Pathways & interactions
[2Fe-2S]-binding domain superfamily (IPR036884)
Short name: 2Fe-2S-bd_dom_sf
- [2Fe-2S]-binding (IPR002888)
- Xanthine dehydrogenase, small subunit, bacteria (IPR012175)
- Xanthine dehydrogenase, small subunit (IPR014307)
- Aldehyde oxidase (IPR014313)
- Aldehyde oxidase/xanthine dehydrogenase (IPR016208)
- 4-hydroxybenzoyl-CoA reductase, gamma subunit (IPR017606)
- Xanthine dehydrogenase E subunit (IPR017611)
- Selenium-dependent xanthine dehydrogenase (IPR017697)
- Molybdenum-binding protein YgfN/XdhD (IPR017699)
The [2Fe-2S] binding domain is found in a range of enzymes including dehydrogenases, oxidases and oxidoreductases.
The aldehyde oxido-reductase (Mop) from the sulphate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas is a homodimer of 907 amino acid residues subunits and is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different [2Fe-2S] centres. It is folded into four domains of which the first two bind the iron sulphur centres and the last two are involved in Mo-co binding. Mo-co is a molybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms a tricyclic system with the pterin bicycle annealed to a pyran ring. The molybdopterin dinucleotide is deeply buried in the protein. The cis-dithiolene group of the pyran ring binds the molybdenum, which is coordinated by three more (oxygen) ligands [PMID: 7502041].
- SSF47741 (SSF47741)