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Q9STG6 (DUT_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase

Short name=dUTPase
EC=3.6.1.23
Alternative name(s):
dUTP pyrophosphatase
dUTP-pyrophosphatase-like 1
Short name=AtDUT1
Gene names
Name:DUT
Synonyms:DUT1
Ordered Locus Names:At3g46940
ORF Names:T6H20.30
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length166 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4

Catalytic activity

dUTP + H2O = dUMP + diphosphate.

Cofactor

Binds 1 magnesium per trimer.

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.

Subunit structure

Homotrimer. Ref.5

Miscellaneous

Silencing of DUT leads to high seedling mortality and affects plant growth and flower organ morphology in surviving plants.

Sequence similarities

Belongs to the dUTPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 166166Deoxyuridine 5'-triphosphate nucleotidohydrolase
PRO_0000401366

Sites

Metal binding1381Magnesium; shared with trimeric partners

Secondary structure

........................... 166
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9STG6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 5487738DF4A55BFF

FASTA16617,557
        10         20         30         40         50         60 
MACVNEPSPK LQKLDRNGIH GDSSPSPFFK VKKLSEKAVI PTRGSPLSAG YDLSSAVDSK 

        70         80         90        100        110        120 
VPARGKALIP TDLSIAVPEG TYARIAPRSG LAWKHSIDVG AGVIDADYRG PVGVILFNHS 

       130        140        150        160 
DADFEVKFGD RIAQLIIEKI VTPDVVEVDD LDETVRGDGG FGSTGV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"The SOS screen in Arabidopsis: a search for functions involved in DNA metabolism."
Siaud N., Dubois E., Massot S., Richaud A., Dray E., Collier J., Doutriaux M.P.
DNA Repair 9:567-578(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase from Arabidopsis thaliana."
Bajaj M., Moriyama H.
Acta Crystallogr. F 63:409-411(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, SUBUNIT.
[6]"Structure of dutpase from Arabidopsis thaliana."
Bajaj M., Moriyama H.
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL096859 Genomic DNA. Translation: CAB51171.1.
CP002686 Genomic DNA. Translation: AEE78222.1.
AF370334 mRNA. Translation: AAK44149.1.
AY062989 mRNA. Translation: AAL34163.1.
PIRT12954.
RefSeqNP_190278.1. NM_114561.3.
UniGeneAt.48742.
At.71138.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P9OX-ray2.00A/B/C1-166[»]
2PC5X-ray2.20A/B/C1-166[»]
ProteinModelPortalQ9STG6.
SMRQ9STG6. Positions 26-153.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G46940.1-P.

Proteomic databases

PaxDbQ9STG6.
PRIDEQ9STG6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G46940.1; AT3G46940.1; AT3G46940.
GeneID823847.
KEGGath:AT3G46940.

Organism-specific databases

TAIRAT3G46940.

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028966.
InParanoidQ9STG6.
KOK01520.
OMALVDTQIS.
PhylomeDBQ9STG6.
ProtClustDBPLN02547.

Enzyme and pathway databases

BioCycARA:AT3G46940-MONOMER.
MetaCyc:AT3G46940-MONOMER.
UniPathwayUPA00610; UER00666.

Gene expression databases

GenevestigatorQ9STG6.

Family and domain databases

InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9STG6.
PROQ9STG6.

Entry information

Entry nameDUT_ARATH
AccessionPrimary (citable) accession number: Q9STG6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names