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InterPro: IPR008263 Glycoside hydrolase, family 16, active site
Protein matches
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UniProtKB Matches: 473 proteins |
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Accession
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IPR008263 Glycoside_hydrolase_16_AS |
Secondary
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IPR000757
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Type
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Active_site |
Signatures
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InterPro Relationships
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Found in
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IPR000757 Glycoside hydrolase, family 16
IPR008264 Beta-glucanase
IPR008985 Concanavalin A-like lectin/glucanase
IPR013320 Concanavalin A-like lectin/glucanase, subgroup
IPR016455 Xyloglucan endotransglucosylase/hydrolase
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GO Term annotation
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Process
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GO:0005975 carbohydrate metabolic process
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Function
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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.
Glycoside hydrolase family 16 GH16 comprises enzymes with a number of known activities; lichenase (EC:3.2.1.73); xyloglucan xyloglucosyltransferase (EC:2.4.1.207); agarase (EC:3.2.1.81); kappa-carrageenase (EC:3.2.1.83); endo-beta-1,3-glucanase (EC:3.2.1.39); endo-beta-1,3-1,4-glucanase (EC:3.2.1.6); endo-beta-galactosidase (EC:3.2.1.103). Two closely clustered and conserved glutamates, which are part of this signature, have been shown to be involved in the catalytic activity of Bacillus licheniformis.
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Structural links
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Database links
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Additional Reading
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Gaiser OJ, Piotukh K, Ponnuswamy MN, Planas A, Borriss R, Heinemann U.
Structural basis for the substrate specificity of a Bacillus 1,3-1,4-beta-glucanase.
J. Mol. Biol. 357 2006 1211-25
[PubMed: 16483609]
http://dx.doi.org/10.1016/j.jmb.2006.01.014
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Michel G, Chantalat L, Duee E, Barbeyron T, Henrissat B, Kloareg B, Dideberg O.
The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases.
Structure 9 2001 513-25
[PubMed: 11435116]
http://dx.doi.org/10.1016/S0969-2126(01)00612-8
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Johansson P, Brumer H 3rd, Baumann MJ, Kallas AM, Henriksson H, Denman SE, Teeri TT, Jones TA.
Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding.
Plant Cell 16 2004 874-86
[PubMed: 15020748]
http://dx.doi.org/10.1105/tpc.020065
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Tsai LC, Shyur LF, Lee SH, Lin SS, Yuan HS.
Crystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes.
J. Mol. Biol. 330 2003 607-20
[PubMed: 12842475]
http://dx.doi.org/10.1016/S0022-2836(03)00630-2
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Juncosa M, Pons J, Dot T, Querol E, Planas A.
Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed mutagenesis.
J. Biol. Chem. 269 1994 14530-5
[PubMed: 8182059]
http://intl.jbc.org/cgi/content/abstract/269/20/14530
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Henrissat B.
A classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 280 ( Pt 2) 1991 309-16
[PubMed: 1747104]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104
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Tsai LC, Shyur LF, Cheng YS, Lee SH.
Crystal structure of truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase in complex with beta-1,3-1,4-cellotriose.
J. Mol. Biol. 354 2005 642-51
[PubMed: 16246371]
http://dx.doi.org/10.1016/j.jmb.2005.09.041
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InterPro 23.1
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