{PDOC00175}
{PS00197; 2FE2S_FER_1}
{PS51085; 2FE2S_FER_2}
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* 2Fe-2S ferredoxin-type iron-sulfur binding domain signature and profile *
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Ferredoxins  are small, acidic, electron transfer proteins that are ubiquitous
in  biological  redox  systems.  They  have  either  4Fe-4S, 3Fe-4S, or 2Fe-2S
cluster.  Among  them,  ferredoxin  with  one  2Fe-2S cluster per molecule are
present  in  plants, animals, and bacteria, and form a distinct 2Fe-Ferredoxin
family  [1,2].  They  are proteins of around one hundred amino acids with four
conserved  cysteine  residues  to  which  the  2Fe-2S cluster is ligated. This
conserved region is also found as a domain in various metabolic enzymes.

Several  structures  of the 2Fe-2S ferredoxin domain have been determined (see
for example <PDB:4FXC>) [3]. The domain is classified as a beta-grasp which is
characterized  as  having  a beta-sheet comprised of four beta-strands and one
alpha-helix  flanking  the  sheet  [4].  The  two  Fe  atoms  are  coordinated
tetrahedrally by the two inorganic S atoms and four cysteinyl S atoms.

Some proteins that contains a 2Fe-2S ferredoxin-type domain are listed below:

 - Ferredoxin from photosynthetic organisms;  namely plants and algae where it
   is located in the chloroplast or cyanelle; and cyanobacteria.
 - Ferredoxin from archaebacteria of the Halobacterium genus.
 - Ferredoxin IV (gene pftA) and V (gene fdxD) from Rhodobacter capsulatus.
 - Ferredoxin in the  toluene  degradation  operon (gene xylT) and naphthalene
   degradation operon (gene nahT) of Pseudomonas putida.
 - Hypothetical Escherichia coli protein yfaE.

 - The N-terminal domain  of the  bifunctional ferredoxin/ferredoxin reductase
   electron  transfer  component of the benzoate 1,2-dioxygenase complex (gene
   benC) from Acinetobacter calcoaceticus, the toluene 4-monooxygenase complex
   (gene tmoF), the toluate 1,2-dioxygenase system (gene xylZ), and the xylene
   monooxygenase system (gene xylA) from Pseudomonas.
 - The N-terminal domain of  phenol  hydroxylase  protein  p5 (gene dmpP) from
   Pseudomonas Putida.
 - The N-terminal domain of  methane  monooxygenase   component C  (gene mmoC)
   from Methylococcus capsulatus .
 - The C-terminal domain of the vanillate degradation pathway  protein vanB in
   a Pseudomonas species.
 - The N-terminal domain of bacterial  fumarate  reductase iron-sulfur protein
   (gene frdB).
 - The  N-terminal  domain  of CDP-6-deoxy-3,4-glucoseen reductase (gene ascD)
   from Yersinia pseudotuberculosis.
 - The central domain of eukaryotic succinate dehydrogenase (ubiquinone) iron-
   sulfur protein.
 - The N-terminal domain of eukaryotic xanthine dehydrogenase.
 - The N-terminal domain of eukaryotic aldehyde oxidase.

Three  of  the  four  conserved  cysteines  are clustered together in the same
region  of  the  protein. Our signature pattern spans that iron-sulfur binding
region. We also developed a profile that covers the whole domain.

-Consensus pattern: C-{C}-{C}-[GA]-{C}-C-[GAST]-{CPDEKRHFYW}-C
                    [The 3 C's are 2Fe-2S ligands]
-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note:  Ferredoxins  from the adrenodoxin subfamily are slightly divergent and
 are not picked up by our pattern (but they are recognized by the profile). We
 have  thus  developed  a  second  pattern  specific  for  this subfamily (see
 <PDOC00642>).

-Last update: March 2005 / Text revised; profile added.

[ 1] Meyer J.
     Trends Ecol. Evol. 3:222-226(1988).
[ 2] Harayama S., Polissi A., Rekik M.
     "Divergent evolution of chloroplast-type ferredoxins."
     FEBS Lett. 285:85-88(1991).
     PubMed=2065785
[ 3] Fukuyama K., Ueki N., Nakamura H., Tsukihara T., Matsubara H.
     "Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis
     refined at 2.5 A resolution: structural comparisons of plant-type
     ferredoxins and an electrostatic potential analysis."
     J. Biochem. 117:1017-1023(1995).
     PubMed=8586613
[ 4] Overington J.P.
     Curr. Opin. Struct. Biol. 2:394-401(1992).

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