Ferredoxin-thioredoxin reductase Pfam: PF02943 Ferredoxin-thioredoxin reductase catalytic beta chain (FeThRed_B) Interpro: IPR004209
Ferredoxin thioredoxin reductase catalytic beta subunit
Pyr_redox_2 and PR00469
PNDRDTASEII Interpro: IPR023753
FAD/NAD-binding_dom; IPR008255 . Pyr_nucl-diS_OxRdtase_2_AS
IPR000103 Pyridine_nuc-diS_OxRdtase_2 and IPR005982
Thioredoxin H and Thioredoxin-like Pfam: PF00085
Thioredoxin Interpro: IPR005746
Thioredoxin-like_fold and IPR013766
Thioredoxin is a class of small redox proteins known to be present in all organisms. It plays a role in many important biological processes, including redox signaling.
In humans, it is encoded by the TXN gene. Loss-of-function mutation of either of the two human thioredoxin genes is lethal at the four-cell stage of the developing embryo. Although not entirely understood, thioredoxin plays a central role in humans and is increasingly linked to medicine through their response to reactive oxygen species (ROS).
In plants, thioredoxins regulate a spectrum of critical functions, ranging from photosynthesis to growth, flowering and the development and germination of seeds. It has also recently been found to play a role in cell-to-cell communication.
Lu J, Holmgren A. The thioredoxin superfamily in oxidative protein folding. Antioxid Redox Signal. 2014 Jul 20;21(3):457-70. PMID: 24483600
Lemaire SD, Miginiac-Maslow M. The thioredoxin superfamily in Chlamydomonas reinhardtii. Photosynth Res. 2004;82(3):203-20.PMID:16143836
Holmgren A, Gleason FK (1988). Thioredoxin and related proteins in procaryotes. FEMS Microbiol. Rev. 4 (4): 271-297.PMID 3152490.
Holmgren A (1988). Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulfide bonds. Biochem. Soc. Trans. 16 (2): 95-96. PMID 3286320.
Holmgren A (1989). Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264 (24): 13963-13966. PMID 2668278.