An optional C-terminal domain is ancestral in α-amylases of bilaterian animals

Abstract

AbstractThe modular structure and organization of most proteins is a fascinating aspect of their origin and evolution. α-Amylases are known to be formed of at least three domains. In a number of bacterial α-amylases, one or several additional domains may exist, which are carbohydrate binding modules, interacting with raw substrates. In animal α-amylases, however, no additional domain has been described. Here we report the presence of a C-terminal domain, previously described only in the bacterium Pseudoalteromonas haloplanktis. This domain is widely distributed in invertebrate α-amylases and must be ancestral, although it has been lost in important phyla or groups, such as vertebrates and insects. Its function is still unknown. In a single genome, enzymes with and without the terminal domain may coexist. In a few instances, this domain has been recruited by other proteins in both bacteria and animals through domain shuffling.