Cloned (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
structures of the C-terminal domain of FbiB in apo-, F420-0-, and FMN-bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WP79 | cf. EC 6.3.2.31, EC 6.3.2.34 | - |
Mycobacterium tuberculosis H37Rv | P9WP79 | cf. EC 6.3.2.31, EC 6.3.2.34 | - |
General Information | Comment | Organism |
---|---|---|
physiological function | FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity | Mycobacterium tuberculosis |