Glutathione S-transferases, subfamily 4, C-terminal (IPR034338)

Short name: GST_4_C

Overlapping homologous superfamilies

Domain relationships


Glutathione S-transferases (GSTs) are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain [PMID: 15822171].

This entry represents the C-terminal alpha helical domain found in subfamily 4 of GST. This subfamily represents a group of mostly uncharacterised bacterial proteins with similarity to GSTs, including YfcF from Escherichia coli. YfcF is reported to have GSH-conjugating activity toward 1-chloro-2,4-dinitorobenzene and GSH-dependent peroxidase activity toward cumene hydroperoxide. It is believe to be important for defense against oxidative stress [PMID: 17018556].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.