DUT_CANAW
ID DUT_CANAW Reviewed; 159 AA.
AC C4YFC7; P43058; Q5A912;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE Short=dUTPase;
DE EC=3.6.1.23;
DE AltName: Full=dUTP pyrophosphatase;
GN Name=DUT1; ORFNames=CAWG_01243;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=7874734; DOI=10.1007/bf00309928;
RA McIntosh E., Looser J., Haynes R.H., Pearlman R.E.;
RT "MluI site-dependent transcriptional regulation of the Candida albicans
RT dUTPase gene.";
RL Curr. Genet. 26:415-421(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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.
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; X77925; CAA54897.1; -; Genomic_DNA.
DR EMBL; CH672346; EEQ43013.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YFC7; -.
DR SMR; C4YFC7; -.
DR STRING; 5476.C4YFC7; -.
DR EnsemblFungi; EEQ43013; EEQ43013; CAWG_01243.
DR VEuPathDB; FungiDB:CAWG_01243; -.
DR HOGENOM; CLU_068508_2_1_1; -.
DR OMA; YAAFVHP; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
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: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 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.
FT CHAIN 1..159
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000413036"
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