ID   DUT_ARATH               Reviewed;         166 AA.
AC   Q9STG6;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
DE   AltName: Full=dUTP-pyrophosphatase-like 1;
DE            Short=AtDUT1;
GN   Name=DUT; Synonyms=DUT1; OrderedLocusNames=At3g46940;
GN   ORFNames=T6H20.30;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=20227352; DOI=10.1016/j.dnarep.2010.02.009;
RA   Siaud N., Dubois E., Massot S., Richaud A., Dray E., Collier J.,
RA   Doutriaux M.P.;
RT   "The SOS screen in Arabidopsis: a search for functions involved in DNA
RT   metabolism.";
RL   DNA Repair 9:567-578(2010).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP   SUBUNIT.
RX   PubMed=17565183; DOI=10.1107/s1744309107016004;
RA   Bajaj M., Moriyama H.;
RT   "Purification, crystallization and preliminary crystallographic analysis of
RT   deoxyuridine triphosphate nucleotidohydrolase from Arabidopsis thaliana.";
RL   Acta Crystallogr. F 63:409-411(2007).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RA   Bajaj M., Moriyama H.;
RT   "Structure of dutpase from Arabidopsis thaliana.";
RL   Submitted (FEB-2009) to the PDB data bank.
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, preventing uracil
CC       incorporation into DNA. {ECO:0000269|PubMed:20227352}.
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       Note=Binds 1 Mg(2+) per trimer.;
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17565183}.
CC   -!- MISCELLANEOUS: Silencing of DUT leads to high seedling mortality and
CC       affects plant growth and flower organ morphology in surviving plants.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; AL096859; CAB51171.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78222.1; -; Genomic_DNA.
DR   EMBL; AF370334; AAK44149.1; -; mRNA.
DR   EMBL; AY062989; AAL34163.1; -; mRNA.
DR   PIR; T12954; T12954.
DR   RefSeq; NP_190278.1; NM_114561.4.
DR   PDB; 2PC5; X-ray; 2.20 A; A/B/C=1-166.
DR   PDB; 4OOP; X-ray; 1.50 A; A/B/C=1-166.
DR   PDB; 4OOQ; X-ray; 2.00 A; A/B/C=1-166.
DR   PDBsum; 2PC5; -.
DR   PDBsum; 4OOP; -.
DR   PDBsum; 4OOQ; -.
DR   AlphaFoldDB; Q9STG6; -.
DR   SMR; Q9STG6; -.
DR   BioGRID; 9167; 1.
DR   STRING; 3702.Q9STG6; -.
DR   iPTMnet; Q9STG6; -.
DR   PaxDb; 3702-AT3G46940-1; -.
DR   EnsemblPlants; AT3G46940.1; AT3G46940.1; AT3G46940.
DR   GeneID; 823847; -.
DR   Gramene; AT3G46940.1; AT3G46940.1; AT3G46940.
DR   KEGG; ath:AT3G46940; -.
DR   Araport; AT3G46940; -.
DR   TAIR; AT3G46940; DUT1.
DR   eggNOG; KOG3370; Eukaryota.
DR   HOGENOM; CLU_068508_2_1_1; -.
DR   InParanoid; Q9STG6; -.
DR   PhylomeDB; Q9STG6; -.
DR   BioCyc; ARA:AT3G46940-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G46940-MONOMER; -.
DR   BRENDA; 3.6.1.23; 399.
DR   UniPathway; UPA00610; UER00666.
DR   EvolutionaryTrace; Q9STG6; -.
DR   PRO; PR:Q9STG6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9STG6; baseline and differential.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IMP:TAIR.
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   NCBIfam; TIGR00576; dut; 1.
DR   PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR   PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
DR   Genevisible; Q9STG6; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..166
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000401366"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared between trimeric partners"
FT                   /evidence="ECO:0000269|PubMed:17565183"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   HELIX           89..95
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          97..100
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:2PC5"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          131..141
FT                   /evidence="ECO:0007829|PDB:4OOP"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:4OOP"
SQ   SEQUENCE   166 AA;  17557 MW;  5487738DF4A55BFF CRC64;
     MACVNEPSPK LQKLDRNGIH GDSSPSPFFK VKKLSEKAVI PTRGSPLSAG YDLSSAVDSK
     VPARGKALIP TDLSIAVPEG TYARIAPRSG LAWKHSIDVG AGVIDADYRG PVGVILFNHS
     DADFEVKFGD RIAQLIIEKI VTPDVVEVDD LDETVRGDGG FGSTGV
//