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NAD(P)-binding domain-containing protein
FAD-dependent oxidoreductase
This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)
Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. [1]. 8771196. The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution. Zhang Y, Bond CS, Bailey S, Cunningham ML, Fairlamb AH, Hunter WN;. Protein Sci 1996;5:52-61. (from Pfam)
NAD-binding protein
glutathione-disulfide reductase
glutathione-disulfide reductase catalyzes the reduction of glutathione disulfide (GSSG) to form two molecules of glutathione (GSH); functions in the maintenance of high levels of reduced glutathione in the cytosol
The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This HMM represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria.
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