The complete amino acid sequence of a dimeric hemoglobin (HbI) from the marine bivalve mollusc Anadara broughtonii was determined by sequencing of the intact chain and peptide fragments produced by cleavage at two asparaginylglycine bonds and at methionyl, arginyl, and tryptophanyl residues. The clam hemoglobin consists of two identical polypeptide chains. The globin chain has 146 amino acid residues with a proline at the NH2 terminus and a leucine at the COOH terminus. The calculated molecular mass of the native hemoglobin was 32945 daltons. The clam hemoglobin contains only two histidine residues, which correspond to the distal and proximal heme-linked positions. Compared with human beta chain, an additional segment of seven residues is present in the NH2-terminal region and also five less residues in the COOH-terminal region. Although such an amino-terminal elongation has been known to be characteristic of hemoglobins from the most primitive living vertebrates Cyclostomata, a very similar structure was found to occur in the hemoglobin from the primitive invertebrate arcid clam.