ferritin-like domain-containing protein belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins that catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; similar to Schizosaccharomyces pombe protein rds1 that may have a function in stress-related responses
ferritin-like domain-containing protein belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins that catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; similar to Schizosaccharomyces pombe protein rds1 that may have a function in stress-related responses
Name, label and taxonomic scope
Tax. Exp
All organisms
Name
ferritin-like domain-containing protein
Label
ferritin-like domain-containing protein belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins that catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; similar to Schizosaccharomyces pombe protein rds1 that may have a function in stress-related responses
Supporting evidence
Comments
The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms.