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InterPro: IPR011837 Glycogen debranching enzyme GlgX
Protein matches
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UniProtKB Matches: 830 proteins |
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Accession
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IPR011837 GlgX_debranch |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR004193 Glycoside hydrolase, family 13, N-terminal
IPR006047 Glycosyl hydrolase, family 13, catalytic domain
IPR013780 Glycosyl hydrolase, family 13, all-beta
IPR013783 Immunoglobulin-like fold
IPR014756 Immunoglobulin E-set
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GO Term annotation
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Process
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GO:0005980 glycogen catabolic process
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Function
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GO:0004133 glycogen debranching enzyme activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
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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.
This entry represents the glycogen debranching enzyme GlgX found in Escherichia coli, as well as its equivalogs in other prokaryotic species. This enzyme encodes an isoamylase-type debranching enzyme with high specificity for hydrolysis of chains consisting of three or four glucose residues, and is classed as family 13 of glycosyl hydrolases [5]. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This entry distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages [6].
More information about this protein can be found at Protein of the Month: alpha-Amylase [7].
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Database links
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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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Dauvillee D, Kinderf IS, Li Z, Kosar-Hashemi B, Samuel MS, Rampling L, Ball S, Morell MK.
Role of the Escherichia coli glgX gene in glycogen metabolism.
J. Bacteriol. 187 1465-73 2005
[PubMed: 15687211]
http://dx.doi.org/10.1128/JB.187.4.1465-1473.2005
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6.
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Yang H, Liu MY, Romeo T.
Coordinate genetic regulation of glycogen catabolism and biosynthesis in Escherichia coli via the CsrA gene product.
J. Bacteriol. 178 1012-7 1996
[PubMed: 8576033]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8576033
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7.
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McDowall J.
Protein of the Month ? alpha-Amylase.
2006
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InterPro 23.1
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