ID DUT_LACLA Reviewed; 150 AA. AC Q9CJ30; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase; DE Short=dUTPase; DE EC=3.6.1.23; DE AltName: Full=dUTP pyrophosphatase; GN Name=dut; OrderedLocusNames=LL0176; ORFNames=L181168; OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=272623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL1403; RX PubMed=11337471; DOI=10.1101/gr.gr-1697r; RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "The complete genome sequence of the lactic acid bacterium Lactococcus RT lactis ssp. lactis IL1403."; RL Genome Res. 11:731-753(2001). 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:0000250}. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP CC route): step 2/2. CC -!- SIMILARITY: Belongs to the dUTPase family. {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; AE005176; AAK04274.1; -; Genomic_DNA. DR PIR; H86646; H86646. DR RefSeq; NP_266332.1; NC_002662.1. DR RefSeq; WP_010905176.1; NC_002662.1. DR AlphaFoldDB; Q9CJ30; -. DR SMR; Q9CJ30; -. DR PaxDb; 272623-L181168; -. DR EnsemblBacteria; AAK04274; AAK04274; L181168. DR KEGG; lla:L181168; -. DR PATRIC; fig|272623.7.peg.198; -. DR eggNOG; COG0756; Bacteria. DR HOGENOM; CLU_068508_0_0_9; -. DR OrthoDB; 9809956at2; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000002196; Chromosome. DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. 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 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..150 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase" FT /id="PRO_0000182872" FT BINDING 67..69 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 80 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 84..86 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 150 AA; 16722 MW; 6702DBCF10942516 CRC64; MKIRGFEVVT KYKNAGINIP KRSTEHSAGY DIEAAETVSF APGEIKLIPT GLKAYMQAGE VLYMYDRSSN PRKKGLVLIN SVGVIDKDYY NNPDNEGHMF MQMRNFTDEE VVIEKGERVV QGVFMPFLVA DGDENQEKEE RTGGFGSTGA //