ID DUT_HISS2 Reviewed; 151 AA. AC B0UUW5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 87. 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=HSM_0007; OS Histophilus somni (strain 2336) (Haemophilus somnus). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Histophilus. OX NCBI_TaxID=228400; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2336; RG US DOE Joint Genome Institute; RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F., RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M., RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S., RA Dyer D.W., Inzana T.J.; RT "Complete sequence of Haemophilus somnus 2336."; RL Submitted (FEB-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; CP000947; ACA32362.1; -; Genomic_DNA. DR RefSeq; WP_011608294.1; NC_010519.1. DR AlphaFoldDB; B0UUW5; -. DR SMR; B0UUW5; -. DR STRING; 228400.HSM_0007; -. DR GeneID; 31486282; -. DR KEGG; hsm:HSM_0007; -. DR HOGENOM; CLU_068508_1_1_6; -. 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..151 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_1000076060" FT BINDING 70..72 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 83 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 87..89 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 97 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" SQ SEQUENCE 151 AA; 16346 MW; F86577AA26C44040 CRC64; MKKIDVKILD PRIGTEFPLP TYATIGSAGL DLRALVDEGF EVQPGETKLI STGLSIYIAD PNLAAVILPR SGLGHKNGIV LGNLVGLIDS DYQGPLMVSL WNRSDKPFKI EIGDRIAQLV FVPVVQAEFN IVEEFQQTDR GNGGFGHSGK K //