InterPro domain: IPR038136

This entry contains 2-phospho-L-lactate transferase (CofD), phosphoenolpyruvate transferase and related sequences. CofD catalyses the fourth step in the biosynthesis of coenzyme F420, which is the transfer of the 2-phospholactate moiety from lactyl (2) diphospho-(5') guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) and GMP. F420 is a flavin derivative found in methanogens, Mycobacteria, and several other lineages. This enzyme is characterised so far in Methanocaldococcus jannaschii (Methanococcus jannaschii) [ 1 , 2 ] but appears restricted to F420-containing species and is predicted to carry out the same function in these other species. CofD monomer contains twelve beta-strands, seven of them forming a Rossmann fold, and thirteen alpha-helices [ 3 ].

1. Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F(420) biosynthesis in Methanococcus jannaschii. Biochemistry 41, 3754-61
2. Molecular insights into the biosynthesis of the F420 coenzyme. J. Biol. Chem. 283, 11832-40