ID   DUT_XANCP               Reviewed;         152 AA.
AC   Q8P458;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=XCC3858;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(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_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; AE008922; AAM43089.1; -; Genomic_DNA.
DR   RefSeq; NP_639198.1; NC_003902.1.
DR   AlphaFoldDB; Q8P458; -.
DR   SMR; Q8P458; -.
DR   STRING; 340.xcc-b100_4042; -.
DR   EnsemblBacteria; AAM43089; AAM43089; XCC3858.
DR   KEGG; xcc:XCC3858; -.
DR   PATRIC; fig|190485.4.peg.4127; -.
DR   eggNOG; COG0756; Bacteria.
DR   HOGENOM; CLU_068508_1_1_6; -.
DR   OMA; YAAFVHP; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..152
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182920"
FT   BINDING         71..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         88..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
SQ   SEQUENCE   152 AA;  16085 MW;  7EB25119DDA03940 CRC64;
     MTQSLQVKLL DPRFGDLWPL PAYATEASAG MDLRAALEAP MTLEPGDAAL IPSGIAIHLD
     DPQVCAVILP RSGLGHRHGI VLGNGTGLID ADYQGPLLIS TWNRGREAFT IEPGDRIAQL
     VILPIVRVSL QVVDTFVDSA RGAGGFGHTG VR