The flavodoxin-like domain is an around 170-residue domain with a flavin
mononucleotide (FMN)-binding site. It is involved in electron transfer
Structure analyses of several flavodoxin-like domains have shown that it is a
wound α-β-α fold with a central 5-stranded parallel hydrophobic
β-sheet flanked on either side by amphipathic α-helices (see
<PDB:2FCR>) [3,4,5]. The FMN is positioned at the tip of the C-terminal side
of the β-sheet . The fold correlates with a highly conserved, repetitive
sequence pattern in which hydrophobic residues cluster in β-strands and
have a 3-4-residue periodicity in α-helices .
Some proteins known to contain a flavodoxin-like domain are listed below:
Flavodoxin, a low-potential electron donor to a number of redox enzymes
Eukaryotic nitric-oxide synthase (NOS).
Bacterial and eukaryotic NADPH-cytochrome P450 reductase.
Yeast protein YCP4.
Fission yeast protein P25, the target of a complex transcriptional system
that involves the AP-1-liker factor PAP1 as positive regulator and CRM1 as
Bacterial protein mioC, a probable electron transporter required for biotin
Bacterial protein hemG.
Bacterial tryptophan repressor-binding protein wrbA.
Bacterial sulfite reductase [NADPH] flavoprotein α-component
(EC 22.214.171.124) (SIR-FP). It catalyzes the 6-electron reduction of sulfite to
The profile we developed covers the entire flavodoxin-like domain.
March 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Grandori R., Carey J. Two highly homologous putative DNA-binding proteins in yeast and E.
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