Glutathione S-transferases Phi, C-terminal (IPR034347)

Short name: GST_Phi_C

Overlapping homologous superfamilies

Domain relationships


This entry represents the C-terminal alpha helical domain found in the Phi subfamily (also known as GSTF) of the glutathione S-transferase (GST) family. GSTF had long been regarded as plant specific but has also been found in basidiomycete fungi [PMID: 25566286].

The class Phi GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau GSTs, respectively [PMID: 16399386, PMID: 11897031]. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides [PMID: 9417936]. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole and shoot regeneration [PMID: 15012285, PMID: 25566286].

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. 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: 11695986].

Contributing signatures

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