EC Number   |
General Information |
Reference |
|---|
  1.3.8.17 | physiological function |
both genes fbiA and fbiB are essential for normal coenzyme F420-5,6 production. fbiA and fbiB constitute an operon. Very low levels of fbiB mRNA are produced by the fbiA mutant |
-, 761374 |
| 1.3.8.17 | physiological function |
F420 biosynthesis in Thermomicrobia proceeds via dehydro F420, which is reduced by a free-standing FMN-dependent nitroreductase (DF420 reductase) that is distantly related to the C-terminal domain of FbiB |
760400 |
| 1.3.8.17 | 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 |
-, 745359 |
| 1.3.8.17 | physiological function |
guanylyltransferase FbiD accepts phosphoenolpyruvate, leading to the formation of intermediate dehydro-F420-0. The C-terminal domain of FbiB then utilizes FMNH2 to reduce dehydro-F420-0, which produces mature F420 species when combined with the gamma-glutamyl ligase activity of the N-terminal domain. FbiB also catalyzes the activities of EC 6.3.2.31, coenzyme F420-0:L-glutamate ligase, and EC 6.3.2.34, coenzyme F420-1:gamma-L-glutamate ligase. Expression of genes FbiABCD is sufficient to produce F420 in Escherichia coli |
-, 757742 |
