Detail Information for IndEnz0018001027
IED ID IndEnz0018001027
Enzyme Type ID peroxidase001027
Protein Name Glutathione S-transferase F9
AtGSTF9
EC 2.5.1.18
AtGSTF7
GST class-phi member 9
Gene Name GSTF9 GLUTTR GSTF7 Phi9 At2g30860 F7F1.7
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MVLKVYGPHFASPKRALVTLIEKGVAFETIPVDLMKGEHKQPAYLALQPFGTVPAVVDGDYKIFESRAVMRYVAEKYRSQGPDLLGKTVEDRGQVEQWLDVEATTYHPPLLNLTLHIMFASVMGFPSDEKLIKESEEKLAGVLDVYEAHLSKSKYLAGDFVSLADLAHLPFTDYLVGPIGKAYMIKDRKHVSAWWDDISSRPAWKETVAKYSFPA
Enzyme Length 215
Uniprot Accession Number O80852
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Redox-regulated enzyme; in oxidative stress conditions methionine oxidation ensure a thermodynamic and structural compensatory mechanism to guarantee H(2)O(2) peroxidase activity despite transferase activity inhibition. {ECO:0000269|PubMed:29732642}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:16538523};
DNA Binding
EC Number 2.5.1.18
Enzyme Function FUNCTION: In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC), and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides. {ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:16538523}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Beta strand (6); Chain (1); Domain (2); Frameshift (1); Helix (13); Modified residue (5); Region (4); Sequence conflict (2); Turn (3)
Keywords 3D-structure;Alternative splicing;Cytoplasm;Detoxification;Oxidation;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Stress response;Transferase
Interact With
Induction INDUCTION: By zinc in roots and benoxacor. {ECO:0000269|PubMed:16538523, ECO:0000269|PubMed:19880396}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
Modified Residue MOD_RES 12; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19376835; MOD_RES 35; /note=Methionine sulfoxide; /evidence=ECO:0000269|PubMed:29732642; MOD_RES 118; /note=Methionine sulfoxide; /evidence=ECO:0000269|PubMed:29732642; MOD_RES 123; /note=Methionine sulfoxide; /evidence=ECO:0000269|PubMed:29732642; MOD_RES 184; /note=Methionine sulfoxide; /evidence=ECO:0000269|PubMed:29732642
Post Translational Modification PTM: Oxidated at Met-35, Met-118, Met-123 and Met-184 in oxidative stress conditions (e.g. hydrogen peroxide H(2)O(2)). {ECO:0000269|PubMed:29732642}.
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 6EZY; 6F01; 6F05;
Mapped Pubmed ID 10785664; 11826309; 14535880; 15159623; 15539469; 15971193; 16526091; 16648217; 17028151; 17644812; 18431481; 18485061; 18538804; 18633119; 19067976; 19174456; 20005002; 20018591; 20377703; 20405473; 20442276; 23281391; 23289948; 23661340; 26616373; 28627464; 29165718; 31870857;
Motif
Gene Encoded By
Mass 24,146
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=71 uM for glutathione (in oxidative conditions) {ECO:0000269|PubMed:29732642}; KM=131 uM for glutathione (in reductive conditions) {ECO:0000269|PubMed:29732642}; KM=1.8 mM for 1-chloro-2,4-dinitrobenzene (in oxidative conditions) {ECO:0000269|PubMed:29732642}; KM=1.3 mM for 1-chloro-2,4-dinitrobenzene (in reductive conditions) {ECO:0000269|PubMed:29732642}; Note=kcat is 0.5 sec(-1) with glutathione as substrate (in oxidative conditions) (PubMed:29732642). kcat is 0.85 sec(-1) with glutathione as substrate (in reductive conditions) (PubMed:29732642). kcat is 0.72 sec(-1) with 1-chloro-2,4-dinitrobenzene as substrate (in oxidative conditions) (PubMed:29732642). kcat is 0.98 sec(-1) with 1-chloro-2,4-dinitrobenzene as substrate (in reductive conditions) (PubMed:29732642). {ECO:0000269|PubMed:29732642};
Metal Binding
Rhea ID RHEA:16437
Cross Reference Brenda