ID DUT_METBU Reviewed; 170 AA. AC Q12XH1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Probable deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_00635}; DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00635}; DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00635}; DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00635}; GN Name=dut {ECO:0000255|HAMAP-Rule:MF_00635}; GN OrderedLocusNames=Mbur_0910; OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / OS ACE-M). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanococcoides. OX NCBI_TaxID=259564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M; RX PubMed=19404327; DOI=10.1038/ismej.2009.45; RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S., RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L., RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N., RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T., RA Cavicchioli R.; RT "The genome sequence of the psychrophilic archaeon, Methanococcoides RT burtonii: the role of genome evolution in cold adaptation."; RL ISME J. 3:1012-1035(2009). 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_00635}. 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_00635}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP CC route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00635}. CC -!- SIMILARITY: Belongs to the dCTP deaminase family. Archaeal dUTPase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00635}. 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; CP000300; ABE51855.1; -; Genomic_DNA. DR RefSeq; WP_011499008.1; NC_007955.1. DR AlphaFoldDB; Q12XH1; -. DR SMR; Q12XH1; -. DR STRING; 259564.Mbur_0910; -. DR GeneID; 3998654; -. DR KEGG; mbu:Mbur_0910; -. DR HOGENOM; CLU_103451_2_0_2; -. DR OrthoDB; 45265at2157; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000001979; Chromosome. DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd07557; trimeric_dUTPase; 1. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00635; dUTPase_arch; 1. DR InterPro; IPR029054; dUTPase-like. DR InterPro; IPR036157; dUTPase-like_sf. DR InterPro; IPR023537; dUTPase_archaeal. DR InterPro; IPR033704; dUTPase_trimeric. DR PANTHER; PTHR42680; DCTP DEAMINASE; 1. DR PANTHER; PTHR42680:SF1; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; dUTPase-like; 1. PE 3: Inferred from homology; KW Hydrolase; Nucleotide metabolism. FT CHAIN 1..170 FT /note="Probable deoxyuridine 5'-triphosphate FT nucleotidohydrolase" FT /id="PRO_1000061431" SQ SEQUENCE 170 AA; 19122 MW; 77861D19B36ECE59 CRC64; MTLLSQNELR ELVLANPPLV ENMIDMDTQL QPNGVEMTLK EIRTIKSPGA VDFDNSGRRL SEGDTIEFNE DGWIHLDPGV YKVLLNEIVN IPKDLAAIAK PRSTLIRCGA TLETAVWDAG YSGRSECMIV VHNKDGFDLK KDARIMQLLF YHLHTEVEEG YSGSYQNENI //