ID DUT_CHLPN Reviewed; 145 AA. AC Q9Z9C2; Q9JQD0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 145. 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=CPn_0059, CP_0716, CpB0060; OS Chlamydia pneumoniae (Chlamydophila pneumoniae). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=83558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CWL029; RX PubMed=10192388; DOI=10.1038/7716; RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.; RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis."; RL Nat. Genet. 21:385-389(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AR39; RX PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., RA Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae RT AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J138; RX PubMed=10871362; DOI=10.1093/nar/28.12.2311; RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.; RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from RT Japan and CWL029 from USA."; RL Nucleic Acids Res. 28:2311-2314(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW-183; RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.; RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with RT other Chlamydia strains based on whole genome sequence analysis."; RL Submitted (MAY-2002) 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; AE001363; AAD18212.1; -; Genomic_DNA. DR EMBL; AE002161; AAF38522.1; -; Genomic_DNA. DR EMBL; BA000008; BAA98270.1; -; Genomic_DNA. DR EMBL; AE009440; AAP97993.1; -; Genomic_DNA. DR PIR; D72124; D72124. DR PIR; D86498; D86498. DR RefSeq; NP_224267.1; NC_000922.1. DR RefSeq; WP_010882709.1; NZ_LN847257.1. DR AlphaFoldDB; Q9Z9C2; -. DR SMR; Q9Z9C2; -. DR STRING; 406984.CPK_ORF00563; -. DR GeneID; 45050103; -. DR KEGG; cpa:CP_0716; -. DR KEGG; cpj:dut; -. DR KEGG; cpn:CPn_0059; -. DR KEGG; cpt:CpB0060; -. DR PATRIC; fig|115713.3.peg.67; -. DR eggNOG; COG0756; Bacteria. DR HOGENOM; CLU_068508_1_2_0; -. DR OMA; RSGMGHK; -. DR OrthoDB; 9809956at2; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000000583; Chromosome. DR Proteomes; UP000000801; 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..145 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_0000182846" 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 145 AA; 15347 MW; 025E5B34DF488A83 CRC64; MTVFCELDSG GELPEYTTPG AAGADLRANI EEPIALLPGQ RALIPTGIKA EIPEGYELQV RPRSGLALKH GITVLNSPGT IDSDYRGEIR VILINFGDST FIIEPKMRIA QVVLSPVVQA TFVVKQESLA ETARGSGGFG HTGAS //