ID   E0RWD7_BUTPB            Unreviewed;       145 AA.
AC   E0RWD7;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE            EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN   Name=dut {ECO:0000313|EMBL:ADL34235.1};
GN   OrderedLocusNames=bpr_I1498 {ECO:0000313|EMBL:ADL34235.1};
OS   Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS   (Clostridium proteoclasticum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL34235.1, ECO:0000313|Proteomes:UP000001299};
RN   [1] {ECO:0000313|EMBL:ADL34235.1, ECO:0000313|Proteomes:UP000001299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51982 / DSM 14932 / B316
RC   {ECO:0000313|Proteomes:UP000001299};
RX   PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA   Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA   Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT   "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT   highlights adaptation to a polysaccharide-rich environment.";
RL   PLoS ONE 5:E11942-E11942(2010).
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:0000256|ARBA:ARBA00000878};
CC   -!- SIMILARITY: Belongs to the dUTPase family.
CC       {ECO:0000256|ARBA:ARBA00006581}.
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DR   EMBL; CP001810; ADL34235.1; -; Genomic_DNA.
DR   RefSeq; WP_013280889.1; NC_014387.1.
DR   AlphaFoldDB; E0RWD7; -.
DR   STRING; 515622.bpr_I1498; -.
DR   KEGG; bpb:bpr_I1498; -.
DR   eggNOG; COG0756; Bacteria.
DR   HOGENOM; CLU_068508_1_2_9; -.
DR   Proteomes; UP000001299; Chromosome 1.
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:InterPro.
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   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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADL34235.1};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001299}.
FT   DOMAIN          28..143
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   145 AA;  16635 MW;  1655F37C3A756285 CRC64;
     MKREVKIKYF NDKIEKLQYI DGKSDWIDLR SAEDIDLKQG EFKLIPLGVA MEIPEGYEAH
     VVPRSSTFKN FGVIQANSMG IIDHSYCGDN DQWFMPVIAM RDTHIGFNDR ICQFRIMENQ
     PHIDFEECEH LTGADRGGFG STGTK
//