Q9STG6 (DUT_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from mutant phenotype Ref.4. Source: TAIR dUMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway dUTP metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	dUTP diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 166

166

Deoxyuridine 5'-triphosphate nucleotidohydrolase

PRO_0000401366

Sites

Metal binding

138

1

Magnesium; shared with trimeric partners

Secondary structure

1

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166

Helix Strand Turn

Details...

Beta strand

30 – 35

6

Beta strand

51 – 54

4

Beta strand

59 – 61

3

Beta strand

66 – 76

11

Beta strand

81 – 86

6

Helix

89 – 95

7

Beta strand

97 – 100

4

Beta strand

103 – 105

3

Beta strand

112 – 118

7

Beta strand

120 – 122

3

Beta strand

124 – 126

3

Beta strand

131 – 141

11

Beta strand

145 – 147

3

Sequences

	Sequence		Length	Mass (Da)
	Q9STG6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5487738DF4A55BFF	FASTA	166	17,557
	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

References

	« Hide 'large scale' referencesShow '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. , 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).
+	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.

IPI

IPI00536097.

PIR

T12954.

RefSeq

NP_190278.1. NM_114561.3.

UniGene

At.48742.
At.71138.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9STG6.

SMR

Q9STG6. Positions 26-153.

ModBase

Search...

Protein-protein interaction databases

STRING

3702.AT3G46940.1-P.

Proteomic databases

PaxDb

Q9STG6.

PRIDE

Q9STG6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT3G46940.1; AT3G46940.1; AT3G46940.

GeneID

823847.

KEGG

ath:AT3G46940.

Organism-specific databases

TAIR

At3g46940.

Phylogenomic databases

eggNOG

COG0756.

HOGENOM

HOG000028966.

InParanoid

Q9STG6.

KO

K01520.

OMA

KVCLINH.

PhylomeDB

Q9STG6.

ProtClustDB

PLN02547.

Enzyme and pathway databases

UniPathway

UPA00610; UER00666.

Gene expression databases

Genevestigator

Q9STG6.

Family and domain databases

InterPro

IPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]

PANTHER

PTHR11241. PTHR11241. 1 hit.

Pfam

PF00692. dUTPase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00576. dut. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9STG6.

Entry information

Entry name

DUT_ARATH

Accession

Primary (citable) accession number: Q9STG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 30, 2010
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program