| Literature References | 1. ADMAN, E.T., SIEKER, L.C. AND JENSEN, L.H.
Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 Angstroms
resolution.
J.MOL.BIOL. 217(2) 337-352 (1991).
2. MEYER, J., GAGNON, J., SIEKER, L.C., VANDORSSELAER, A. AND MOULIS, J.M.
Rudredoxin from Clostridium thermosaccharolyticum - Amino acid sequence,
mass spectrometric and preliminary crystallographic data.
BIOCHEM.J. 271(3) 839-841 (1990).
3. BACHMAYER, H., YASUNOBU, K.T., PEEL, J.L. AND MAYHEW, S.
Non-heme iron proteins.
J.BIOL.CHEM. 243 1022-1030 (1968).
4. CHEN, J.C. AND MORTENSEN, L.E.
2 Open reading frames (ORFs) identified near the hydrogenase structural
genes in Azotobacter vinelandii, the 1st ORF may encode for a polypeptide
similar to rubredoxins.
BIOCHIM.BIOPHYS.ACTA 1131(1) 122-124 (1992).
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| Documentation | Rubredoxin is a low molecular weight non-haem iron-containing bacterial
protein involved in electron transfer [1,2], sometimes replacing ferredoxin
as an electron carrier [3]. Its active site contains an iron atom co-
ordinated by the sulphurs of 4 conserved Cys residues residing on 2 loops
[2,3], which are the most well-conserved regions of the protein [3]. In
some species, the rubredoxin gene is closely linked to the dehydrogenase
gene, and its transcription is required for dehydrogenase activity [4]. The
reason for this is as yet unknown, but rubredoxin may act as a source of
electrons for the molecular hydrogen-splitting activity of the
dehydrogenase [4].
RUBREDOXIN is a 2-element fingerprint that provides a signature for the
rubredoxins. The fingerprint was derived from an initial alignment of 7
sequences: motifs 1 and 2 span the 2 loops involved in binding the
iron atom - motif 2 includes the region encoded by PROSITE pattern
RUBREDOXIN (PS00202), which contains 2 of the iron-binding Cys residues.
Two iterations on OWL22.1 were required to reach convergence, at which
point a true set comprising 23 sequences was identified.
An update on SPTR37_9f identified a true set of 38 sequences.
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