D
IPR001155

NADH:flavin oxidoreductase/NADH oxidase, N-terminal

InterPro entry
Short nameOxRdtase_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

cellular component

  • None

Cross References

Contributing Member Database Entry
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