v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Desulfoferrodoxin is a non-haem iron protein which contains two types of iron atoms per molecule, a desulfoferrodoxin-like FES(4) site, and an octahedral coordinated high-spin ferrous site with nitrogen/oxygen-containing ligands. The short N-terminal domain contains four conserved Cys for binding of the ferric iron atom, and is homologous to the small protein desulforedoxin. The remainder of the molecule binds the ferrous iron atom and is similar to neelaredoxin, a monomeric blue non-haem iron protein. The homologue from Treponema pallidum, although essentially a full length homologue, lacks three of the four Cys residues in the N-terminal domain; the domain may have lost ferric binding ability but may have some conserved structural role such as dimerisation, or some new function. This protein is described in some articles as rubredoxin oxidoreductase (rbo), and its gene shares an operon with the rubredoxin gene in Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303). |
| Short Name | Desulfoferrodoxin_rbo |