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superoxide dismutase family protein
superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold. (from Pfam)
superoxide dismutase [Cu-Zn] SodC
This HMM describes the Cu,Zn-type superoxide dismutase SodC, found broadly as a periplasmic protein in Proteobacteria. The model includes both SodCI and SodCII of Salmonella, the first of which remains functional and protective after phagocytosis by macrophages and serves as a virulence factor. A disulfide bond-forming pair of Cys residues is invariant is members of this group of Cu,Zn-type superoxide dismutases.
superoxide dismutase [Cu-Zn] SodC2
superoxide dismutase [Cu-Zn] SodC2 eliminates superoxide radicals by catalyzing their conversion into hydrogen peroxide and oxygen
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