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* Adrenodoxin family, iron-sulfur binding region signature *
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Ferredoxins [1] are a group of iron-sulfur  proteins  which  mediate  electron
transfer in a wide variety of metabolic reactions.  Ferredoxins can be divided
into several subgroups depending upon  the  physiological  nature  of the iron
sulfur  cluster(s)  and  according  to  sequence  similarities.  One family of
ferredoxins groups together the following proteins that all bind a single 2Fe-
2S iron-sulfur cluster:

 - Adrenodoxin (ADX) (adrenal ferredoxin), a  vertebrate mitochondrial protein
   which transfers electrons from adrenodoxin reductase to cytochrome P450scc,
   which is involved in cholesterol side chain cleavage.
 - Putidaredoxin (PTX), a Pseudomonas putida protein which transfers electrons
   from putidaredoxin  reductase to  cytochrome P450-cam, which is involved in
   the oxidation of camphor.
 - Terpredoxin  [2],  a  Pseudomonas  protein  which  transfers electrons from
   terpredoxin reductase  to  cytochrome  P450-terp,  which is involved in the
   oxidation of alpha-terpineol.
 - Escherichia coli ferredoxin (gene fdx) [3] whose  exact function is not yet
   known.
 - Rhodobacter capsulatus ferredoxin VI [4], which may transfer electrons to a
   yet uncharacterized oxygenase.
 - Caulobacter crescentus ferredoxin (gene fdxB) [5].

In these proteins, four cysteine  residues bind the iron-sulfur cluster. Three
of these cysteines are  clustered  together in the same region of the protein.
Our signature pattern spans that iron-sulfur binding region.

-Consensus pattern: C-x(2)-[STA]-x-[STAV]-C-[STA]-T-C-[HR]
                    [The three C's are 2Fe-2S ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Last update: June 1994 / Pattern and text revised.

[ 1] Meyer J.
     Trends Ecol. Evol. 3:222-226(1988).
[ 2] Peterson J.A., Lu J.-Y., Geisselsoder J., Graham-Lorence S., Carmona C.,
     Witney F., Lorence M.C.
     J. Biol. Chem. 267:14193-14203(1992).
[ 3] Ta D.T., Vickery L.E.
     J. Biol. Chem. 267:11120-11125(1992).
[ 4] Naud I., Vincon M., Garin J., Gaillard J., Forest E., Jouanneau Y.
     Eur. J. Biochem. 222:933-939(1994).
[ 5] Amemiya K
     EMBL/Genbank: X51607.