Cu,Zn superoxide dismutase-like superfamily

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: All beta proteins [ 48724] (165)
• Fold: Immunoglobulin-like beta-sandwich [ 48725] (27)
  • sandwich; 7 strands in 2 sheets; greek-key
    some members of the fold have additional strands
• Superfamily: Cu,Zn superoxide dismutase-like [ 49329]
• Families: Cu,Zn superoxide dismutase-like [ 49330] (2)

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Superfamily statistics

	Genomes (596)	UniProt 15.0	PDB chains (SCOP 1.73)
Domains	1,449	1,681	50
Proteins	1,296	1,585	50

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Functional annotation

• General category: Metabolism
• Detailed category: Redox

Function annotation of SCOP domain superfamilies

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InterPro annotation

• Cross references: IPR001424 SSF49329 Protein matches
• Abstract:

  Superoxide dismutases are ubiquitous metalloproteins that prevent damage by oxygen-mediated free radicals by catalysing the dismutation of superoxide into molecular oxygen and hydrogen peroxide [2751312]. Superoxide is a normal by-product of aerobic respiration and is produced by a number of reactions, including oxidative phosphorylation and photosynthesis. The dismutase enzymes have a very high catalytic efficiency due to the attraction of superoxide to the ions bound at the active site [1463506, 3891411].

  There are three forms of superoxide dismutase, depending on the metal cofactor: Cu/Zn (which binds both copper and zinc), Fe and Mn types. The Fe and Mn forms are similar in their primary, secondary and tertiary structures, but are distinct from the Cu/Zn form [2263641]. Prokaryotes and protists contain Mn, Fe or both types, while most eukaryotic organisms utilise the Cu/Zn type.

InterPro database

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