PROSITE documentation PDOC00082Copper/Zinc superoxide dismutase signatures
Copper/Zinc superoxide dismutase (EC 1.15.1.1) (SODC) [1] 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 [2].
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.
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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). | |
| PubMed ID | 3315461 |
| 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). | |
| PubMed ID | 1556751 |
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