DUT_COXBU
ID DUT_COXBU Reviewed; 152 AA.
AC Q45920;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=CBU_0293;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nine Mile phase I;
RA Thiele D., Willems H., Oswald W., Krauss H.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAO89850.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X79075; CAA55678.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO89850.2; ALT_INIT; Genomic_DNA.
DR PIR; S44300; S44300.
DR RefSeq; NP_819336.2; NC_002971.3.
DR PDB; 3TQZ; X-ray; 1.75 A; A=1-152.
DR PDBsum; 3TQZ; -.
DR AlphaFoldDB; Q45920; -.
DR SMR; Q45920; -.
DR STRING; 227377.CBU_0293; -.
DR DNASU; 1208175; -.
DR EnsemblBacteria; AAO89850; AAO89850; CBU_0293.
DR GeneID; 1208175; -.
DR KEGG; cbu:CBU_0293; -.
DR PATRIC; fig|227377.7.peg.288; -.
DR eggNOG; COG0756; Bacteria.
DR HOGENOM; CLU_068508_1_1_6; -.
DR OMA; YAAFVHP; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..152
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000182856"
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"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:3TQZ"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:3TQZ"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3TQZ"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:3TQZ"
SQ SEQUENCE 152 AA; 16214 MW; 00041727C1882C57 CRC64;
MTHSVQLKIL DKRLGSEFPL PAYATTGSAG LDLRACLDEP LKIEPDETCL ISTGLAIYLG
HSNVAATILP RSGLGHKHGI VLGNLVGLID SDYQGPLMVS CWNRGKEPYT INPGDRIAQL
VVLPILKAQF AVVEEFELTE RGAGGFGSSG QN
