ID DUT_RICRS Reviewed; 148 AA. AC A8GRY1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 27-MAR-2024, entry version 81. 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=A1G_03095; OS Rickettsia rickettsii (strain Sheila Smith). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=392021; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sheila Smith; RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Dasch G., Eremeeva M.; RT "Complete genome sequence of Rickettsia rickettsii."; RL Submitted (SEP-2007) 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; CP000848; ABV76156.1; -; Genomic_DNA. DR RefSeq; WP_012150745.1; NZ_CP121767.1. DR AlphaFoldDB; A8GRY1; -. DR SMR; A8GRY1; -. DR GeneID; 79937302; -. DR KEGG; rri:A1G_03095; -. DR HOGENOM; CLU_068508_1_2_5; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000006832; 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. FT CHAIN 1..148 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_1000015509" FT BINDING 68..70 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 81 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 85..87 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 95 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" SQ SEQUENCE 148 AA; 16002 MW; F512C345FEB8CAF2 CRC64; MTITQVKIKK LENFSGSLPE YATEHSAGMD LIAANEQPIT IKAAAIQLIP TGIAIALPDS FEAQIRPRSG LAVKHGITVA NSPGTIDADY RGEIKVILIN LGKEDFIIEK GMRIAQMIIA KYERILWEES ISLMETMRGS GGFGSTGV //