ID   DUT_EREGS               Reviewed;         153 AA.
AC   Q74ZF0;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=AGR249C;
OS   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54739.1; -; Genomic_DNA.
DR   RefSeq; NP_986915.1; NM_211977.1.
DR   AlphaFoldDB; Q74ZF0; -.
DR   SMR; Q74ZF0; -.
DR   STRING; 284811.Q74ZF0; -.
DR   EnsemblFungi; AAS54739; AAS54739; AGOS_AGR249C.
DR   GeneID; 4623217; -.
DR   KEGG; ago:AGOS_AGR249C; -.
DR   eggNOG; KOG3370; Eukaryota.
DR   HOGENOM; CLU_068508_2_1_1; -.
DR   InParanoid; Q74ZF0; -.
DR   OMA; ICYPDLE; -.
DR   OrthoDB; 1343066at2759; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central.
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..153
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182929"
FT   BINDING         75
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         88
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         91
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         94
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         99
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         143
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         148
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
FT   BINDING         149
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /evidence="ECO:0000250|UniProtKB:P33317"
SQ   SEQUENCE   153 AA;  16071 MW;  B642014781B1B4E2 CRC64;
     MTDQPAKKVH SAPTLKVQLR SENAIAPTKG SAAAAGYDIY ASQDCVIPGR GQGLVATDVS
     FTVPVGTYGR IAPRSGLAVK HGIQTGAGVV DRDYTGEVKI VLFNHSDRDY AVKRGDRVAQ
     LVLERIVDDA EVVVVESLDE SSRGEGGFGS TGN
//