v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | The desulforedoxin domain is a small non-haem iron domain present in the desulforedoxin (Dx) and desulfoferrodoxin (Superoxide reductase or Dfx) proteins of some archeael and bacterial methanogens and sulfate/sulfur reducers. It constitutes essentially the full length of desulforedoxin, and the N-terminal domain of Desulfoferrodoxin.Desulforedoxin is a small, single-domain homodimeric protein. Each subunit (of 36 amino acid residues) contains an iron atom bound to four cysteinyl sulfur atoms, Fe(S-Cys)4, in a distorted tetrahedral coordination. Its metal centre is similar to that found in rubredoxin type proteins [ ]. Desulfoferrodoxin forms a homodimeric protein, with each protomer comprised of two domains, the N-terminal DSRD domain and C-terminal superoxide reductase-like (SORL) domain. Each domain has a distinct iron centre: the DSRD iron centre I, Fe(S-Cys)4; and the SORL iron centre II, Fe[His4Cys(Glu)] []. |
| Short Name | Desulfoferrodoxin_N |