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 27-MAR-2024, entry version 137. 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}; GN OrderedLocusNames=CBU_0293; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; 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; Evidence={ECO:0000255|HAMAP- CC 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}; 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; 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 OrthoDB; 9809956at2; -. 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 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 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 //