Catalase core domain superfamily (IPR037060)
Short name: Catalase_core_sf
- Catalase haem-binding site (IPR002226)
- Catalase core domain (IPR011614)
- Catalase, mono-functional, haem-containing (IPR018028)
- Catalase superfamily (IPR020835)
- Catalase active site (IPR024708)
- Catalase, mono-functional, haem-containing, clades 1 and 3 (IPR024711)
- Catalase, mono-functional, haem-containing, clade 2 (IPR024712)
- Catalase, clade 3 (IPR040333)
Catalases (EC:184.108.40.206) are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects [PMID: 11351128]. Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases (IPR000763) that are closely related to plant peroxidases, and non-haem, manganese-containing catalases (IPR007760) that are found in bacteria [PMID: 14745498]. Based on a phylogenetic analysis, catalases can be classified into clade 1, 2 and 3. Clade 1 contains small subunit catalases from plants and a subset of bacteria; clade 2 contains large subunit catalases from fungi and a second subset of bacteria; and clade 3 contains small subunit catalases from bacteria, fungi, protists, animals, and plants [PMID: 9287428, PMID: 12557185].
This entry represent the core-forming domain superfamily of mono-functional, haem-containing catalases. It does not cover the region that carries an immune-responsive amphipathic octa-peptide that is found in the C-terminal of some catalases (IPR010582).
- G3DSA:220.127.116.11 (G3DSA:18.104.22.168)