ID   DUT_METPP               Reviewed;         149 AA.
AC   A2SIY4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Mpe_A2570;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM95523.1; -; Genomic_DNA.
DR   RefSeq; WP_011830155.1; NC_008825.1.
DR   AlphaFoldDB; A2SIY4; -.
DR   SMR; A2SIY4; -.
DR   STRING; 420662.Mpe_A2570; -.
DR   EnsemblBacteria; ABM95523; ABM95523; Mpe_A2570.
DR   KEGG; mpt:Mpe_A2570; -.
DR   eggNOG; COG0756; Bacteria.
DR   HOGENOM; CLU_068508_1_1_4; -.
DR   OMA; ICYPDLE; -.
DR   OrthoDB; 1669228at2; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000000366; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..149
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_1000015482"
FT   BINDING         68..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         85..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
SQ   SEQUENCE   149 AA;  15608 MW;  DD5BBA4220C78CDD CRC64;
     MTTIDVKVLD PRMADQLPAY ATPGSAGLDL RACLDAPLLL EPGQTQLIPT GLSIHIGDPG
     LAAVILPRSG LGHKHGIVLG NLVGLIDSDY QGPLMVSCWN RGLAAFTVQP LERIAQLVIV
     PVVQASFRVV DDFGASERGE GGFGSTGQR