Protein Family Models

This domain is found close to the N-terminus of the Klebsiella starch debranching pullulanase enzyme [1]. The structure of the domain is a beta sandwich fold. [1]. 16650854. Crystal structure of pullulanase: evidence for parallel binding of oligosaccharides in the active site. Mikami B, Iwamoto H, Malle D, Yoon HJ, Demirkan-Sarikaya E, Mezaki Y, Katsuya Y;. J Mol Biol. 2006;359:690-707. (from Pfam)

Date:

2024-10-16

This entry represents the uncharacterised C-terminal domain of secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants [1]. Both enzymes hydrolyse alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. [1]. 18815382. Further evidence for the mandatory nature of polysaccharide debranching for the aggregation of semicrystalline starch and for overlapping functions of debranching enzymes in Arabidopsis leaves. Wattebled F, Planchot V, Dong Y, Szydlowski N, Pontoire B, Devin A, Ball S, D'Hulst C;. Plant Physiol. 2008;148:1309-1323. (from Pfam)

Date:

2024-10-16

Domain is found in pullanase - carbohydrate de-branching - proteins. It is found both to the N or the C terminii of of the alpha-amylase active site region. This domain contains several conserved aromatic residues that are suggestive of a carbohydrate binding function. [1]. 12625841. New Knowledge from Old: In silico discovery of novel protein domains in Streptomyces coelicolor. Yeats C, Bentley S, Bateman A;. BMC Microbiol 2003;3:3-3. (from Pfam)

Date:

2024-10-16

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

type I pullulanase which catalyzes the hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen; similar to Thermotoga maritima type I pullulanase

Date:

2019-03-21