P42769 (GSTF1_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 75.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutathione S-transferase PM239X14 EC=2.5.1.18 Alternative name(s): GST class-phi |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic identifier | 3702 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 218 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | |
| 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 process | Detoxification Stress response |
| Cellular component | Cytoplasm |
| Molecular function | Oxidoreductase Peroxidase Transferase |
| Gene Ontology (GO) | |
| Biological_process | response to stress Inferred from electronic annotation. Source: UniProtKB-KW response to toxinInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | glutathione transferase activity Inferred from electronic annotation. Source: EC peroxidase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 218 | 218 | Glutathione S-transferase PM239X14 | PRO_0000185849 | |||||
Regions | |||||||||
| Domain | 2 – 85 | 84 | GST N-terminal | ||||||
| Domain | 93 – 218 | 126 | GST C-terminal | ||||||
| Region | 12 – 13 | 2 | Glutathione binding By similarity | ||||||
| Region | 41 – 42 | 2 | Glutathione binding By similarity | ||||||
| Region | 55 – 56 | 2 | Glutathione binding By similarity | ||||||
| Region | 69 – 70 | 2 | Glutathione binding By similarity | ||||||
Sequences
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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. |
| IPI | IPI00530259. |
| PIR | S36835. |
3D structure databases | |
| ProteinModelPortal | P42769. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Gene expression databases | |
| Genevestigator | P42769. |
Family and domain databases | |
| Gene3D | 1.20.1050.10. 1 hit. 3.40.30.10. 1 hit. |
| InterPro | IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Pfam | PF00043. GST_C. 1 hit. [Graphical view] |
| SUPFAM | SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit. |
| PROSITE | PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GSTF1_ARATH | ||||||||
| Accession | Primary (citable) accession number: P42769 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
