NADH:flavin oxidoreductase/NADH oxidase, N-terminal (IPR001155)

Short name: OxRdtase_FMN_N

Overlapping homologous superfamilies

Domain relationships


The TIM-barrel fold is a closed barrel structure composed of an eight-fold repeat of beta-alpha units, where the eight parallel beta strands on the inside are covered by the eight alpha helices on the outside [PMID: 11257493]. It is a widely distributed fold which has been found in many enzyme families that catalyse completely unrelated reactions [PMID: 12206759]. The active site is always found at the C-terminal end of this domain.

Proteins in this entry are a variety of NADH:flavin oxidoreductase/NADH oxidase enzymes, found mostly in bacteria or fungi, that contain a TIM-barrel fold. They commonly use FMN/FAD as cofactor and include:

  • dimethylamine dehydrogenase
  • trimethylamine dehydrogenase
  • 12-oxophytodienoate reductase
  • NADPH dehydrogenase
  • NADH oxidase

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0010181 FMN binding
GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.