PROSITE documentation PDOC00082

Copper/Zinc superoxide dismutase signatures




Description

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

SOD_CU_ZN_1, PS00087; Copper/Zinc superoxide dismutase signature 1  (PATTERN)

SOD_CU_ZN_2, PS00332; Copper/Zinc superoxide dismutase signature 2  (PATTERN)


References

1AuthorsBannister J.V., Bannister W.H., Rotilio G.
TitleAspects of the structure, function, and applications of superoxide dismutase.
SourceCRC Crit. Rev. Biochem. 22:111-180(1987).
PubMed ID3315461

2AuthorsSmith M.W., Doolittle R.F.
TitleA comparison of evolutionary rates of the two major kinds of superoxide dismutase.
SourceJ. Mol. Evol. 34:175-184(1992).
PubMed ID1556751



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