ID   DUT_CANAL               Reviewed;         159 AA.
AC   P0CY19; A0A1D8PCH6; P43058; Q5A912;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   Name=DUT1; OrderedLocusNames=CAALFM_C101330CA;
GN   ORFNames=CaO19.10832, CaO19.3322;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; CP017623; AOW25826.1; -; Genomic_DNA.
DR   PIR; S51498; S51498.
DR   RefSeq; XP_718145.1; XM_713052.1.
DR   AlphaFoldDB; P0CY19; -.
DR   SMR; P0CY19; -.
DR   STRING; 237561.P0CY19; -.
DR   PRIDE; P0CY19; -.
DR   GeneID; 3640188; -.
DR   KEGG; cal:CAALFM_C101330CA; -.
DR   CGD; CAL0000195525; DUT1.
DR   VEuPathDB; FungiDB:C1_01330C_A; -.
DR   eggNOG; KOG3370; Eukaryota.
DR   HOGENOM; CLU_068508_2_1_1; -.
DR   InParanoid; P0CY19; -.
DR   OMA; YAAFVHP; -.
DR   OrthoDB; 1495752at2759; -.
DR   UniPathway; UPA00610; UER00666.
DR   PRO; PR:P0CY19; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IDA:CGD.
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   PANTHER; PTHR11241; PTHR11241; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR00576; dut; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..159
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182930"
FT   BINDING         78..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         92..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153..154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   159 AA;  16945 MW;  982C016F1D31013A CRC64;
     MTSEDQSLKK QKLESTQSLK VYLRSPKGKV PTKGSALAAG YDLYSAEAAT IPAHGQGLVS
     TDISIIVPIG TYGRVAPRSG LAVKHGISTG AGVIDADYRG EVKVVLFNHS EKDFEIKEGD
     RIAQLVLEQI VNADIKEISL EELDNTERGE GGFGSTGKN