DUT_SALPC
ID DUT_SALPC Reviewed; 152 AA.
AC C0Q1X2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=SPC_3813;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN47888.1; -; Genomic_DNA.
DR RefSeq; WP_000976078.1; NC_012125.1.
DR AlphaFoldDB; C0Q1X2; -.
DR SMR; C0Q1X2; -.
DR EnsemblBacteria; ACN47888; ACN47888; SPC_3813.
DR KEGG; sei:SPC_3813; -.
DR HOGENOM; CLU_068508_1_1_6; -.
DR OMA; YAAFVHP; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000001599; 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.
FT CHAIN 1..152
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_1000119246"
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"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
SQ SEQUENCE 152 AA; 16168 MW; A3524F74748CE1F2 CRC64;
MMKKIDVKIL DPRVGQQFPL PTYATSGSAG LDLRACLDDA VELAPGATTL VPTGLAIHIA
DPSLAAVMLP RSGLGHKHGI VLGNLVGLID SDYQGQLMVS IWNRGQDSFT IEPGERIAQM
VFVPVVQAEF NLVEAFDATE RGEGGFGHSG RK
