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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.

These patterns will not detect proteins related to SODC, but which have lost their catalytic activity, such as Vaccinia virus protein A45.

April 2006 / Patterns revised.

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

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

Consensus pattern: [GA]-[IMFAT]-H-[LIVF]-H-{S}-x-[GP]-[SDG]-x-[STAGDE] The 2 H's are copper ligands Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: 5.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00087 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00087 • Scan Swiss-Prot/TrEMBL entries against PS00087 • view ligand binding statistics

Matching PDB structures: 1AZV 1B4L 1BZO 1CB4 ... [ALL]

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

Consensus pattern: G-[GNHD]-[SGA]-[GR]-x-R-x-[SGAWRV]-C-x(2)-[IV] C is involved in a disulfide bond Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00332 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00332 • Scan Swiss-Prot/TrEMBL entries against PS00332 • view ligand binding statistics

Matching PDB structures: 1AZV 1B4L 1B4T 1BA9 ... [ALL]

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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