ID DUT_BACTN Reviewed; 144 AA. AC Q8A245; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 113. 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=BT_3461; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., RA Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(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; AE015928; AAO78567.1; -; Genomic_DNA. DR RefSeq; NP_812373.1; NC_004663.1. DR RefSeq; WP_008767650.1; NZ_UYXG01000003.1. DR AlphaFoldDB; Q8A245; -. DR SMR; Q8A245; -. DR STRING; 226186.BT_3461; -. DR PaxDb; 226186-BT_3461; -. DR EnsemblBacteria; AAO78567; AAO78567; BT_3461. DR GeneID; 60924642; -. DR KEGG; bth:BT_3461; -. DR PATRIC; fig|226186.12.peg.3528; -. DR eggNOG; COG0756; Bacteria. DR HOGENOM; CLU_068508_1_2_10; -. DR InParanoid; Q8A245; -. DR OrthoDB; 9809956at2; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000001414; Chromosome. DR GO; GO:0004170; F:dUTP diphosphatase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central. 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..144 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_0000182826" FT BINDING 63..65 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 76 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" FT BINDING 80..82 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116" SQ SEQUENCE 144 AA; 15590 MW; 77B093540F371178 CRC64; MNVQVINKSK HPLPAYATEL SAGMDIRANL SEPITLAPLQ RCLVPTGIYI ALPQGFEAQV RPRSGLAIKK GITVLNSPGT IDADYRGEVC IILVNLSSEP FVIEDGERIA QMVIARHEQA VWQEVEVLDE TERGAGGFGH TGRG //