ID   DUT_SYNWW               Reviewed;         145 AA.
AC   Q0AYH7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Swol_0911;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68227.1; -; Genomic_DNA.
DR   RefSeq; WP_011640332.1; NC_008346.1.
DR   AlphaFoldDB; Q0AYH7; -.
DR   SMR; Q0AYH7; -.
DR   STRING; 335541.Swol_0911; -.
DR   EnsemblBacteria; ABI68227; ABI68227; Swol_0911.
DR   KEGG; swo:Swol_0911; -.
DR   eggNOG; COG0756; Bacteria.
DR   HOGENOM; CLU_068508_1_2_9; -.
DR   OMA; YAAFVHP; -.
DR   OrthoDB; 1669228at2; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001968; 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..145
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_1000076075"
FT   BINDING         65..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         82..84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
SQ   SEQUENCE   145 AA;  15881 MW;  FDFC2662C68E155A CRC64;
     MKVLFNRLHS HDLPLPRYMT PGSSGLDLYA AVDEEILIPS GKIVLVPTGL ALAIPEGYEA
     QIRPRSGLAL KYGITLLNTP GTIDADYRGE IKVIVINLGD KDYILKRGER IAQMVFSRVE
     KAEFMEVKSL DETLRGAGGF GHTGI