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InterPro: IPR000757 Glycoside hydrolase, family 16
Protein matches
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UniProtKB Matches: 2022 proteins |
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Accession
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IPR000757 Glyco_hydro_16 |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR013320 Concanavalin A-like lectin/glucanase, subgroup
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Found in
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IPR008264 Beta-glucanase
IPR016455 Xyloglucan endotransglucosylase/hydrolase
IPR017168 Glycoside hydrolase, family 16, CRH1, predicted
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Contains
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IPR008263 Glycoside hydrolase, family 16, active site
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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).
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Structural links
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Database links
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Pfam Clan: CL0004.16
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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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Tempel W, Liu ZJ, Horanyi PS, Deng L, Lee D, Newton MG, Rose JP, Ashida H, Li SC, Li YT, Wang BC.
Three-dimensional structure of GlcNAcalpha1-4Gal releasing endo-beta-galactosidase from Clostridium perfringens.
Proteins 59 2005 141-4
[PubMed: 15688452]
http://dx.doi.org/10.1002/prot.20363
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Allouch J, Helbert W, Henrissat B, Czjzek M.
Parallel substrate binding sites in a beta-agarase suggest a novel mode of action on double-helical agarose.
Structure 12 2004 623-32
[PubMed: 15062085]
http://dx.doi.org/10.1016/j.str.2004.02.020
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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, 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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