Thioredoxin family: Thioredoxin Type APR, Thioredoxin Type Clot, Thioredoxin Type CxxS, Thioredoxin Type F, Thioredoxin Type H, Thioredoxin Type Lilium, Thioredoxin Type M, Thioredoxin Type NRX, Thioredoxin Type O, Thioredoxin Type TDX, Thioredoxin Type X, Thioredoxin Type Y and Other Thioredoxin
Pfam: PF02943 Ferredoxin-thioredoxin reductase catalytic beta chain (FeThRed_B)
Ferredoxin thioredoxin reductase catalytic beta subunit
Pyr_redox_2 and PR00469
FAD/NAD-binding_dom; IPR008255 . Pyr_nucl-diS_OxRdtase_2_AS
IPR000103 Pyridine_nuc-diS_OxRdtase_2 and IPR005982
Thioredoxin H and Thioredoxin-like
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.
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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.