ID   DUT_ANTLO               Reviewed;         143 AA.
AC   Q6E4Q0;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   13-SEP-2023, entry version 55.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000250|UniProtKB:P33317};
DE            Short=dUTPase {ECO:0000250|UniProtKB:P33317};
DE            EC=3.6.1.23 {ECO:0000250|UniProtKB:P33317};
DE   AltName: Full=dUTP pyrophosphatase {ECO:0000250|UniProtKB:P33317};
GN   Name=DUT1;
OS   Antonospora locustae (Microsporidian parasite) (Nosema locustae).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Antonospora.
OX   NCBI_TaxID=278021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15186746; DOI=10.1016/j.cub.2004.04.041;
RA   Slamovits C.H., Fast N.M., Law J.S., Keeling P.J.;
RT   "Genome compaction and stability in microsporidian intracellular
RT   parasites.";
RL   Curr. Biol. 14:891-896(2004).
CC   -!- FUNCTION: Involved in nucleotide metabolism via production of dUMP, the
CC       immediate precursor of thymidine nucleotides, and decreases the
CC       intracellular concentration of dUTP so that uracil cannot be
CC       incorporated into DNA. {ECO:0000250|UniProtKB:P33317}.
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:0000250|UniProtKB:P33317};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10249;
CC         Evidence={ECO:0000250|UniProtKB:P33317};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P33317};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P33317}.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; AY574349; AAT72741.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6E4Q0; -.
DR   SMR; Q6E4Q0; -.
DR   UniPathway; UPA00610; UER00666.
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.
FT   CHAIN           1..143
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182927"
FT   BINDING         65
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         78
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         132
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         138
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
SQ   SEQUENCE   143 AA;  15526 MW;  F8E434A8A47CBA8C CRC64;
     MSEIITVKRL FSDAKIPVRH SEGAAAYDLY AYEDTVVAPN ERKVIATGVR ITVPLSCQGT
     IYSRSGLALK YCIEIFGVNI GPGETKDIVV DIYNHGKMPF NVAKGDRIAQ IVFIKLFGGD
     LHEVSELSDT KRGSCGWGST GIS
//