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Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase)

 DUT_YEAST               Reviewed;         147 AA.
P33317; D6VQP8;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 2.
25-OCT-2017, entry version 155.
RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
Short=dUTPase;
EC=3.6.1.23;
AltName: Full=dUTP pyrophosphatase;
Name=DUT1; OrderedLocusNames=YBR252W; ORFNames=YBR1705;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8223452;
Gadsden M.H., McIntosh E.M., Game J.C., Wilson P.J., Haynes R.H.;
"dUTP pyrophosphatase is an essential enzyme in Saccharomyces
cerevisiae.";
EMBO J. 12:4425-4431(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8256522; DOI=10.1002/yea.320091014;
Doignon F., Biteau N., Aigle M., Crouzet M.;
"The complete sequence of a 6794 bp segment located on the right arm
of chromosome II of Saccharomyces cerevisiae. Finding of a putative
dUTPase in a yeast.";
Yeast 9:1131-1137(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: This enzyme is involved in nucleotide metabolism: it
produces dUMP, the immediate precursor of thymidine nucleotides
and it decreases the intracellular concentration of dUTP so that
uracil cannot be incorporated into DNA.
-!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP
(dUTP route): step 2/2.
-!- SUBUNIT: Homotrimer.
-!- MISCELLANEOUS: Present with 4340 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: Each trimer binds three substrate molecules. The
ligands are bound between subunits, and for each substrate
molecule, residues from adjacent subunits contribute to the
binding interactions.
-!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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EMBL; X74263; CAA52322.1; -; Genomic_DNA.
EMBL; L20296; AAA65611.1; -; Genomic_DNA.
EMBL; Z36121; CAA85215.1; -; Genomic_DNA.
EMBL; AY693064; AAT93083.1; -; Genomic_DNA.
EMBL; BK006936; DAA07368.1; -; Genomic_DNA.
PIR; S38189; S38189.
RefSeq; NP_009811.3; NM_001178600.3.
PDB; 3F4F; X-ray; 2.00 A; A/B/C=1-147.
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.
PDB; 3P48; X-ray; 1.67 A; A/B/C=1-147.
PDBsum; 3F4F; -.
PDBsum; 3HHQ; -.
PDBsum; 3P48; -.
ProteinModelPortal; P33317; -.
SMR; P33317; -.
BioGrid; 32947; 97.
DIP; DIP-1661N; -.
IntAct; P33317; 5.
MINT; MINT-410177; -.
STRING; 4932.YBR252W; -.
iPTMnet; P33317; -.
MaxQB; P33317; -.
PRIDE; P33317; -.
EnsemblFungi; YBR252W; YBR252W; YBR252W.
GeneID; 852554; -.
KEGG; sce:YBR252W; -.
EuPathDB; FungiDB:YBR252W; -.
SGD; S000000456; DUT1.
GeneTree; ENSGT00390000018390; -.
HOGENOM; HOG000028966; -.
KO; K01520; -.
OMA; GVILINH; -.
OrthoDB; EOG092C5PPT; -.
BioCyc; YEAST:YBR252W-MONOMER; -.
BRENDA; 3.6.1.23; 984.
Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates.
UniPathway; UPA00610; UER00666.
EvolutionaryTrace; P33317; -.
PRO; PR:P33317; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0035870; F:dITP diphosphatase activity; IDA:SGD.
GO; GO:0004170; F:dUTP diphosphatase activity; IDA:SGD.
GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
GO; GO:0035863; P:dITP catabolic process; IDA:SGD.
GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
GO; GO:0046081; P:dUTP catabolic process; IDA:SGD.
GO; GO:0009213; P:pyrimidine deoxyribonucleoside triphosphate catabolic process; IMP:SGD.
CDD; cd07557; trimeric_dUTPase; 1.
InterPro; IPR029054; dUTPase-like.
InterPro; IPR036157; dUTPase-like_sf.
InterPro; IPR008181; dUTPase_1.
InterPro; IPR033704; dUTPase_trimeric.
Pfam; PF00692; dUTPase; 1.
SUPFAM; SSF51283; SSF51283; 1.
TIGRFAMs; TIGR00576; dut; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding;
Nucleotide metabolism; Reference proteome.
CHAIN 1 147 Deoxyuridine 5'-triphosphate
nucleotidohydrolase.
/FTId=PRO_0000182937.
REGION 68 70 Substrate binding.
REGION 82 85 Substrate binding.
REGION 142 143 Substrate binding.
BINDING 93 93 Substrate; via amide nitrogen and
carbonyl oxygen.
BINDING 137 137 Substrate.
CONFLICT 10 10 K -> N (in Ref. 1; CAA52322).
{ECO:0000305}.
STRAND 8 13 {ECO:0000244|PDB:3P48}.
STRAND 22 25 {ECO:0000244|PDB:3P48}.
STRAND 29 34 {ECO:0000244|PDB:3P48}.
STRAND 39 41 {ECO:0000244|PDB:3P48}.
STRAND 45 50 {ECO:0000244|PDB:3P48}.
STRAND 53 56 {ECO:0000244|PDB:3P48}.
STRAND 61 66 {ECO:0000244|PDB:3P48}.
HELIX 69 75 {ECO:0000244|PDB:3P48}.
STRAND 77 79 {ECO:0000244|PDB:3P48}.
STRAND 93 98 {ECO:0000244|PDB:3P48}.
STRAND 100 102 {ECO:0000244|PDB:3P48}.
STRAND 104 106 {ECO:0000244|PDB:3P48}.
STRAND 111 120 {ECO:0000244|PDB:3P48}.
STRAND 125 128 {ECO:0000244|PDB:3P48}.
STRAND 136 138 {ECO:0000244|PDB:3F4F}.
SEQUENCE 147 AA; 15307 MW; 19AC6012C3A061F2 CRC64;
MTATSDKVLK IQLRSASATV PTKGSATAAG YDIYASQDIT IPAMGQGMVS TDISFTVPVG
TYGRIAPRSG LAVKNGIQTG AGVVDRDYTG EVKVVLFNHS QRDFAIKKGD RVAQLILEKI
VDDAQIVVVD SLEESARGAG GFGSTGN


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