PROSITE documentation PDOC50902Flavodoxin-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 1.8.1.2) (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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Grandori R. Carey J. |
| Title | Two highly homologous putative DNA-binding proteins in yeast and E. coli. | |
| Source | Trends Biochem. Sci. 19:72-72(1994). | |
| PubMed ID | 8160268 |
| 2 | Authors | Grandori R. Carey J. |
| Title | Six new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin. | |
| Source | Protein Sci. 3:2185-2193(1994). | |
| PubMed ID | 7756978 |
| 3 | Authors | Wang M. Roberts D.L. Paschke R. Shea T.M. Masters B.S.S. Kim J.-J.P. |
| Title | Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 94:8411-8416(1997). | |
| PubMed ID | 9237990 |
| 4 | Authors | Zhao 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. |
| Title | Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. | |
| Source | Protein Sci. 8:298-306(1999). | |
| PubMed ID | 10048323 |
| 5 | Authors | Drennan C.L. Pattridge K.A. Weber C.H. Metzger A.L. Hoover D.M. Ludwig M.L. |
| Title | Refined structures of oxidized flavodoxin from Anacystis nidulans. | |
| Source | J. Mol. Biol. 294:711-724(1999). | |
| PubMed ID | 10610791 | |
| DOI | 10.1006/jmbi.1999.3151 |
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