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{
"metadata": {
"accession": "PS51762",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
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"integrated": "IPR000757",
"hierarchy": null,
"name": {
"name": "Glycosyl hydrolases family 16 (GH16) domain profile",
"short": "GH16_2"
},
"description": [
{
"text": "<p>The glycosyl hydrolases family 16 (GH16) [[cite:PUB00000503]] contains functionally\nheterogeneous members, including beta-agarases, endo-1,3-beta-glucanases\n(laminarinases), endo-beta-1,3-1,4-glucanases (lichenases), kappa-\ncarrageenases, endo-beta-galactosidases and xyloglucan endotransferases. These\nenzymes share a common ancestor and have diverged significantly in their\nprimary sequence.\n\nThe GH16 catalytic domain has a classical sandwich-like beta-jelly roll fold,\nformed by two main, closely packed and curved antiparallel beta sheets,\ncreating a deep channel harboring the catalytic machinery.\nEven though the GH16 domains have now diverged significantly in their primary\nsequences, they all feature a common catalytic motif, E-[ILV]-D-[IVAF]-\n[VILMF](0,1)-E. The two glutamic acid residues in the conserved motif are the\nnucleophile and the general base involved in catalysis, whereas the aspartic\nacid residue is important in maintaining the relative position of these\ncatalytic amino acids [[cite:PUB00029321]][[cite:PUB00010686]].\n\nSome proteins known to contain a GH16 domain are listed below:\n\n - Bacterial beta-1,3-1,4-glucanases, or lichenases, (EC 3.2.1.73) mainly from\n Bacillus but also from Clostridium thermocellum (gene licB), Fibrobacter\n succinogenes and Rhodothermus marinus (gene bglA).\n - Bacillus circulans beta-1,3-glucanase A1 (EC 3.2.1.39) (gene glcA).\n - Alteromonas carrageenovora kappa-carrageenase (EC 3.2.1.83) (gene cgkA).\n - Rhizobium meliloti endo-1,3-1,4-beta-glycanase exoK.\n - Streptomyces coelicolor agarase (EC 3.2.1.81) (gene dagA).\n - Zobellia galactanivorans beta-agarase A (EC 3.2.1.81) (gene agaA).\n - Zobellia galactanivorans beta-agarase B (EC 3.2.1.81) (gene agaB).\n - Saccharophagus sp. AG21 beta-agarase (gene agy1), includes a GH16 domain\n and two CBM6 (carbohydrate binding type-6) domain.\n - Microbulbifer thermotolerans agarase (agaA).\n - Thermotoga maritima laminarinase.\n - Saccharomyces cerevisiae beta-glucan synthesis-associated protein SKN1 [[cite:PUB00016652]].\n - Saccharomyces cerevisiae beta-glucan synthesis-associated protein KRE6 [[cite:PUB00016652]].\n\nTwo closely clustered conserved glutamates have been shown [[cite:PUB00002845]] to be involved\nin the catalytic activity of Bacillus licheniformis lichenase. We used the\nregion that contains these residues as a signature pattern. We have also\ndeveloped a profile that covers the entire GH16 domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00002845": {
"PMID": 8182059,
"ISBN": null,
"volume": "269",
"issue": "20",
"year": 1994,
"title": "Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed mutagenesis.",
"URL": null,
"raw_pages": "14530-5",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Juncosa M",
"Pons J",
"Dot T",
"Querol E",
"Planas A."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/269/20/14530"
},
"PUB00010686": {
"PMID": 11435116,
"ISBN": null,
"volume": "9",
"issue": "6",
"year": 2001,
"title": "The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases.",
"URL": null,
"raw_pages": "513-25",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Michel G",
"Chantalat L",
"Duee E",
"Barbeyron T",
"Henrissat B",
"Kloareg B",
"Dideberg O."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(01)00612-8"
},
"PUB00016652": {
"PMID": 10601196,
"ISBN": null,
"volume": "181",
"issue": "24",
"year": 1999,
"title": "Localization of synthesis of beta1,6-glucan in Saccharomyces cerevisiae.",
"URL": null,
"raw_pages": "7414-20",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Montijn RC",
"Vink E",
"Muller WH",
"Verkleij AJ",
"Van Den Ende H",
"Henrissat B",
"Klis FM."
],
"DOI_URL": "http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=10601196"
},
"PUB00029321": {
"PMID": 12970344,
"ISBN": null,
"volume": "278",
"issue": "47",
"year": 2003,
"title": "The three-dimensional structures of two beta-agarases.",
"URL": null,
"raw_pages": "47171-80",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Allouch J",
"Jam M",
"Helbert W",
"Barbeyron T",
"Kloareg B",
"Henrissat B",
"Czjzek M."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M308313200"
},
"PUB00000503": {
"PMID": 1747104,
"ISBN": null,
"volume": "280 ( Pt 2)",
"issue": null,
"year": 1991,
"title": "A classification of glycosyl hydrolases based on amino acid sequence similarities.",
"URL": null,
"raw_pages": "309-16",
"medline_journal": "Biochem J",
"ISO_journal": "Biochem. J.",
"authors": [
"Henrissat B."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104"
}
},
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"interactions": 0,
"matches": 69989,
"pathways": 0,
"proteins": 69537,
"proteomes": 9131,
"sets": 0,
"structural_models": {
"alphafold": 56358,
"bfvd": 3
},
"structures": 119,
"taxa": 17620
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "7eo3",
"name": "X-ray structure analysis of beita-1,3-glucanase"
}
}
}
