cd00305: Cu-Zn_SOD1-like (This model is not part of the current CDD release)
copper/zinc superoxide dismutase SOD1 and similar proteins
This subfamily represents copper/zinc superoxide dismutase SOD1 and similar proteins. Superoxide dismutases catalyze the conversion of superoxide radicals to 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 causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Mature SOD1 is a stable homodimer containing a catalytic Cu(II) ion and a Zn(II) ion with a structural role that increases enzyme stability. The presence of an invariant disulfide bond further stabilizes the protein. SOD1 is dependent on the copper chaperone for superoxide dismutase (CCS) for activity. It may function more than just as a reactive oxygen scavenging protein. In yeast, SOD1 functions in the glucose repression of cellular respiration; it interacts and stabilizes the membrane-bound casein kinase homologs, Yck1 and Yck2, which are involved in several nutrient-sensing pathways in the cell including glucose and amino acid sensing.