| Primary Identifier | IPR006313 | Type | Family |
| Short Name | EfeB/EfeN |
| description | This entry represents a small family of proteins with a typical Tat (twin-arginine translocation) signal sequence, suggesting that the family is exported in a folded state, perhaps with a bound redox cofactor. Proteins in this family include deferrochelatase/peroxidase EfeB, which is involved in the recovery of exogenous heme iron. It extracts iron from heme while preserving the tetrapyrrole ring intact [, ]. Crystal structure of EfeB revealed that it has ferredoxin-like fold domains (N- and C-terminal) consisting of an α+β fold that contains an antiparallel β-sheet composed of four β-strands. A large heme binding pocket is located in the C-terminal domain []. This entry also includes deferrochelatase/peroxidase EfeN from Bacillus subtilis, which shows two domains with a ferredoxin-fold and best activity in the acidic range of pH []. |
