BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms

Trends Biochem Sci. 2002 Oct;27(10):497-500. doi: 10.1016/s0968-0004(02)02181-3.


A novel FAD-binding domain, BLUF, exemplified by the N-terminus of the AppA protein from Rhodobacter sphaeroides, is present in various proteins, primarily from Bacteria. The BLUF domain is involved in sensing blue-light (and possibly redox) using FAD and is similar to the flavin-binding PAS domains and cryptochromes. The predicted secondary structure reveals that the BLUF domain is a novel FAD-binding fold.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Binding Sites
  • Flavin-Adenine Dinucleotide / metabolism*
  • Flavoproteins / chemistry*
  • Flavoproteins / metabolism*
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Tertiary
  • Rhodobacter sphaeroides / metabolism
  • Sequence Alignment


  • AppA protein, Rhodobacter sphaeroides
  • Bacterial Proteins
  • Flavoproteins
  • Flavin-Adenine Dinucleotide