ID   DUT_BURTA               Reviewed;         148 AA.
AC   Q2T0H6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
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};
GN   OrderedLocusNames=BTH_I0767;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000086; ABC36324.1; -; Genomic_DNA.
DR   RefSeq; WP_009892605.1; NZ_CP008785.1.
DR   PDB; 4LHR; X-ray; 1.50 A; A=1-148.
DR   PDBsum; 4LHR; -.
DR   AlphaFoldDB; Q2T0H6; -.
DR   SMR; Q2T0H6; -.
DR   GeneID; 66546303; -.
DR   KEGG; bte:BTH_I0767; -.
DR   HOGENOM; CLU_068508_1_1_4; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001930; Chromosome I.
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   NCBIfam; TIGR00576; dut; 1.
DR   PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR   PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism.
FT   CHAIN           1..148
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_1000015457"
FT   BINDING         67..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         84..86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   HELIX           10..14
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          44..54
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   HELIX           68..74
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          91..99
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:4LHR"
FT   STRAND          112..120
FT                   /evidence="ECO:0007829|PDB:4LHR"
SQ   SEQUENCE   148 AA;  15783 MW;  DEF793839D83E4A4 CRC64;
     MKLDLKILDA RMRDYLPKYA TTGSAGLDLR ACLDAPVTLK PGDTALVPTG LAIHLADPGY
     AALILPRSGL GHKHGIVLGN LVGLIDSDYQ GELMISTWNR GQTEFVLNPF ERLAQLVIVP
     VVQATFNIVG DFAQSDRGAG GFGSTGRH
//