{PDOC50902}
{PS50902; FLAVODOXIN_LIKE}
{BEGIN}
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* Flavodoxin-like domain profile *
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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 alpha-beta-alpha  fold  with  a  central 5-stranded parallel hydrophobic
beta-sheet flanked   on   either   side   by  amphipathic  alpha-helices  (see
<PDB:2FCR>) [3,4,5].  The  FMN is positioned at the tip of the C-terminal side
of the beta-sheet [3]. The fold correlates with a highly conserved, repetitive
sequence pattern  in  which  hydrophobic  residues cluster in beta-strands and
have a 3-4-residue periodicity in alpha-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   alpha-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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: March 2003 / First entry.

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

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