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InterPro: IPR011613 Glycoside hydrolase 15-related

Protein matchesHelp
UniProtKB
Matches:
852 proteins
AccessionHelp IPR011613 Glyco_hydro_15_rel
SecondaryHelp IPR000165
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR012341 Six-hairpin glycosidase
Found in IPR000165 Glycoside hydrolase, family 15
IPR006425 Glucan 1,4-alpha-glucosidase
IPR006465 Glucoamylase
IPR008291 Glucan 1,4-alpha-glucosidase, starch-binding
GO Term annotationHelp
Process GO:0005976 polysaccharide metabolic process
Function GO:0004339 glucan 1,4-alpha-glucosidase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

O-Glycosyl hydrolases EC:3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.

Glycoside hydrolase family 15 GH15 comprises enzymes with several known activities; glucoamylase (EC:3.2.1.3); alpha-glucosidase (EC:3.2.1.20); glucodextranase (EC:3.2.1.70).

Glucoamylase (GA) catalyses the release of D-glucose from the non-reducing ends of starch and other oligo- or poly-saccharides. Studies of fungal GA have indicated 3 closely-clustered acidic residues that play a role in the catalytic mechanism [5]. This region is also conserved in a recently sequenced bacterial GA [6].

The 3D structure of the pseudo-tetrasaccharide acarbose complexed with glucoamylase II(471) from Aspergillus awamori var. X100 has been determined to 2.4A resolution [7]. The protein belongs to the mainly-alpha class, and contains 19 helices and 9 strands.

Structural linksHelp
CATH: 1.50.10.10
Database linksHelp
Enzyme: EC:3.2.1.3
PANDIT: PF00723
Pfam Clan: CL0059.11

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR011613 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P04065 Glucoamylase S1

P07683 Glucoamylase 1

P29761 Glucoamylase

Q59005 Uncharacterized glycosyl hydrolase MJ1610

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR006425 Glucan 1,4-alpha-glucosidase
IPR015220 Glucodextranase N
IPR014718 Glycoside hydrolase-type carbohydrate-binding, subgroup
IPR006465 Glucoamylase
IPR005036 Putative phosphatase regulatory subunit
IPR011013 Glycoside hydrolase-type carbohydrate-binding
IPR012341 Six-hairpin glycosidase
IPR008928 Six-hairpin glycosidase-like
IPR011613 Glycoside hydrolase 15-related
IPR000165 Glycoside hydrolase, family 15
PDB Chain
ModBase
SWISS-MODEL

PublicationsHelp
1. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G.
Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995 [PubMed: 7624375]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
2. Davies G, Henrissat B.
Structures and mechanisms of glycosyl hydrolases.
Structure 3 853-9 1995 [PubMed: 8535779]
http://dx.doi.org/10.1016/S0969-2126(01)00220-9
3. Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
4. Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
5. Sierks MR, Ford C, Reilly PJ, Svensson B.
Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.
Protein Eng. 3 193-8 1990 [PubMed: 1970434]
http://dx.doi.org/10.1093/protein/3.3.193
6. Ohnishi H, Kitamura H, Minowa T, Sakai H, Ohta T.
Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme.
Eur. J. Biochem. 207 413-8 1992 [PubMed: 1633799]
http://dx.doi.org/10.1111/j.1432-1033.1992.tb17064.x
7. 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 15631-9 1994 [PubMed: 8195212]
http://intl.jbc.org/cgi/reprint/269/22/15631.pdf

Additional ReadingHelp
Sevcik J, Solovicova A, Hostinova E, Gasperik J, Wilson KS, Dauter Z.
Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 54 1998 854-66 [PubMed: 9757101]
http://dx.doi.org/10.1107/S0907444998002005
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 2004 10575-83 [PubMed: 14660574]
http://dx.doi.org/10.1074/jbc.M310771200
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, 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
Sevcik J, Hostinova E, Solovicova A, Gasperik J, Dauter Z, Wilson KS.
Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain.
FEBS J. 273 2006 2161-71 [PubMed: 16649993]
http://dx.doi.org/10.1111/j.1742-4658.2006.05230.x
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InterPro 23.1