Protein Family Models

Date:

2024-08-14

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:

2024-08-14

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:

2024-08-14

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:

2024-08-14

1,4-alpha-glucan-branching protein transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain

Date:

2024-08-15

Catalyzes the transfer of a segment of a 1,4-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain

Gene:

glgB

Date:

2021-08-24

This HMM describes the glycogen branching enzymes which are responsible for the transfer of chains of approx. 7 alpha(1--4)-linked glucosyl residues to other similar chains (in new alpha(1--6) linkages) in the biosynthesis of glycogen. This enzyme is a member of the broader amylase family of starch hydrolases which fold as (beta/alpha)8 barrels, the so-called TIM-barrel structure [1,2]. All of the sequences comprising the seed of this model have been experimentally characterized. (For instance, [3]). This model encompasses both bacterial and eukaryotic species. No archaea have this enzyme, although Aquifex aolicus does. Two species, Bacillus thuringiensis and Clostridium perfringens have two sequences each which are annotated as amylases. These annotations are aparrently in error. GP|18143720 from C. perfringens, for instance, contains the note "674 aa, similar to gp:A14658_1 amylase (1,4-alpha-glucan branching enzyme (EC 2.4.1.18) ) from Bacillus thuringiensis (648 aa); 51.1% identity in 632 aa overlap." A branching enzyme from Porphyromonas gingivales, OMNI|PG1793, appears to be more closely related to the eukaryotic species (across a deep phylogenetic split) and may represent an instance of lateral transfer from this species' host. A sequence from Arabidopsis thaliana, GP|9294564, scores just above trusted, but appears either to contain corrupt sequence or, more likely, to be a pseudogene as some of the conserved catalytic residues common to the alpha amylase family are not conserved here.

Gene:

glgB

Date:

2021-04-27

Catalyzes the transfer of a segment of a 1,4-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain

Gene:

glgB

Date:

2021-07-22