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Protein

Glutathione S-transferase 4

Gene

GST4

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides. Most active with substrates possessing a chloroacetamide structure. Trans-cinnamic acid and 1-chloro-2,4-dinitrobenzene are not effective substrates. May play an important role in the benoxacor-mediated protection of maize from metolachlor injury.

Catalytic activityi

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

pH dependencei

Optimum pH is 7.5-8. Active from pH 6 to 9.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141GlutathioneBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 4 (EC:2.5.1.18)
Alternative name(s):
GST class-phi member 4
GST-27
GST-IV
Gene namesi
Name:GST4
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305: Chromosome 10

Organism-specific databases

GrameneiP46420.
MaizeGDBi113242.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 223222Glutathione S-transferase 4PRO_0000185843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Blocked amino end (Ala)

Proteomic databases

PRIDEiP46420.

Expressioni

Tissue specificityi

Seedling roots.

Inductioni

By herbicides.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP46420.
SMRiP46420. Positions 6-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8582GST N-terminalAdd
BLAST
Domaini90 – 223134GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 442Glutathione bindingBy similarity
Regioni56 – 572Glutathione bindingBy similarity
Regioni69 – 702Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Phi family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

HOGENOMiHOG000125746.
KOiK00799.
OMAiDERPHVK.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46420-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPAVKVYG WAISPFVSRA LLALEEAGVD YELVPMSRQD GDHRRPEHLA
60 70 80 90 100
RNPFGKVPVL EDGDLTLFES RAIARHVLRK HKPELLGGGR LEQTAMVDVW
110 120 130 140 150
LEVEAHQLSP PAIAIVVECV FAPFLGRERN QAVVDENVEK LKKVLEVYEA
160 170 180 190 200
RLATCTYLAG DFLSLADLSP FTIMHCLMAT EYAALVHALP HVSAWWQGLA
210 220
ARPAANKVAQ FMPVGAGAPK EQE
Length:223
Mass (Da):24,570
Last modified:January 23, 2007 - v2
Checksum:i24235245AFB4A403
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79515 mRNA. Translation: CAA56047.1.
U12679 mRNA. Translation: AAA20585.1.
PIRiS52037.
RefSeqiNP_001105366.1. NM_001111896.1.
UniGeneiZm.17839.

Genome annotation databases

EnsemblPlantsiGRMZM2G132093_T01; GRMZM2G132093_P01; GRMZM2G132093.
GeneIDi542311.
KEGGizma:542311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79515 mRNA. Translation: CAA56047.1.
U12679 mRNA. Translation: AAA20585.1.
PIRiS52037.
RefSeqiNP_001105366.1. NM_001111896.1.
UniGeneiZm.17839.

3D structure databases

ProteinModelPortaliP46420.
SMRiP46420. Positions 6-212.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP46420.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiGRMZM2G132093_T01; GRMZM2G132093_P01; GRMZM2G132093.
GeneIDi542311.
KEGGizma:542311.

Organism-specific databases

GrameneiP46420.
MaizeGDBi113242.

Phylogenomic databases

HOGENOMiHOG000125746.
KOiK00799.
OMAiDERPHVK.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV."
    Jepson I., Lay V.J., Holt D.C., Bright S.W.J., Greenland A.J.
    Plant Mol. Biol. 26:1855-1866(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. UE95.
    Tissue: Seedling root.
  2. "A cDNA clone encoding the 27-kilodalton subunits of glutathione S-transferase IV from Zea mays."
    Irzyk G.P., Potter S., Ward E., Fuerst E.P.
    Plant Physiol. 107:311-312(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Pioneer hybrid 3906.
  3. "Purification and characterization of a glutathione S-transferase from benoxacor-treated maize (Zea mays)."
    Irzyk G.P., Fuerst E.P.
    Plant Physiol. 102:803-810(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.

Entry informationi

Entry nameiGSTF4_MAIZE
AccessioniPrimary (citable) accession number: P46420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.