ID   DUT_METBF               Reviewed;         171 AA.
AC   Q46EG2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=Mbar_A0752;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ69730.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46EG2; -.
DR   SMR; Q46EG2; -.
DR   STRING; 269797.Mbar_A0752; -.
DR   PaxDb; 269797-Mbar_A0752; -.
DR   KEGG; mba:Mbar_A0752; -.
DR   eggNOG; arCOG04048; Archaea.
DR   HOGENOM; CLU_103451_2_0_2; -.
DR   OrthoDB; 45265at2157; -.
DR   UniPathway; UPA00610; UER00666.
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..171
FT                   /note="Probable deoxyuridine 5'-triphosphate
FT                   nucleotidohydrolase"
FT                   /id="PRO_1000061430"
SQ   SEQUENCE   171 AA;  19100 MW;  23854036D3A59BD0 CRC64;
     MTLLSSTELR KLIQATPSLL ENAIDIETQI QPNGLELTLK EVKTIDGSGA VDFDNSERQL
     PDGKTLEFGN DGWIHLPKGI YKVLFNEIVN IPMNLAAIAK PRSTLIRCGT TLETAVWDAG
     YRGRSESMLV VYNTEGFRLK KDARIMQLLF YTLGAEVEKG YSGIYQNENT K
//