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alpha amylase C-terminal domain-containing protein
Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain. [1]. 8107092. Refined molecular structure of pig pancreatic alpha-amylase at 2.1 A resolution. Larson SB, Greenwood A, Cascio D, Day J, McPherson A;. J Mol Biol 1994;235:1560-1584. [2]. 9600843. Crystal structure of yellow meal worm alpha-amylase at 1.64 A resolution. Strobl S, Maskos K, Betz M, Wiegand G, Huber R, Gomis-Ruth FX, Glockshuber R;. J Mol Biol 1998;278:617-628. (from Pfam)
carbohydrate-binding module family 20 domain-containing protein
alpha-amylase family glycosyl hydrolase
alpha-amylase family protein; alpha-amylase family glycosyl hydrolase
alpha-amylase family protein may catalyze the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides| alpha-amylase family glycosyl hydrolase functions as a glycoside hydrolase that may act on starch, glycogen, and related oligo- and polysaccharides
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