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InterPro: IPR015220 Glucodextranase N

Protein matchesHelp
UniProtKB
Matches:
96 proteins
AccessionHelp IPR015220 Glucodextran_N
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR014718 Glycoside hydrolase-type carbohydrate-binding, subgroup
Found in IPR006425 Glucan 1,4-alpha-glucosidase
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Glucodextranase domain N, uniquely found in bacterial and archaeal glucoamylases and glucodextranases, adopts a structure consisting of 17 antiparallel beta-strands. These beta-strands are divided into two beta-sheets, and one of the beta-sheets is wrapped by an extended polypeptide, which appears to stabilise the domain. This domain, together with glycoside hydrolase domain A (IPR011613), is mainly involved with catalytic activity, hydrolysing alpha-1,6-glucosidic linkages of dextran to release beta-D-glucose from the non-reducing end via an inverting reaction mechanism [1].

Structural linksHelp
SCOP: b.30.5.5
CATH: 2.70.98.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR015220 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P29761 Glucoamylase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR012341 Six-hairpin glycosidase
IPR006425 Glucan 1,4-alpha-glucosidase
IPR008928 Six-hairpin glycosidase-like
IPR015220 Glucodextranase N
IPR014718 Glycoside hydrolase-type carbohydrate-binding, subgroup
IPR011613 Glycoside hydrolase 15-related
IPR000165 Glycoside hydrolase, family 15
IPR011013 Glycoside hydrolase-type carbohydrate-binding
SWISS-MODEL
ModBase

PublicationsHelp
1. Mizuno M, Tonozuka T, Suzuki S, Uotsu-Tomita R, Kamitori S, Nishikawa A, Sakano Y.
Structural insights into substrate specificity and function of glucodextranase.
J. Biol. Chem. 279 10575-83 2004 [PubMed: 14660574]
http://dx.doi.org/10.1074/jbc.M310771200

Additional ReadingHelp
Aleshin AE, Feng PH, Honzatko RB, Reilly PJ.
Crystal structure and evolution of a prokaryotic glucoamylase.
J. Mol. Biol. 327 2003 61-73 [PubMed: 12614608]
http://dx.doi.org/10.1016/S0022-2836(03)00084-6
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InterPro 24.0