{PDOC00179}
{PS00202; RUBREDOXIN}
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* Rubredoxin signature *
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Rubredoxins [1] are small electron-transfer prokaryotic proteins. They contain
an iron atom which is ligated  by  four cysteine residues. Rubredoxins are, in
some cases, functionally  interchangeable with  ferredoxins.  As a pattern for
these proteins we have selected a conserved  region  that  includes two of the
cysteine residues that bind the iron atom.

-Consensus pattern: [LIVM]-x-{G}-{R}-W-x-C-P-x-C-[AGD]
                    [The 2 C's bind the iron atom]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 2.

-Note: In Pseudomonas oleovorans rubredoxin 2 (gene alkG) [2], this pattern is
 found twice because alkG has two rubredoxin domains.
-Note: Rubrerythrin [3], a  protein  with  inorganic pyrophosphatase  activity
 from Desulfovibrio  vulgaris  possesses  a C-terminal rubredoxin-like domain.
 But this domain is too divergent to be detected by the above pattern.

-Last update: December 2004 / Pattern and text revised.

[ 1] Berg J.M., Holm R.H.
     (In) Iron-sulfur proteins, Spiro T.G., Ed., pp1-66, Wiley, New-York,
     (1982).
[ 2] Kok M., Oldenhuis R., der Linden M.P.G., Meulenberg C.H.C., Kingma J.,
     "Witholt B
     The Pseudomonas oleovorans alkBAC operon encodes two structurally
     related rubredoxins and an aldehyde dehydrogenase."
     J. Biol. Chem. 264:5442-5451(1989).
     PubMed=2647719;
[ 3] van Beeumen J.J., van Driessche G., Liu M.-Y., Le Gall J.
     "The primary structure of rubrerythrin, a protein with inorganic
     pyrophosphatase activity from Desulfovibrio vulgaris. Comparison with
     hemerythrin and rubredoxin."
     J. Biol. Chem. 266:20645-20653(1991).
     PubMed=1657933;

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