DUT_YEAST
ID DUT_YEAST Reviewed; 147 AA.
AC P33317; D6VQP8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 179.
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=YBR252W; ORFNames=YBR1705;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8223452; DOI=10.1002/j.1460-2075.1993.tb06127.x;
RA Gadsden M.H., McIntosh E.M., Game J.C., Wilson P.J., Haynes R.H.;
RT "dUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae.";
RL EMBO J. 12:4425-4431(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8256522; DOI=10.1002/yea.320091014;
RA Doignon F., Biteau N., Aigle M., Crouzet M.;
RT "The complete sequence of a 6794 bp segment located on the right arm of
RT chromosome II of Saccharomyces cerevisiae. Finding of a putative dUTPase in
RT a yeast.";
RL Yeast 9:1131-1137(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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;
CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 2/2.
CC -!- SUBUNIT: Homotrimer.
CC -!- MISCELLANEOUS: Present with 4340 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Each trimer binds three substrate molecules. The ligands
CC are bound between subunits, and for each substrate molecule, residues
CC from adjacent subunits contribute to the binding interactions.
CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR EMBL; X74263; CAA52322.1; -; Genomic_DNA.
DR EMBL; L20296; AAA65611.1; -; Genomic_DNA.
DR EMBL; Z36121; CAA85215.1; -; Genomic_DNA.
DR EMBL; AY693064; AAT93083.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07368.1; -; Genomic_DNA.
DR PIR; S38189; S38189.
DR RefSeq; NP_009811.3; NM_001178600.3.
DR PDB; 3F4F; X-ray; 2.00 A; A/B/C=1-147.
DR PDB; 3HHQ; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 3P48; X-ray; 1.67 A; A/B/C=1-147.
DR PDBsum; 3F4F; -.
DR PDBsum; 3HHQ; -.
DR PDBsum; 3P48; -.
DR AlphaFoldDB; P33317; -.
DR SMR; P33317; -.
DR BioGRID; 32947; 103.
DR DIP; DIP-1661N; -.
DR IntAct; P33317; 5.
DR MINT; P33317; -.
DR STRING; 4932.YBR252W; -.
DR iPTMnet; P33317; -.
DR MaxQB; P33317; -.
DR PaxDb; P33317; -.
DR PRIDE; P33317; -.
DR EnsemblFungi; YBR252W_mRNA; YBR252W; YBR252W.
DR GeneID; 852554; -.
DR KEGG; sce:YBR252W; -.
DR SGD; S000000456; DUT1.
DR VEuPathDB; FungiDB:YBR252W; -.
DR eggNOG; KOG3370; Eukaryota.
DR GeneTree; ENSGT00390000018390; -.
DR HOGENOM; CLU_068508_2_1_1; -.
DR OMA; YAAFVHP; -.
DR BioCyc; YEAST:YBR252W-MON; -.
DR BRENDA; 3.6.1.23; 984.
DR Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates.
DR UniPathway; UPA00610; UER00666.
DR EvolutionaryTrace; P33317; -.
DR PRO; PR:P33317; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P33317; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0035870; F:dITP diphosphatase activity; IDA:SGD.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IDA:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0035863; P:dITP catabolic process; IDA:SGD.
DR GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0046081; P:dUTP catabolic process; IDA:SGD.
DR GO; GO:0009213; P:pyrimidine deoxyribonucleoside triphosphate catabolic process; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..147
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000182937"
FT BINDING 68..70
FT /ligand="substrate"
FT BINDING 82..85
FT /ligand="substrate"
FT BINDING 93
FT /ligand="substrate"
FT BINDING 137
FT /ligand="substrate"
FT BINDING 142..143
FT /ligand="substrate"
FT CONFLICT 10
FT /note="K -> N (in Ref. 1; CAA52322)"
FT /evidence="ECO:0000305"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3P48"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3P48"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3F4F"
SQ SEQUENCE 147 AA; 15307 MW; 19AC6012C3A061F2 CRC64;
MTATSDKVLK IQLRSASATV PTKGSATAAG YDIYASQDIT IPAMGQGMVS TDISFTVPVG
TYGRIAPRSG LAVKNGIQTG AGVVDRDYTG EVKVVLFNHS QRDFAIKKGD RVAQLILEKI
VDDAQIVVVD SLEESARGAG GFGSTGN
