Structural homologies between the amino acid sequence of Clostridium pasteurianum MoFe protein and the DNA sequences of nifD and K genes of phylogenetically diverse bacteria.
The complete amino acid sequence of the larger (alpha-) subunit and about 70% of the total sequence of the smaller (beta-) subunit of the MoFe protein from Clostridium pasteurianum was determined by analyses of peptides derived from BrCN cleavage and by digestions with trypsin, staphylococcal protease and lysylendo-peptidase of the separated subunits. The alpha-subunit has 529 amino acid residues, giving an Mr value of 58 774. This is the first complete sequence for the alpha-subunit of an isolated MoFe protein. In comparing the sequences of both subunits to those from other sources, 5 out of 9 cysteines in the alpha-subunit and 3 out of 6 in the beta-subunit are invariant, thus suggesting a function as ligands to FeS and MoFeS clusters in the MoFe protein. All of these cysteines are located in the amino terminal halves of both subunits.
D000595:Amino Acid Sequence; D003013:Clostridium / Q000201:enzymology*; D005288:Ferredoxins / Q000235:genetics; D005796:Genes; D005798:Genes, Bacterial; D046911:Macromolecular Substances; D008983:Molybdoferredoxin / Q000235:genetics; D009591:Nitrogenase / Q000235:genetics
D005288:Ferredoxins; D046911:Macromolecular Substances; D008983:Molybdoferredoxin; D009591:Nitrogenase