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Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (dUTP-pyrophosphatase-like 1) (AtDUT1)

 DUT_ARATH               Reviewed;         166 AA.
Q9STG6;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 113.
RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
Short=dUTPase;
EC=3.6.1.23;
AltName: Full=dUTP pyrophosphatase;
AltName: Full=dUTP-pyrophosphatase-like 1;
Short=AtDUT1;
Name=DUT; Synonyms=DUT1; OrderedLocusNames=At3g46940;
ORFNames=T6H20.30;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
FUNCTION.
PubMed=20227352; DOI=10.1016/j.dnarep.2010.02.009;
Siaud N., Dubois E., Massot S., Richaud A., Dray E., Collier J.,
Doutriaux M.P.;
"The SOS screen in Arabidopsis: a search for functions involved in DNA
metabolism.";
DNA Repair 9:567-578(2010).
[5]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
SUBUNIT.
PubMed=17565183; DOI=10.1107/S1744309107016004;
Bajaj M., Moriyama H.;
"Purification, crystallization and preliminary crystallographic
analysis of deoxyuridine triphosphate nucleotidohydrolase from
Arabidopsis thaliana.";
Acta Crystallogr. F 63:409-411(2007).
[6]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
Bajaj M., Moriyama H.;
"Structure of dutpase from Arabidopsis thaliana.";
Submitted (FEB-2009) to the PDB data bank.
-!- 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,
preventing uracil incorporation into DNA.
{ECO:0000269|PubMed:20227352}.
-!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) per trimer.;
-!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP
(dUTP route): step 2/2.
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17565183}.
-!- MISCELLANEOUS: Silencing of DUT leads to high seedling mortality
and affects plant growth and flower organ morphology in surviving
plants.
-!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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EMBL; AL096859; CAB51171.1; -; Genomic_DNA.
EMBL; CP002686; AEE78222.1; -; Genomic_DNA.
EMBL; AF370334; AAK44149.1; -; mRNA.
EMBL; AY062989; AAL34163.1; -; mRNA.
PIR; T12954; T12954.
RefSeq; NP_190278.1; NM_114561.4.
UniGene; At.48742; -.
UniGene; At.71138; -.
PDB; 2PC5; X-ray; 2.20 A; A/B/C=1-166.
PDB; 4OOP; X-ray; 1.50 A; A/B/C=1-166.
PDB; 4OOQ; X-ray; 2.00 A; A/B/C=1-166.
PDBsum; 2PC5; -.
PDBsum; 4OOP; -.
PDBsum; 4OOQ; -.
ProteinModelPortal; Q9STG6; -.
SMR; Q9STG6; -.
BioGrid; 9167; 1.
STRING; 3702.AT3G46940.1; -.
iPTMnet; Q9STG6; -.
PaxDb; Q9STG6; -.
PRIDE; Q9STG6; -.
EnsemblPlants; AT3G46940.1; AT3G46940.1; AT3G46940.
GeneID; 823847; -.
Gramene; AT3G46940.1; AT3G46940.1; AT3G46940.
KEGG; ath:AT3G46940; -.
Araport; AT3G46940; -.
TAIR; locus:2102817; AT3G46940.
eggNOG; KOG3370; Eukaryota.
eggNOG; COG0756; LUCA.
HOGENOM; HOG000028966; -.
KO; K01520; -.
OMA; GVILINH; -.
OrthoDB; EOG09360O3G; -.
PhylomeDB; Q9STG6; -.
BioCyc; ARA:AT3G46940-MONOMER; -.
BioCyc; MetaCyc:AT3G46940-MONOMER; -.
BRENDA; 3.6.1.23; 399.
Reactome; R-ATH-499943; Interconversion of nucleotide di- and triphosphates.
UniPathway; UPA00610; UER00666.
EvolutionaryTrace; Q9STG6; -.
PRO; PR:Q9STG6; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9STG6; baseline and differential.
Genevisible; Q9STG6; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0004170; F:dUTP diphosphatase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:TAIR.
GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central.
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 1 166 Deoxyuridine 5'-triphosphate
nucleotidohydrolase.
/FTId=PRO_0000401366.
METAL 138 138 Magnesium; shared with trimeric partners.
{ECO:0000269|PubMed:17565183}.
STRAND 30 35 {ECO:0000244|PDB:4OOP}.
STRAND 42 45 {ECO:0000244|PDB:4OOP}.
STRAND 51 54 {ECO:0000244|PDB:4OOP}.
STRAND 59 61 {ECO:0000244|PDB:4OOP}.
STRAND 66 70 {ECO:0000244|PDB:4OOP}.
STRAND 73 76 {ECO:0000244|PDB:4OOP}.
STRAND 81 86 {ECO:0000244|PDB:4OOP}.
HELIX 89 95 {ECO:0000244|PDB:4OOP}.
STRAND 97 100 {ECO:0000244|PDB:4OOP}.
STRAND 103 105 {ECO:0000244|PDB:2PC5}.
STRAND 113 118 {ECO:0000244|PDB:4OOP}.
STRAND 120 122 {ECO:0000244|PDB:4OOP}.
STRAND 124 126 {ECO:0000244|PDB:4OOP}.
STRAND 131 141 {ECO:0000244|PDB:4OOP}.
STRAND 145 147 {ECO:0000244|PDB:4OOP}.
SEQUENCE 166 AA; 17557 MW; 5487738DF4A55BFF CRC64;
MACVNEPSPK LQKLDRNGIH GDSSPSPFFK VKKLSEKAVI PTRGSPLSAG YDLSSAVDSK
VPARGKALIP TDLSIAVPEG TYARIAPRSG LAWKHSIDVG AGVIDADYRG PVGVILFNHS
DADFEVKFGD RIAQLIIEKI VTPDVVEVDD LDETVRGDGG FGSTGV


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