IPR001155
NADH:flavin oxidoreductase/NADH oxidase, N-terminal
InterPro entry
Short name | OxRdtase_FMN_N |
Overlapping homologous superfamilies | |
domain relationships |
Description
The TIM-barrel fold is a closed barrel structure composed of an eight-fold repeat of β-α units, where the eight parallel β strands on the inside are covered by the eight α helices on the outside
[1]. It is a widely distributed fold which has been found in many enzyme families that catalyse completely unrelated reactions
[2]. 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
References
1.The TIM-barrel fold: a versatile framework for efficient enzymes. Wierenga RK. FEBS Lett. 492, 193-8, (2001). View articlePMID: 11257493
2.One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. Nagano N, Orengo CA, Thornton JM. J. Mol. Biol. 321, 741-65, (2002). View articlePMID: 12206759
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- Pfam:PF00724
Representative structure
1z41: Crystal structure of oxidized YqjM from Bacillus subtilis