Abstract
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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins*
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Binding Sites
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Flavin-Adenine Dinucleotide / metabolism*
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Flavoproteins / chemistry*
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Flavoproteins / metabolism*
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Molecular Sequence Data
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Protein Binding
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Protein Structure, Tertiary
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Rhodobacter sphaeroides / metabolism
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Sequence Alignment
Substances
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AppA protein, Rhodobacter sphaeroides
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Bacterial Proteins
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Flavoproteins
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Flavin-Adenine Dinucleotide