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P42769 (GSTF1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. 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 PM239X14

EC=2.5.1.18
Alternative name(s):
GST class-phi
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Specifically catalyzes the conjugation of synthetic 1-chloro-2,4-ditrobenzene to GSH. Also functions as a glutathione peroxidase, converting linoleate oxidation products into their corresponding hydroxyacids. This enzyme may thus serve to protect the cell from oxygen toxicity as well as from exogenous toxins such as herbicides. Ref.1

Catalytic activity

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

Subcellular location

Cytoplasmcytosol Probable.

Tissue specificity

Expressed in vegetative rosettes.

Developmental stage

Expressed up until the first flowering buds, after which, levels dramatically decrease.

Sequence similarities

Belongs to the GST superfamily. Phi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Caution

This protein probably does not originate from A.thaliana, rather it resemble fungal GTSs.

Ontologies

Keywords
   Biological processDetoxification
Stress response
   Cellular componentCytoplasm
   Molecular functionOxidoreductase
Peroxidase
Transferase
Gene Ontology (GO)
   Biological_processresponse to stress

Inferred from electronic annotation. Source: UniProtKB-KW

response to toxic substance

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 218218Glutathione S-transferase PM239X14
PRO_0000185849

Regions

Domain2 – 8584GST N-terminal
Domain93 – 218126GST C-terminal
Region12 – 132Glutathione binding By similarity
Region41 – 422Glutathione binding By similarity
Region55 – 562Glutathione binding By similarity
Region69 – 702Glutathione binding By similarity

Sequences

Sequence LengthMass (Da)Tools
P42769 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C7E6B6EC5320C33A

FASTA21824,364
        10         20         30         40         50         60 
MVTVKLYGMA YSTCTKRVYT TAKEIGVDVK IVPVDLMKGE HKEPAYLDNY HPFGVIPVLE 

        70         80         90        100        110        120 
DEDGTKIYES RAISRYLVAK YGKGSSLLPS PSDPKAYGLF EQAASVEYSS FDPPASSLAY 

       130        140        150        160        170        180 
ERVFAGMRGL KTNEELAKKY VDTLNAKMDG YERILSKQKY LAGNDFTLAD LFHLPYGAMV 

       190        200        210 
AQLEPTVLDS KPHVKAWWAA SLRVIPGRLL RNSSKEFM 

« Hide

References

[1]"A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana. Molecular cloning and functional characterization."
Bartling D., Radzio R., Steiner U., Weiler E.W.
Eur. J. Biochem. 216:579-586(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: cv. Landsberg erecta.
Tissue: Leaf.
[2]Erratum
Bartling D., Radzio R., Steiner U., Weiler E.W.
Eur. J. Biochem. 218:1096-1096(1993)
[3]"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: GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68304 mRNA. Translation: CAA48376.1.
PIRS36835.

3D structure databases

ProteinModelPortalP42769.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Gene expression databases

GenevestigatorP42769.

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.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 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 nameGSTF1_ARATH
AccessionPrimary (citable) accession number: P42769
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 80 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