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InterPro: IPR011613 Glycoside hydrolase 15-related
Protein matches
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UniProtKB Matches: 852 proteins |
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Accession
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IPR011613 Glyco_hydro_15_rel |
Secondary
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IPR000165
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Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR012341 Six-hairpin glycosidase
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Found in
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IPR000165 Glycoside hydrolase, family 15
IPR006425 Glucan 1,4-alpha-glucosidase
IPR006465 Glucoamylase
IPR008291 Glucan 1,4-alpha-glucosidase, starch-binding
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GO Term annotation
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Process
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GO:0005976 polysaccharide metabolic process
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Function
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GO:0004339 glucan 1,4-alpha-glucosidase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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.
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Structural links
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Database links
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Pfam Clan: CL0059.11
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Publications
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1.
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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
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2.
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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
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3.
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Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
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4.
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Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
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5.
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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
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6.
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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
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7.
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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
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Additional Reading
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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
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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
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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
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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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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
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