ID DUT_CHLPB Reviewed; 145 AA. AC B3EPL0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 85. 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=Cphamn1_0943; OS Chlorobium phaeobacteroides (strain BS1). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=331678; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BS1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F., RA Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium phaeobacteroides BS1."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. 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; CP001101; ACE03888.1; -; Genomic_DNA. DR AlphaFoldDB; B3EPL0; -. DR SMR; B3EPL0; -. DR STRING; 331678.Cphamn1_0943; -. DR KEGG; cpb:Cphamn1_0943; -. DR eggNOG; COG0756; Bacteria. DR HOGENOM; CLU_068508_1_2_10; -. DR OrthoDB; 9809956at2; -. DR UniPathway; UPA00610; UER00666. 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. FT CHAIN 1..145 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_1000094952" FT BINDING 65..67 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 82..84 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 92 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" SQ SEQUENCE 145 AA; 15650 MW; DE39A33BD2379DEF CRC64; MVKVPVVRVN EKAILPHYAT FQAAGMDLAA CLDEPVTLAP FSTALIPTGL AIELPPGYEA QLRPRSGLAL KHMISLPNAP ATIDADYRGE VMVILVNYGK TPFIVCHGDR IAQMVVARYE HVRLEEVKAL SETDRGDGGF GHTGV //