Conserved of amino acid sequence of <i>Panulirus argus</i> α-amylase respect to other known α-amylases (<i>L</i>. <i>vannamei</i>, accession no. CAA54524, <i>M</i>. <i>japonicus</i>, AHN91844, <i>Daphnia pulex</i>, EFX81580, <i>Tenebrio molitor</i>, P56634, <i>H</i>. <i>sapiens</i>, AAA51724 and <i>Oryzias latipes</i>, XP_004085115).

<p>Identical residues in all sequences are indicated by (*) under the column, conserved substitutions are indicated by (:), and semi-conserved substitutions are indicated by (.). Deletions are indicated by dashes. The predicted peptide cleavage site is indicated by an arrow. Cysteine residues are shaded in light gray. Active site residues are shaded black and labeled (▼). Calcium binding residues (Asn122, Arg179, Asp188, and His222) are shown in bold and labeled (♣), and chloride binding site residues (Arg216, Asn317, Arg353) are shown in bold and labeled (♦). Positions of β-sheets and α-helices are indicated by lines over the sequence. Known conserved sequence regions in the alpha-amylase family: region VI in red, region I in yellow, region V in green, region II in blue, region III in grey, region IV in pink. The less conserved seventh region was not identified in β8. Asparagine predicted to be <i>N</i>-glycosylated is highlighted in red.