|PROSITE documentation PDOC00082 [for PROSITE entry PS00332]|
Copper/Zinc superoxide dismutase (EC 126.96.36.199) (SODC)  is one of the three forms of an enzyme that catalyzes the dismutation of superoxide radicals. SODC binds one atom each of zinc and copper. Various forms of SODC are known: a cytoplasmic form in eukaryotes, an additional chloroplast form in plants, an extracellular form in some eukaryotes, and a periplasmic form in prokaryotes. The metal binding sites are conserved in all the known SODC sequences .
We derived two signature patterns for this family of enzymes: the first one contains two histidine residues that bind the copper atom; the second one is located in the C-terminal section of SODC and contains a cysteine which is involved in a disulfide bond.Note:
These patterns will not detect proteins related to SODC, but which have lost their catalytic activity, such as Vaccinia virus protein A45.Last update:
April 2006 / Patterns revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Bannister J.V., Bannister W.H., Rotilio G.|
|Title||Aspects of the structure, function, and applications of superoxide dismutase.|
|Source||CRC Crit. Rev. Biochem. 22:111-180(1987).|
|2||Authors||Smith M.W., Doolittle R.F.|
|Title||A comparison of evolutionary rates of the two major kinds of superoxide dismutase.|
|Source||J. Mol. Evol. 34:175-184(1992).|