ID DUT_CHRVO Reviewed; 150 AA. AC Q7MBE8; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 122. 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=CV_3081; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC OS 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=243365; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(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 --------------------------------------------------------------------------- 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; AE016825; AAQ60750.1; -; Genomic_DNA. DR RefSeq; WP_011136628.1; NC_005085.1. DR AlphaFoldDB; Q7MBE8; -. DR SMR; Q7MBE8; -. DR STRING; 243365.CV_3081; -. DR KEGG; cvi:CV_3081; -. DR eggNOG; COG0756; Bacteria. DR HOGENOM; CLU_068508_1_1_4; -. DR OrthoDB; 9809956at2; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000001424; 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..150 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_0000182849" FT BINDING 69..71 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 82 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 86..88 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" SQ SEQUENCE 150 AA; 15941 MW; 731296903C9C8241 CRC64; MQAVIDVKIL DARLRDNLPA YATAGSAGLD LRAATEETMT IQPGETQLVP TGIAIHLSDP GLAAMLLPRS GLGHKHGIVL GNLVGLIDSD YQGQMFVSVW NRGQQPFRLE PMERIAQMVI VPVVQASFNI VDDFDASDRG AGGFGSTGRG //