Detail Information for IndEnz0018000533
IED ID IndEnz0018000533
Enzyme Type ID peroxidase000533
Protein Name Glutathione S-transferase A4
EC 2.5.1.18
GST A4-4
GSTA4-4
GST class-alpha member 4
Glutathione S-transferase 5.7
GST 5.7
Gene Name Gsta4 Gsta
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAAKPKLYYFNGRGRMESIRWLLAAAGVEFEEEFLETREQYEKMQKDGHLLFGQVPLVEIDGMMLTQTRAILSYLAAKYNLYGKDLKERVRIDMYADGTQDLMMMIAVAPFKTPKEKEESYDLILSRAKTRYFPVFEKILKDHGEAFLVGNQLSWADIQLLEAILMVEELSAPVLSDFPLLQAFKTRISNIPTIKKFLQPGSQRKPPPDGPYVEVVRTVLKF
Enzyme Length 222
Uniprot Accession Number P24472
Absorption
Active Site
Activity Regulation
Binding Site BINDING 9; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P13745
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:10508391};
DNA Binding
EC Number 2.5.1.18
Enzyme Function FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000269|PubMed:10508391}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (7); Binding site (1); Chain (1); Domain (2); Helix (12); Modified residue (1); Natural variant (3); Region (2); Sequence conflict (3); Turn (2)
Keywords 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Reference proteome;Transferase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm.
Modified Residue MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P14942
Post Translational Modification PTM: The N-terminus is blocked.
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 1B48; 1GUK;
Mapped Pubmed ID 11217851; 11326268; 11851347; 11884396; 12020353; 12466851; 12646569; 12904583; 14595844; 14610273; 14681479; 14761685; 15629866; 15831471; 16223495; 16325481; 16466397; 18311940; 18799693; 18930016; 18973680; 19482077; 19880816; 20150287; 20404090; 20832906; 20966433; 21267068; 22038048; 22323595; 22711583; 22881716; 23690225; 25501545; 26010708; 26654979; 27065323; 27133129; 27626380; 27998724; 29127112; 29708596; 31515474; 32044382; 7904605; 9806360;
Motif
Gene Encoded By
Mass 25,564
Kinetics
Metal Binding
Rhea ID RHEA:16437
Cross Reference Brenda 2.5.1.18;