ID   DUT_ENCCU               Reviewed;         144 AA.
AC   Q8SRS0;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 102.
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; OrderedLocusNames=ECU06_0430;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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; AL590446; CAD25403.1; -; Genomic_DNA.
DR   RefSeq; NP_585799.1; NM_001041421.1.
DR   AlphaFoldDB; Q8SRS0; -.
DR   SMR; Q8SRS0; -.
DR   STRING; 284813.Q8SRS0; -.
DR   GeneID; 859223; -.
DR   KEGG; ecu:ECU06_0430; -.
DR   VEuPathDB; MicrosporidiaDB:ECU06_0430; -.
DR   HOGENOM; CLU_068508_3_0_1; -.
DR   InParanoid; Q8SRS0; -.
DR   OMA; QIAENIC; -.
DR   OrthoDB; 1343066at2759; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000000819; Chromosome VI.
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..144
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182928"
FT   BINDING         66
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         133
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"
FT   BINDING         139
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
SQ   SEQUENCE   144 AA;  15850 MW;  9921FE374F5413FC CRC64;
     MTVSEIRVRK INPRAKIPKR QSEGAAGYDI HSVESGRIPP NGRKSVRTGL AWDVPQSVVG
     LVFGRSGLAL RNWIEVVETC VHPGEDKELV ITLVNNGREV FEYEESSRIA QLVFVPVLSC
     EIDLVESLDL TERGCLGFGS TGMK
//