This entry contains information that has been generated using an AI language model. Please exercise discretion when interpreting the information provided.
Member database | PANTHER |
PANTHER type | family |
Short name | Thioredoxin_ResA/DsbE_sf AI |
Description
AI-generatedUnreviewed
The thioredoxin family ResA/DsbE subfamily consists of thiol-disulfide oxidoreductases that play a crucial role in the synthesis of c-type cytochromes. Members of this family are involved in reducing disulfide bonds in apocytochrome c, which is a necessary step before heme can be covalently attached. Some proteins within this family may also participate in the formation of disulfide bonds in periplasmic proteins or act as disulfide oxidoreductases in the biogenesis of cytochromes c. Additionally, certain members are implicated in sporulation and redox reactions through reversible oxidation of their active center dithiol to a disulfide, catalyzing dithiol-disulfide exchange reactions.