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A2XMN2 (GSTU1_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 39. 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:
Probable glutathione S-transferase GSTU1

EC=2.5.1.18
Gene names
Name:GSTU1
Synonyms:GST1
ORF Names:OsI_013325
OrganismOryza sativa subsp. indica (Rice)
Taxonomic identifier39946 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activity

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

Sequence similarities

Belongs to the GST superfamily. Tau family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Molecular functionTransferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processresponse to cadmium ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 231231Probable glutathione S-transferase GSTU1
PRO_0000295653

Regions

Domain5 – 8480GST N-terminal
Domain97 – 220124GST C-terminal
Region68 – 692Glutathione binding By similarity

Sites

Binding site151Glutathione By similarity
Binding site421Glutathione By similarity
Binding site561Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Experimental info

Sequence conflict881S → P in AAC05216. Ref.1
Sequence conflict901A → G in AAC05216. Ref.1
Sequence conflict991Y → F in AAC05216. Ref.1
Sequence conflict1301Q → H in AAC05216. Ref.1
Sequence conflict175 – 1795WFYSY → CSTAT in AAC05216. Ref.1
Sequence conflict2011C → R in AAC05216. Ref.1
Sequence conflict2081A → V in AAC05216. Ref.1

Secondary structure

.................................... 231
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A2XMN2 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 42C953E8F540DAB0

FASTA23125,832
        10         20         30         40         50         60 
MAEEKELVLL DFWVSPFGQR CRIAMAEKGL EFEYREEDLG NKSDLLLRSN PVHRKIPVLL 

        70         80         90        100        110        120 
HAGRPVSESL VILQYLDDAF PGTPHLLSPA NSGDADAAYA RATARFWADY VDRKLYDCGS 

       130        140        150        160        170        180 
RLWRLKGEPQ AAAGREMAEI LRTLEAELGD REFFGGGGGG RLGFVDVALV PFTAWFYSYE 

       190        200        210        220        230 
RCGGFSVEEV APRLAAWARR CGRIDSVAKH LPSPEKVYDF VGVLKKKYGV E 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of rice glutathione S-transferase."
Yun C.-H., Lee M.C., Park J.H., Eun M.Y.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Milyang 23.
[2]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. 93-11.
[3]"Organisation and structural evolution of the rice glutathione S-transferase gene family."
Soranzo N., Sari Gorla M., Mizzi L., De Toma G., Frova C.
Mol. Genet. Genomics 271:511-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF050102 mRNA. Translation: AAC05216.1.
CM000128 Genomic DNA. Translation: EAY92092.1.
PIRT02765.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OYJX-ray1.95A/B/C/D1-231[»]
ProteinModelPortalA2XMN2.
SMRA2XMN2. Positions 2-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING39947.LOC_Os03g57200.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneA2XMN2.

Phylogenomic databases

eggNOGNOG245965.
HOGENOMHOG000125749.

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]
PfamPF13417. 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 nameGSTU1_ORYSI
AccessionPrimary (citable) accession number: A2XMN2
Secondary accession number(s): O65032
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 39 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references