ID   DUT_BRUA2               Reviewed;         157 AA.
AC   Q2YRG4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=BAB1_1687;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(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; AM040264; CAJ11643.1; -; Genomic_DNA.
DR   RefSeq; WP_002964766.1; NZ_KN046823.1.
DR   PDB; 3MBQ; X-ray; 2.10 A; A/B/C=1-157.
DR   PDB; 3MDX; X-ray; 1.45 A; A=1-157.
DR   PDBsum; 3MBQ; -.
DR   PDBsum; 3MDX; -.
DR   AlphaFoldDB; Q2YRG4; -.
DR   SMR; Q2YRG4; -.
DR   STRING; 359391.BAB1_1687; -.
DR   EnsemblBacteria; CAJ11643; CAJ11643; BAB1_1687.
DR   GeneID; 45124982; -.
DR   GeneID; 55591299; -.
DR   KEGG; bmf:BAB1_1687; -.
DR   PATRIC; fig|359391.11.peg.203; -.
DR   HOGENOM; CLU_068508_1_0_5; -.
DR   OMA; YAAFVHP; -.
DR   PhylomeDB; Q2YRG4; -.
DR   UniPathway; UPA00610; UER00666.
DR   EvolutionaryTrace; Q2YRG4; -.
DR   PRO; PR:Q2YRG4; -.
DR   Proteomes; UP000002719; 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   PANTHER; PTHR11241; PTHR11241; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR00576; dut; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..157
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000231401"
FT   BINDING         76..78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         93..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   STRAND          12..15
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   HELIX           17..19
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          54..64
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          69..74
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   HELIX           77..83
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          100..108
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          121..129
FT                   /evidence="ECO:0007829|PDB:3MDX"
FT   STRAND          134..137
FT                   /evidence="ECO:0007829|PDB:3MBQ"
SQ   SEQUENCE   157 AA;  16660 MW;  7C9BB78942CFADEF CRC64;
     MTAASSSAPT LGIIRLEHAK GLDLPAYETA GSAGMDLRAA VAEDRQIVLL PGRRTLVPTG
     LILEIPQGYE VQIRPRSGLA FKNGITCLNT PGTIDSDYRG EVKVLLINLG DDDFRIERGM
     RIAQAVFAPV IQPKIEERAK ISETARGAGG FGSTGTA