InterPro : IPR019479

Name  Peroxiredoxin, C-terminal Short Name  Peroxiredoxin_C
Type  Domain Description  This entry represents the C-terminal domain of 1-Cys peroxiredoxin, a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols []. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerisation of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine found upstream of this domain. Glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulphide to the sulphydryl and consequent activation of the enzyme []. The domain is associated with , which carries the catalytic cysteine.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

2 Found In

Id Name Short Name Type
IPR012336 Thioredoxin-like fold Thioredoxin-like_fold Domain
IPR017559 Alkyl hydroperoxide reductase subunit C AhpC Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Choi HJ Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. 1998 Nat Struct Biol 5 400-6
Manevich Y Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. 2004 Proc Natl Acad Sci U S A 101 3780-5



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)