ID   DUT_XANOM               Reviewed;         155 AA.
AC   Q2P8A8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_00116};
DE            Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00116};
DE            EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00116};
DE   AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00116};
GN   Name=dut {ECO:0000255|HAMAP-Rule:MF_00116}; OrderedLocusNames=XOO0464;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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_00116}.
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_00116};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00116};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00116}.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00116}.
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DR   EMBL; AP008229; BAE67219.1; -; Genomic_DNA.
DR   RefSeq; WP_011407449.1; NC_007705.1.
DR   AlphaFoldDB; Q2P8A8; -.
DR   SMR; Q2P8A8; -.
DR   GeneID; 57848922; -.
DR   KEGG; xom:XOO0464; -.
DR   HOGENOM; CLU_068508_1_1_6; -.
DR   OMA; YAAFVHP; -.
DR   UniPathway; UPA00610; UER00666.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00116; dUTPase_bact; 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.
FT   CHAIN           1..155
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_1000015527"
FT   BINDING         74..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         91..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
SQ   SEQUENCE   155 AA;  16298 MW;  B623C68EFEFEEF9E CRC64;
     MSTPTQSLQV KLLDPRFGDL WPLPAYATES SAGMDLRAAL EAPMTLQPGD AALIPSGIAI
     HLADPQLCAV ILPRSGLGHR HGIVLGNGTG LIDADYQGPL LISTWNRGRE AFTIEPGDRI
     AQLVILPIVR AGLQVVDTFV DSARGAGGFG HTGVR