LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | This entry represents a group of proteins, containing ferritin-like domain, which is an about 145-residue domain made of a four-helix bundle surrounding a non-heme, non-sulphur, oxo-bridged diiron site. The diiron site is contained within a twisted, left-handed four-helix-bundle constituted of two anti-parallel helix pairs connected through a left-handed crossover connection. Known ligand residues at non-heme, non-sulphur diiron sites in proteins include His, Asp, Glu, and Tyr. Proteins containing a ferritin-like diiron domain possess the ability to catalyzeoxidation of Fe 2+to Fe 2+by O 2, i.e. ferroxidase activity. The ferritin- like diiron domain occurs in stand-alone form in ferritin and bacterioferritinor in association with the rubredoxin-like domain in rubrerythrin [].Proteins known to contain a ferritin-like diiron domain are listed below: Ferritin (Ftn), an eukaryotic intracellular protein that stores iron in a soluble, nontoxic, readily available form.Bacterioferritin (Bfr), a prokaryotic protein which may perform functions in iron detoxification and storage.Rubrerythrin (Rr), a non-heme protein isolated from anaerobic sulphate- reducing bacteria.Nigerythrin (Nr), a prokaryotic protein of unknown function. |
| Short Name | Ferritin-like_diiron |
