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Q9STG6

- DUT_ARATH

UniProt

Q9STG6 - DUT_ARATH

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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

DUT

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

dUTP + H2O = dUMP + diphosphate.

Cofactori

Mg2+Note: Binds 1 Mg(2+) per trimer.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi138 – 1381Magnesium; shared with trimeric partners1 Publication

GO - Molecular functioni

  1. dUTP diphosphatase activity Source: UniProtKB-EC
  2. identical protein binding Source: UniProtKB
  3. magnesium ion binding Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: TAIR
  2. dUMP biosynthetic process Source: UniProtKB-UniPathway
  3. dUTP metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G46940-MONOMER.
MetaCyc:AT3G46940-MONOMER.
ReactomeiREACT_263273. Pyrimidine biosynthesis.
UniPathwayiUPA00610; UER00666.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC:3.6.1.23)
Short name:
dUTPase
Alternative name(s):
dUTP pyrophosphatase
dUTP-pyrophosphatase-like 1
Short name:
AtDUT1
Gene namesi
Name:DUT
Synonyms:DUT1
Ordered Locus Names:At3g46940
ORF Names:T6H20.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G46940.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 166166Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000401366Add
BLAST

Proteomic databases

PaxDbiQ9STG6.
PRIDEiQ9STG6.

Expressioni

Gene expression databases

GenevestigatoriQ9STG6.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

STRINGi3702.AT3G46940.1-P.

Structurei

Secondary structure

1
166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 356Combined sources
Beta strandi51 – 544Combined sources
Beta strandi59 – 613Combined sources
Beta strandi66 – 7611Combined sources
Beta strandi81 – 866Combined sources
Helixi89 – 957Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi103 – 1053Combined sources
Beta strandi112 – 1187Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi131 – 14111Combined sources
Beta strandi145 – 1473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P9OX-ray2.00A/B/C1-166[»]
2PC5X-ray2.20A/B/C1-166[»]
ProteinModelPortaliQ9STG6.
SMRiQ9STG6. Positions 26-153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9STG6.

Family & Domainsi

Sequence similaritiesi

Belongs to the dUTPase family.Curated

Phylogenomic databases

eggNOGiCOG0756.
HOGENOMiHOG000028966.
KOiK01520.
OMAiFERFDRI.
PhylomeDBiQ9STG6.

Family and domain databases

Gene3Di2.70.40.10. 1 hit.
InterProiIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR008181. dUTPase_1.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR00576. dut. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9STG6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MACVNEPSPK LQKLDRNGIH GDSSPSPFFK VKKLSEKAVI PTRGSPLSAG
60 70 80 90 100
YDLSSAVDSK VPARGKALIP TDLSIAVPEG TYARIAPRSG LAWKHSIDVG
110 120 130 140 150
AGVIDADYRG PVGVILFNHS DADFEVKFGD RIAQLIIEKI VTPDVVEVDD
160
LDETVRGDGG FGSTGV
Length:166
Mass (Da):17,557
Last modified:May 1, 2000 - v1
Checksum:i5487738DF4A55BFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096859 Genomic DNA. Translation: CAB51171.1.
CP002686 Genomic DNA. Translation: AEE78222.1.
AF370334 mRNA. Translation: AAK44149.1.
AY062989 mRNA. Translation: AAL34163.1.
PIRiT12954.
RefSeqiNP_190278.1. NM_114561.3.
UniGeneiAt.48742.
At.71138.

Genome annotation databases

EnsemblPlantsiAT3G46940.1; AT3G46940.1; AT3G46940.
GeneIDi823847.
KEGGiath:AT3G46940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096859 Genomic DNA. Translation: CAB51171.1 .
CP002686 Genomic DNA. Translation: AEE78222.1 .
AF370334 mRNA. Translation: AAK44149.1 .
AY062989 mRNA. Translation: AAL34163.1 .
PIRi T12954.
RefSeqi NP_190278.1. NM_114561.3.
UniGenei At.48742.
At.71138.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2P9O X-ray 2.00 A/B/C 1-166 [» ]
2PC5 X-ray 2.20 A/B/C 1-166 [» ]
ProteinModelPortali Q9STG6.
SMRi Q9STG6. Positions 26-153.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT3G46940.1-P.

Proteomic databases

PaxDbi Q9STG6.
PRIDEi Q9STG6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G46940.1 ; AT3G46940.1 ; AT3G46940 .
GeneIDi 823847.
KEGGi ath:AT3G46940.

Organism-specific databases

TAIRi AT3G46940.

Phylogenomic databases

eggNOGi COG0756.
HOGENOMi HOG000028966.
KOi K01520.
OMAi FERFDRI.
PhylomeDBi Q9STG6.

Enzyme and pathway databases

UniPathwayi UPA00610 ; UER00666 .
BioCyci ARA:AT3G46940-MONOMER.
MetaCyc:AT3G46940-MONOMER.
Reactomei REACT_263273. Pyrimidine biosynthesis.

Miscellaneous databases

EvolutionaryTracei Q9STG6.
PROi Q9STG6.

Gene expression databases

Genevestigatori Q9STG6.

Family and domain databases

Gene3Di 2.70.40.10. 1 hit.
InterProi IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR008181. dUTPase_1.
[Graphical view ]
Pfami PF00692. dUTPase. 1 hit.
[Graphical view ]
SUPFAMi SSF51283. SSF51283. 1 hit.
TIGRFAMsi TIGR00576. dut. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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).

Entry informationi

Entry nameiDUT_ARATH
AccessioniPrimary (citable) accession number: Q9STG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3