EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR008291 Glucan 1,4-alpha-glucosidase, starch-binding

Protein matches Help

UniProtKB

Matches:

70 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR008291 Glucamylse_SBD

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF001031	Glu-a-glcsd_SBD	70
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000165 Glycoside hydrolase, family 15

Contains

IPR002044 Glycoside hydrolase, carbohydrate-binding
IPR011613 Glycoside hydrolase 15-related
IPR013783 Immunoglobulin-like fold

GO Term annotation Help

Process

GO:0000272 polysaccharide catabolic process

Function

GO:0004339 glucan 1,4-alpha-glucosidase activity

InterPro annotation

Entry Details in BioMart

Abstract

Glucan 1,4-alpha-glucosidase (glucoamylase; EC:3.2.1.3) catalyses the release of glucose from the non-reducing ends of starch and related polysaccharides. Smaller molecular forms of the enzyme, G2, arise by proteolytic cleavage(s) of the carboxyl end of the large form, G1. Only G1 adsorbs and digests raw starch, but both forms are equally active towards soluble poly- and oligosaccharides [1]. The majority of these enzymes are multidomain proteins consisting of a catalytic domain connected to a starch-binding domain (SBD) by an O-glycosylated linker region. Glu179 and Glu400 of the the Aspergillus niger sequence is involved in the general acid catalysis of the enzyme. Conserved tryptophan residues are involved in interactions of the glucoamylases with substrates and inhibitors [2].

Structural links Help

PDB - click here

SCOP: a.102.1.1 , b.3.1.1

CATH: 1.50.10.10 , 2.60.40.10

Database links Help

Enzyme: EC:3.2.1.3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008291

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P22832 Glucoamylase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002044	Glycoside hydrolase, carbohydrate-binding
IPR013784	Carbohydrate-binding-like fold
IPR013783	Immunoglobulin-like fold
IPR012341	Six-hairpin glycosidase
IPR008928	Six-hairpin glycosidase-like
IPR008291	Glucan 1,4-alpha-glucosidase, starch-binding
IPR011613	Glycoside hydrolase 15-related
IPR000165	Glycoside hydrolase, family 15
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Svensson B, Larsen K, Gunnarsson A. Characterization of a glucoamylase G2 from Aspergillus niger. Eur. J. Biochem. 154 497-502 1986 [PubMed: 3081341] http://dx.doi.org/10.1111/j.1432-1033.1986.tb09425.x
2.	Gottschalk TE, Fierobe HP, Mirgorodskaya E, Clarke AJ, Tull D, Sigurskjold BW, Christensen T, Payre N, Frandsen TP, Juge N, McGuire KA, Cottaz S, Roepstorff P, Driguez H, Williamson G, Svensson B. Structure, function and protein engineering of starch-degrading enzymes. Biochem. Soc. Trans. 26 198-204 1998 [PubMed: 9649747] http://www.biochemsoctrans.org/bst/026/0198/bst0260198.htm

Additional Reading Open in usermanual
	Sorimachi K, Jacks AJ, Le Gal-Coeffet MF, Williamson G, Archer DB, Williamson MP. Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 259 1996 970-87 [PubMed: 8683599] http://dx.doi.org/10.1006/jmbi.1996.0374
	Sorimachi K, Le Gal-Coeffet MF, Williamson G, Archer DB, Williamson MP. Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin. Structure 5 1997 647-61 [PubMed: 9195884] http://dx.doi.org/10.1016/S0969-2126(97)00220-7
	Aleshin AE, Stoffer B, Firsov LM, Svensson B, Honzatko RB. Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism. Biochemistry 35 1996 8319-28 [PubMed: 8679589] http://dx.doi.org/10.1021/bi960321g
	Aleshin AE, Hoffman C, Firsov LM, Honzatko RB. Refined crystal structures of glucoamylase from Aspergillus awamori var. X100. J. Mol. Biol. 238 1994 575-91 [PubMed: 8176747] http://dx.doi.org/10.1006/jmbi.1994.1316
	Aleshin AE, Firsov LM, Honzatko RB. Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution. J. Biol. Chem. 269 1994 15631-9 [PubMed: 8195212] http://intl.jbc.org/cgi/reprint/269/22/15631.pdf

InterPro 23.1