Protein Family Models

This domain is found in a range of enzymes that act on branched substrates - isoamylase, pullulanase and branching enzyme. This family also contains the beta subunit of 5' AMP activated kinase. [1]. 9719642. Three-dimensional structure of Pseudomonas isoamylase at 2.2 A resolution. Katsuya Y, Mezaki Y, Kubota M, Matsuura Y;. J Mol Biol 1998;281:885-897. [2]. 14673168. Mutations in the gal83 glycogen-binding domain activate the snf1/gal83 kinase pathway by a glycogen-independent mechanism. Wiatrowski HA, Van Denderen BJ, Berkey CD, Kemp BE, Stapleton D, Carlson M;. Mol Cell Biol 2004;24:352-361. [3]. 12747837. AMPK beta subunit targets metabolic stress sensing to glycogen. Polekhina G, Gupta A, Michell BJ, van Denderen B, Murthy S, Feil SC, Jennings IG, Campbell DJ, Witters LA, Parker MW, Kemp BE, Stapleton D;. Curr Biol 2003;13:867-871. [4]. 12747836. A novel domain in AMP-activated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias. Hudson ER, Pan DA, James J, Lucocq JM, Hawley SA, Green KA, Baba O, Terashima T, Hardie DG;. Curr Biol 2003;13:861-866. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

glycogen debranching protein (GlgX) hydrolyzes (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin, and their beta-limit dextrins

Date:

2024-08-21

This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This HMM distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase.

Gene:

glgX

Date:

2024-05-30