; WDAGYEG; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001826; 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..154
FT                   /note="Probable deoxyuridine 5'-triphosphate
FT                   nucleotidohydrolase"
FT                   /id="PRO_0000153639"
SQ   SEQUENCE   154 AA;  17315 MW;  203B7FED196C8958 CRC64;
     MILGEYVLRD LFPDLDEDQY QPAGIDLKLD RVFRLEGRGA LLEGDDKRLP EYREVETEGG
     VFELEPNVPY VLELAPELEI PEDTAVLFLP RSTLLRSGVS VHTALGDPGF RGKIRVLAVN
     HHAAPYRIAH GERVVQAVFL RAEDAGRYEG DYGR