1.5.99.15	Ferredoxin	ferredoxin may serve as an electron donor	742781	
1.5.99.15	flavin	iron-sulfur flavoprotein	727782	
1.5.99.15	FMN	-	742870	
1.5.99.15	FMN	bioinformatic analysis reveals the presence of one FMN-binding site. The purified protein shows an absorbance peaks at 380 and 460 nm, characteristic of oxidized FMN	727782	
1.5.99.15	FMN	DmrB contains 2 FMN molecules on the active site at the monomer-monomer interface. The FMN-1 molecule shows ionic interactions with residues Ser110 and Asn116 along with some non-bonded contacts. The FMN-2 molecule shows ionic contacts with Lys123 and Gln120 and pi-pi stacking with the Tyr85 residue. FMN stabilizes and preserves the secondary and quaternary structure of DmrB against thermal insult	764885	
1.5.99.15	FMN	the enzyme contains one flavin mononucleotide (FMN)-binding site	742781	
1.5.99.15	FMN	within a homotrimer, each monomer-monomer interface exhibits an active site with two adjacently bound flavin mononucleotide (FMN) ligands, one deeply buried and tightly bound and one more peripheral. Computational docking suggests that the peripheral site binds either the observed FMN (the electron donor for the overall reaction) or the pterin, H2MPT (the electron acceptor for the overall reaction), in configurations ideal for electron transfer to and from the tightly bound FMN. Analysis of the FMN binding structure in the active site, and kinetics, overview	742870	
1.5.99.15	additional information	determination of FMN is the cofactor of DmrB, overview	742870	
1.5.99.15	additional information	NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MJ0208. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MJ0208 can transfer electrons to dihydromethanopterin	742781	
1.5.99.15	additional information	NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MM1854. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MM1854 can transfer electrons to dihydromethanopterin	742781