InterPro domain: IPR002563

This domain can be found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes, and various other oxidoreductase and monooxygenase enzymes [ 1 , 2 , 3 ].

This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.

1. Microbial ferric iron reductases. FEMS Microbiol. Rev. 27, 427-47
2. Aminobacter aminovorans NADH:flavin oxidoreductase His140: a highly conserved residue critical for NADH binding and utilization. Biochemistry 43, 12887-93
3. Structural proteomics of an archaeon. Nat. Struct. Biol. 7, 903-9