PROSITE documentation PDOC00179Rubredoxin 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.
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.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Berg J.M. Holm R.H. |
Source | (In) Iron-sulfur proteins, Spiro T.G., Ed., pp1-66, Wiley, New-York, (1982). |
2 | Authors | Kok M. Oldenhuis R. der Linden M.P.G. Meulenberg C.H.C. Kingma J. |
Title | Witholt B The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase. | |
Source | J. Biol. Chem. 264:5442-5451(1989). | |
PubMed ID | 2647719 |
3 | Authors | van Beeumen J.J. van Driessche G. Liu M.-Y. Le Gall J. |
Title | The primary structure of rubrerythrin, a protein with inorganic pyrophosphatase activity from Desulfovibrio vulgaris. Comparison with hemerythrin and rubredoxin. | |
Source | J. Biol. Chem. 266:20645-20653(1991). | |
PubMed ID | 1657933 |
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