Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9ZRT5 (GSTT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Glutathione S-transferase T1

Short name=AtGSTT1
EC=2.5.1.18
Alternative name(s):
GST class-theta member 1
Glutathione S-transferase 10
Gene names
Name:GSTT1
Synonyms:GST10
Ordered Locus Names:At5g41210
ORF Names:MEE6.28
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrobenzyl chloride (pNBC), and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides. Ref.5

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

Subcellular location

Nucleus Ref.6.

Sequence similarities

Belongs to the GST superfamily. Theta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Biological processDetoxification
   Cellular componentNucleus
   Molecular functionOxidoreductase
Peroxidase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to toxic substance

Inferred from electronic annotation. Source: UniProtKB-KW

toxin catabolic process

Traceable author statement Ref.5. Source: TAIR

   Cellular_componentcytoplasm

Non-traceable author statement Ref.5. Source: TAIR

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

peroxisome

Inferred from direct assay PubMed 17951448. Source: TAIR

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Glutathione S-transferase T1
PRO_0000413574

Regions

Domain2 – 8382GST N-terminal
Domain90 – 233144GST C-terminal
Region12 – 132Glutathione binding By similarity
Region41 – 422Glutathione binding By similarity
Region54 – 552Glutathione binding By similarity
Region67 – 682Glutathione binding By similarity
Motif243 – 2453Microbody targeting signal Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZRT5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 6F16FE1399E793B7

FASTA24527,653
        10         20         30         40         50         60 
MMKLKVYADR MSQPSRAVII FCKVNGIQFD EVLISLAKRQ QLSPEFKDIN PLGKVPAIVD 

        70         80         90        100        110        120 
GRLKLFESHA ILIYLSSAFP SVADHWYPND LSKRAKIHSV LDWHHTNLRR GAAGYVLNSV 

       130        140        150        160        170        180 
LGPALGLPLN PKAAAEAEQL LTKSLSTLET FWLKGNAKFL LGSNQPSIAD LSLVCELMQL 

       190        200        210        220        230        240 
QVLDDKDRLR LLSTHKKVEQ WIENTKKATM PHFDETHEIL FKVKEGFQKR REMGTLSKPG 


LQSKI 

« Hide

References

« Hide 'large scale' references
[1]"Identification and cloning of AtGST 10, members of a novel type of plant glutathione transferases."
Dixon D.P., Cole D.J., Edwards R.
Plant Gene Register PGR99-053
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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.
[5]"Probing the diversity of the Arabidopsis glutathione S-transferase gene family."
Wagner U., Edwards R., Dixon D.P., Mauch F.
Plant Mol. Biol. 49:515-532(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, GENE FAMILY, NOMENCLATURE.
Strain: cv. Columbia.
[6]"Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily."
Dixon D.P., Hawkins T., Hussey P.J., Edwards R.
J. Exp. Bot. 60:1207-1218(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ131580 mRNA. Translation: CAA10457.1.
AB010072 Genomic DNA. Translation: BAB09723.1.
CP002688 Genomic DNA. Translation: AED94654.1.
AY054659 mRNA. Translation: AAK96850.1.
AY072466 mRNA. Translation: AAL66881.1.
PIRT51594.
RefSeqNP_198937.1. NM_123486.3.
UniGeneAt.24905.

3D structure databases

ProteinModelPortalQ9ZRT5.
SMRQ9ZRT5. Positions 2-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid19374. 2 interactions.
IntActQ9ZRT5. 1 interaction.
STRING3702.AT5G41210.1-P.

Proteomic databases

PaxDbQ9ZRT5.
PRIDEQ9ZRT5.

Protocols and materials databases

DNASU834123.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G41210.1; AT5G41210.1; AT5G41210.
GeneID834123.
KEGGath:AT5G41210.

Organism-specific databases

TAIRAT5G41210.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125747.
InParanoidQ9ZRT5.
KOK00799.
OMAHTNLRRG.
PhylomeDBQ9ZRT5.

Enzyme and pathway databases

BioCycARA:AT5G41210-MONOMER.

Gene expression databases

GenevestigatorQ9ZRT5.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSTT1_ARATH
AccessionPrimary (citable) accession number: Q9ZRT5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: May 1, 1999
Last modified: June 11, 2014
This is version 96 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names