PROSITE documentation PDOC50902
Flavodoxin-like domain profile


The flavodoxin-like domain is an around 170-residue domain with a flavin mononucleotide (FMN)-binding site. It is involved in electron transfer reactions [1,2].

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 [3]. 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 [2].

Some proteins known to contain a flavodoxin-like domain are listed below:

  • Flavodoxin, a low-potential electron donor to a number of redox enzymes (see <PDOC00178>).
  • 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 negative regulator.
  • Bacterial protein mioC, a probable electron transporter required for biotin synthase activity.
  • Bacterial protein hemG.
  • Bacterial tryptophan repressor-binding protein wrbA.
  • Bacterial sulfite reductase [NADPH] flavoprotein α-component (EC (SIR-FP). It catalyzes the 6-electron reduction of sulfite to sulfide.

The profile we developed covers the entire flavodoxin-like domain.

Last update:

March 2003 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

FLAVODOXIN_LIKE, PS50902; Flavodoxin-like domain profile  (MATRIX)


1AuthorsGrandori R. Carey J.
TitleTwo highly homologous putative DNA-binding proteins in yeast and E. coli.
SourceTrends Biochem. Sci. 19:72-72(1994).
PubMed ID8160268

2AuthorsGrandori R. Carey J.
TitleSix new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin.
SourceProtein Sci. 3:2185-2193(1994).
PubMed ID7756978

3AuthorsWang M. Roberts D.L. Paschke R. Shea T.M. Masters B.S.S. Kim J.-J.P.
TitleThree-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.
SourceProc. Natl. Acad. Sci. U.S.A. 94:8411-8416(1997).
PubMed ID9237990

4AuthorsZhao Q. Modi S. Smith G. Paine M. McDonagh P.D. Wolf C.R. Tew D. Lian L.-Y. Roberts G.C.K. Driessen H.P.C.
TitleCrystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution.
SourceProtein Sci. 8:298-306(1999).
PubMed ID10048323

5AuthorsDrennan C.L. Pattridge K.A. Weber C.H. Metzger A.L. Hoover D.M. Ludwig M.L.
TitleRefined structures of oxidized flavodoxin from Anacystis nidulans.
SourceJ. Mol. Biol. 294:711-724(1999).
PubMed ID10610791

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