ID DUT_BIFLO Reviewed; 158 AA.
AC Q8G4E8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 105.
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=BL1438;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014295; AAN25235.1; -; Genomic_DNA.
DR RefSeq; NP_696599.1; NC_004307.2.
DR RefSeq; WP_007055963.1; NC_004307.2.
DR AlphaFoldDB; Q8G4E8; -.
DR SMR; Q8G4E8; -.
DR STRING; 206672.BL1438; -.
DR EnsemblBacteria; AAN25235; AAN25235; BL1438.
DR GeneID; 69578389; -.
DR KEGG; blo:BL1438; -.
DR PATRIC; fig|206672.9.peg.296; -.
DR HOGENOM; CLU_068508_1_3_11; -.
DR OrthoDB; 9809956at2; -.
DR PhylomeDB; Q8G4E8; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000000439; 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 NCBIfam; TIGR00576; dut; 1.
DR PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; dUTPase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..158
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000182830"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 92..94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
SQ SEQUENCE 158 AA; 16747 MW; F97BD03FA2011CF4 CRC64;
MAFDETYNEP ESTEVLVKSL DPEHPAQLHY AHAGDAGADL ITTVDVTLKP FERALVPTGV
AIALPAGYVA LVHPRSGLAA KQGVTVLNAP GTVDAGYRGE IKVPLINLDP KHTAVFHPGD
RIAQLVIQRY VEARFIPAET LPGSDRAERG FGSTGVAS
//
