DUT_BURTA
ID DUT_BURTA Reviewed; 148 AA.
AC Q2T0H6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-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=BTH_I0767;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC36324.1; -; Genomic_DNA.
DR RefSeq; WP_009892605.1; NZ_CP008785.1.
DR PDB; 4LHR; X-ray; 1.50 A; A=1-148.
DR PDBsum; 4LHR; -.
DR AlphaFoldDB; Q2T0H6; -.
DR SMR; Q2T0H6; -.
DR PRIDE; Q2T0H6; -.
DR EnsemblBacteria; ABC36324; ABC36324; BTH_I0767.
DR GeneID; 66546303; -.
DR KEGG; bte:BTH_I0767; -.
DR HOGENOM; CLU_068508_1_1_4; -.
DR OMA; YAAFVHP; -.
DR OrthoDB; 1669228at2; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000001930; Chromosome I.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism.
FT CHAIN 1..148
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_1000015457"
FT BINDING 67..69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 84..86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:4LHR"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 44..54
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4LHR"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4LHR"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:4LHR"
SQ SEQUENCE 148 AA; 15783 MW; DEF793839D83E4A4 CRC64;
MKLDLKILDA RMRDYLPKYA TTGSAGLDLR ACLDAPVTLK PGDTALVPTG LAIHLADPGY
AALILPRSGL GHKHGIVLGN LVGLIDSDYQ GELMISTWNR GQTEFVLNPF ERLAQLVIVP
VVQATFNIVG DFAQSDRGAG GFGSTGRH