Complete amino acid sequence of Halobacterium halobium ferredoxin containing an Nepsilon-acetyllysine residue.
1. The complete amino acid sequence of the 2Fe-2S ferredoxin from Halobacterium halobium was determined to be: (formula see text):2. The apoferredoxin chain consists of 128 amino acid residues and has a molecular weight of 14,330. 3. There are only four cysteines in this ferredoxin molecule; they should be involved in the binding of the two iron atoms at the active center. Ther relative positions of these cysteines are similar to those of the cysteines in chloroplast ferredoxins. 4. There is a high degree of homology between H. halobium ferredoxin and chloroplast ferredoxins, though the latter molecules contain only about 98 amino acid residues. 5. H. halobium ferredoxin contains a single residue of Nepsilon-acetyllysine.
D000595:Amino Acid Sequence; D005288:Ferredoxins; D006217:Halobacterium / Q000032:analysis*; D008239:Lysine / Q000031:analogs & derivatives*; D010446:Peptide Fragments / Q000032:analysis
D005288:Ferredoxins; D010446:Peptide Fragments; D008239:Lysine