PROSITE documentation PDOC00179
Rubredoxin signature


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.


In Pseudomonas oleovorans rubredoxin 2 (gene alkG) [2], this pattern is found twice because alkG has two rubredoxin domains.


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.


Technical section

PROSITE method (with tools and information) covered by this documentation:

RUBREDOXIN, PS00202; Rubredoxin signature  (PATTERN)


1AuthorsBerg J.M. Holm R.H.
Source(In) Iron-sulfur proteins, Spiro T.G., Ed., pp1-66, Wiley, New-York, (1982).

2AuthorsKok M. Oldenhuis R. der Linden M.P.G. Meulenberg C.H.C. Kingma J.
TitleWitholt B The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase.
SourceJ. Biol. Chem. 264:5442-5451(1989).
PubMed ID2647719

3Authorsvan Beeumen J.J. van Driessche G. Liu M.-Y. Le Gall J.
TitleThe primary structure of rubrerythrin, a protein with inorganic pyrophosphatase activity from Desulfovibrio vulgaris. Comparison with hemerythrin and rubredoxin.
SourceJ. Biol. Chem. 266:20645-20653(1991).
PubMed ID1657933

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