Superoxide dismutases (SODs) are ubiquitous metalloproteins that prevent damage by oxygen-mediated free radicals by catalyzing the dismutation of superoxide into molecular oxygen and hydrogen peroxide [1]. There are three families of SODs differing in their metal cofactor and their species distribution. CU/Zn-SODs are found mostly in eukaryotes, Fe/Mn-SODs in prokaryotes, mitochondria and protists and Ni-SODs in prokaryotes. The Cu/Zn SOD folds into an eight-stranded β-sandwich, similar to the immunoglobulin fold [2].
The minor olive pollen allergen Ole e 5 belongs to this family [3].
Family-defining Pfam domains (at least one of these domains is present in each family member):
Pfam domain | Pfam clan | ||
PF00080 | Copper/zinc superoxide dismutase (SODC) | - |
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