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Reviewed, UniProtKB/Swiss-Prot P12653 (GSTF1_MAIZE)

Last modified January 19, 2010. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glutathione S-transferase 1
    EC=2.5.1.18
Alternative name(s):
    GST-I
    GST-29
    GST class-phi member 1
Gene names
Name: GST1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea

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Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides.

Catalytic activity

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

Subunit structure

Homodimer or heterodimer of GST-I and GST-IV (=GST-II).

Tissue specificity

Expressed in the stem and leaves, lower levels are seen in the pollen and endosperm.

Sequence similarities

Belongs to the GST superfamily. Phi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

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Ontologies

Keywords
   Molecular functionTransferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular functionglutathione transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 214213Glutathione S-transferase 1
PRO_0000185841

Regions

Domain2 – 8382GST N-terminal
Domain88 – 214127GST C-terminal

Experimental info

Sequence conflict151L → V in AAA33470. Ref.2
Sequence conflict151L → V in AAA33469. Ref.2

Secondary structure

1 ........................................ 214
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P12653-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 97DA6337ADF03CB1

FASTA21423,822
        10         20         30         40         50         60 
MAPMKLYGAV MSWNLTRCAT ALEEAGSDYE IVPINFATAE HKSPEHLVRN PFGQVPALQD 

        70         80         90        100        110        120 
GDLYLFESRA ICKYAARKNK PELLREGNLE EAAMVDVWIE VEANQYTAAL NPILFQVLIS 

       130        140        150        160        170        180 
PMLGGTTDQK VVDENLEKLK KVLEVYEARL TKCKYLAGDF LSLADLNHVS VTLCLFATPY 

       190        200        210 
ASVLDAYPHV KAWWSGLMER PSVQKVAALM KPSA

« Hide

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References

[1]"Characterization and heterospecific expression of cDNA clones of genes in the maize GSH S-transferase multigene family."
Grove G., Zarlengo R.P., Timmerman K.P., Li N.-Q., Tam M.F., Tu C.-P.D.
Nucleic Acids Res. 16:425-438(1988) [PubMed: 3277162] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structural analysis of a maize gene coding for glutathione-S-transferase involved in herbicide detoxification."
Shah D.M., Hironaka C.M., Wiegand R.C., Harding E.I., Krivi G.G., Tiemeier D.C.
Plant Mol. Biol. 6:203-211(1986) [Agricola: IND86033490]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Messenger RNA encoding a glutathione-S-transferase responsible for herbicide tolerance in maize is induced in response to safener treatment."
Wiegand R.C., Shah D.M., Mozer T.J., Harding E.I., Diaz-Collier J., Saunders C., Jaworski E.G., Tiemeier D.C.
Plant Mol. Biol. 7:235-243(1986) [Agricola: IND87010820]
Cited for: PROTEIN SEQUENCE OF 2-16.
[4]"Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism."
Neuefeind T., Huber R., Dasenbrock H., Prade L., Bieseler B.
J. Mol. Biol. 274:446-453(1997) [PubMed: 9417926] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]"Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase -- explanations for the selectivity of the enzyme in plants."
Prade L., Huber R., Bieseler B.
Structure 6:1445-1452(1998) [PubMed: 9817846] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X06754 mRNA. Translation: CAA29928.1.
M16901 mRNA. Translation: AAA33470.1.
M16902, M16900 Genomic DNA. Translation: AAA33469.1.
PIRXUZM1. S03726.
RefSeqNP_001105412.1.
UniGeneZm.9

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXDX-ray2.50A/B2-210[»]
1BYEX-ray2.80A/B/C/D2-214[»]
ModBaseSearch...

Proteomic databases

PRIDEP12653.

Genome annotation databases

GeneID542366.
KEGGzma:542366.

Organism-specific databases

GrameneP12653.
MaizeGDB65344.

Enzyme and pathway databases

BRENDA2.5.1.18. 289.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGSTF1_MAIZE
AccessionPrimary (citable) accession number: P12653
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 78 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents