Complete amino acid sequence of cytochrome c551 from Erythrobacter species strain OCh 114.
The complete amino acid sequence of cytochrome c551 isolated from an aerobic photosynthetic bacterium, Erythrobacter sp. strain OCh 114, was determined. The cytochrome molecule was composed of a total of 119 amino acid residues and its molecular weight including heme was calculated to be 13,235. The sequence was (Sequence: see text). Its molecular weight indicates that this cytochrome is of the L-type. Sequence alignment with other bacterial cytochromes c shows that this cytochrome is similar to cytochromes c of Rhodobacter capsulatus, Rhodobacter sphaeroides, and Paracoccus denitrificans, which were grouped into the alpha-3 subcluster from the 16S rRNA sequence analysis.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001420:Bacteria, Aerobic / Q000145:classification / Q000201:enzymology*; D001426:Bacterial Proteins; D003574:Cytochrome c Group; D008928:Mitochondria / Q000201:enzymology; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis; D010788:Photosynthesis; D010802:Phylogeny
D000596:Amino Acids; D001426:Bacterial Proteins; D003574:Cytochrome c Group; D010446:Peptide Fragments; C017167:cytochrome C(551)