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Q9FQA3 (GST23_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 transferase GST 23

EC=2.5.1.18
Alternative name(s):
Glutathione transferase GST 36
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in multiple disease resistance (MDR). Ref.4

Catalytic activity

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

Miscellaneous

The presence of Asp-179 is significantly associated with a multiple disease resistance.

Sequence similarities

Belongs to the GST superfamily.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Caution

Ref.1 describes GST23 and GST36 as two different members of the GST family but they seem to be allelic variants of the same gene.

Ontologies

Keywords
   Biological processPlant defense
   Molecular functionTransferase
Gene Ontology (GO)
   Biological_processdefense response

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 222222Glutathione transferase GST 23
PRO_0000411116

Regions

Domain4 – 8380GST N-terminal
Domain89 – 220132GST C-terminal
Region67 – 682Glutathione binding By similarity

Sites

Binding site141Glutathione By similarity
Binding site411Glutathione By similarity
Binding site551Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Natural variations

Natural variant1411E → D. Ref.1
Natural variant1791H → D. Ref.1
Natural variant1951L → V. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9FQA3 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: C56E9A67CC4EE9CC

FASTA22224,879
        10         20         30         40         50         60 
MAEKGVKVLG MWASPMVIRV EWALRLKGVE YEYVDEDLAN KSADLLRHNP VTKKVPVLVH 

        70         80         90        100        110        120 
DGKPVAESTI IVEYIDEVWK GGYPIMPGDP YERAQARFWA RFAEDKCNAA LYPIFTATGE 

       130        140        150        160        170        180 
AQRKAVHEAQ QCLKTLETAL EGKKFFGGDA VGYLDIVVGW FAHWLPVIEE VTGASVVTHE 

       190        200        210        220 
ELPLMKAWFG RFLALDVVKA ALPDRDRLLA ANKARREQLL SA 

« Hide

References

« Hide 'large scale' references
[1]"A genomics approach to the comprehensive analysis of the glutathione S-transferase gene family in soybean and maize."
McGonigle B., Keeler S.J., Lau S.M., Koeppe M.K., O'Keefe D.P.
Plant Physiol. 124:1105-1120(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASP-141; ASP-179 AND VAL-195.
[2]"Maize full-length cDNA project."
Yu Y., Currie J., Lomeli R., Angelova A., Collura K., Wissotski M., Campos D., Kudrna D., Golser W., Ashely E., Haller K., Descour A., Fernandes J., Zuccolo A., Soderlund C., Walbot V.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. B73.
[3]"Insights into corn genes derived from large-scale cDNA sequencing."
Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V., Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.
Plant Mol. Biol. 69:179-194(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Multivariate analysis of maize disease resistances suggests a pleiotropic genetic basis and implicates a GST gene."
Wisser R.J., Kolkman J.M., Patzoldt M.E., Holland J.B., Yu J., Krakowsky M., Nelson R.J., Balint-Kurti P.J.
Proc. Natl. Acad. Sci. U.S.A. 108:7339-7344(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF244688 mRNA. Translation: AAG34831.1.
AF244701 mRNA. Translation: AAG34844.1.
BT040471 mRNA. Translation: ACF85476.1.
EU963788 mRNA. Translation: ACG35906.1.
RefSeqNP_001104994.1. NM_001111524.1.
UniGeneZm.561.

3D structure databases

ProteinModelPortalQ9FQA3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID541845.
KEGGzma:541845.

Organism-specific databases

GrameneQ9FQA3.
MaizeGDB452083.
542096.

Phylogenomic databases

HOGENOMHOG000125749.
KOK00799.

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 nameGST23_MAIZE
AccessionPrimary (citable) accession number: Q9FQA3
Secondary accession number(s): Q9FQB6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 73 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