ID DUT_RICPR Reviewed; 148 AA. AC Q9ZDD2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 118. 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=RP399; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). 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; AJ235271; CAA14856.1; -; Genomic_DNA. DR PIR; F71697; F71697. DR RefSeq; NP_220780.1; NC_000963.1. DR RefSeq; WP_004597580.1; NC_000963.1. DR PDB; 7N56; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J/K/L=1-148. DR PDB; 7N6S; X-ray; 1.75 A; A/B/C/D/E/F=1-148. DR PDBsum; 7N56; -. DR PDBsum; 7N6S; -. DR AlphaFoldDB; Q9ZDD2; -. DR SMR; Q9ZDD2; -. DR STRING; 272947.gene:17555479; -. DR EnsemblBacteria; CAA14856; CAA14856; CAA14856. DR GeneID; 57569524; -. DR KEGG; rpr:RP399; -. DR PATRIC; fig|272947.5.peg.412; -. DR eggNOG; COG0756; Bacteria. DR HOGENOM; CLU_068508_1_2_5; -. DR OrthoDB; 9809956at2; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000002480; 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 1: Evidence at protein level; KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; KW Reference proteome. FT CHAIN 1..148 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_0000182903" 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" FT STRAND 3..10 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 27..32 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 52..56 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 61..66 FT /evidence="ECO:0007829|PDB:7N6S" FT HELIX 69..75 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 95..100 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 113..121 FT /evidence="ECO:0007829|PDB:7N6S" FT STRAND 123..129 FT /evidence="ECO:0007829|PDB:7N6S" FT TURN 138..141 FT /evidence="ECO:0007829|PDB:7N6S" SQ SEQUENCE 148 AA; 16068 MW; 23A97A89A3702001 CRC64; MTIIEVKIKK LENFLGNLPE YATEHSAGMD LVAANEQSIT IKVGSIQLIP TGIAIALPES FEAQIRPRSG LAVKHGITVA NSPGTIDADY RGEIKVLLIN LGNKDFIIEK GMRIAQMIIA KYERVLWAET SILTETMRGR GGFGSTGL //