ID DUT_YERPE Reviewed; 151 AA. AC Q8ZJP5; Q0WKP5; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 136. 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=YPO0047, y0094, YP_0048; OS Yersinia pestis. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis; RX PubMed=11586360; DOI=10.1038/35097083; RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T., RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., RA Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIM10+ / Biovar Mediaevalis; RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002; RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.; RT "Genome sequence of Yersinia pestis KIM."; RL J. Bacteriol. 184:4601-4611(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91001 / Biovar Mediaevalis; RX PubMed=15368893; DOI=10.1093/dnares/11.3.179; RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., RA Wang J., Huang P., Yang R.; RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate RT avirulent to humans."; RL DNA Res. 11:179-197(2004). 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 -!- SEQUENCE CAUTION: CC Sequence=AAM83688.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAS60329.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AL590842; CAL18737.1; -; Genomic_DNA. DR EMBL; AE009952; AAM83688.1; ALT_INIT; Genomic_DNA. DR EMBL; AE017042; AAS60329.1; ALT_INIT; Genomic_DNA. DR PIR; AH0006; AH0006. DR RefSeq; YP_002345143.1; NC_003143.1. DR AlphaFoldDB; Q8ZJP5; -. DR SMR; Q8ZJP5; -. DR STRING; 214092.YPO0047; -. DR PaxDb; 214092-YPO0047; -. DR DNASU; 1145041; -. DR EnsemblBacteria; AAS60329; AAS60329; YP_0048. DR KEGG; ype:YPO0047; -. DR KEGG; ypk:y0094; -. DR KEGG; ypm:YP_0048; -. DR PATRIC; fig|1028802.3.peg.670; -. DR eggNOG; COG0756; Bacteria. DR HOGENOM; CLU_068508_1_1_6; -. DR OMA; RSGMGHK; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000000815; Chromosome. DR Proteomes; UP000001019; Chromosome. DR Proteomes; UP000002490; 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..151 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_0000182923" 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; 16212 MW; 00CFC87C93D12BF8 CRC64; MKKIDIKILD PRVGNEFPLP TYATEGSAGL DLRACLDHAV ELQPGQTTLL PTGLAIHIGD SALAAVILPR SGLGHKHGIV LGNLVGLIDS DYQGQLMVSV WNRGQQPFTI EPGERIAQMV FVPVVQAEFN LVEDFTDSER GTGGFGHSGR Q //