InterPro : IPR010987

Name  Glutathione S-transferase, C-terminal-like Short Name  Glutathione-S-Trfase_C-like
Type  Domain Description  In eukaryotes, glutathione S-transferases (GSTs) participate in the detoxification of reactive electrophillic compounds by catalysing their conjugation to glutathione. GST is found as a domain in S-crystallins from squid, and proteins with no known GST activity, such as eukaryotic elongation factors 1-gamma and the HSP26 family of stress-related proteins, which include auxin-regulated proteins in plants and stringent starvation proteins in Escherichia coli. The major lens polypeptide of cephalopods is also a GST []. Bacterial GSTs of known function often have a specific, growth-supporting role in biodegradative metabolism: epoxide ring opening and tetrachlorohydroquinone reductive dehalogenation are two examples of the reactions catalysed by these bacterial GSTs. Some regulatory proteins, like the stringent starvation proteins, also belong to the GST family []. GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol.Glutathione S-transferases form homodimers, but in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 subunits. The homodimeric enzymes display a conserved structural fold. Each monomer is composed of a distinct N-terminal sub-domain, which adopts the thioredoxin fold, and a C-terminal all-helical sub-domain, which adopts a 4-helical bundle fold. This entry is the C-terminal domain.Glutaredoxin 2 (Grx2), glutathione-dependent disulphide oxidoreductases, is structurally similar to GSTs, even though they lack any sequence similarity. Grx2 is also composed of N and C-terminal subdomains. It is thought that the primary function of Grx2 is to catalyse reversible glutathionylation of proteins with glutathione in cellular redox regulation including the response to oxidative stress. Grx2 is dissimilar to other glutaredoxins apart from containing the conserved active site residues [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR004046 Glutathione S-transferase, C-terminal GST_C Domain
IPR007494 Glutaredoxin 2, C-terminal Glutaredoxin2_C Domain

0 Contains

3 Found In

Id Name Short Name Type
IPR004526 Glutamyl-tRNA synthetase, archaeal/eukaryotic cytosolic Glu-tRNA-synth_arc/euk Family
IPR003083 S-crystallin S-crystallin Family
IPR017410 Mitochondrial outer membrane transport complex protein, metaxin Metaxin Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Fernandes AP Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. 2004 Antioxid Redox Signal 6 63-74
Armstrong RN Structure, catalytic mechanism, and evolution of the glutathione transferases. 1997 Chem Res Toxicol 10 2-18
Vuilleumier S Bacterial glutathione S-transferases: what are they good for? 1997 J Bacteriol 179 1431-41

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)