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{
"metadata": {
"accession": "IPR036156",
"entry_id": null,
"type": "homologous_superfamily",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"ssf": {
"SSF49303": "beta-Galactosidase/glucuronidase domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR036156",
"name": "Beta-Galactosidase/glucuronidase domain superfamily",
"type": "Homologous_superfamily",
"children": []
},
"name": {
"name": "Beta-Galactosidase/glucuronidase domain superfamily",
"short": "Beta-gal/glucu_dom_sf"
},
"description": [
{
"text": "<p>This entry describes the beta-galactosidase/glucuronidase domain superfamily which has an immunoglobulin-like β-sandwich fold composed of seven strands in two sheets, it has a greek-key topology [[cite:PUB00004183]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Glycoside hydrolase family 2 [cazy:GH2]\r\ncomprises enzymes with several known activities: beta-galactosidase ([ec:3.2.1.23]); beta-mannosidase ([ec:3.2.1.25]); beta-glucuronidase ([ec:3.2.1.31]).</p>\r\n\r\n<p>These enzymes contain a conserved glutamic acid residue which has been shown [[cite:PUB00002709]], in Escherichia coli lacZ ([swissprot:P00722]), to be the general acid/base catalyst in the active site of the enzyme.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>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 [[cite:PUB00004870], [cite:PUB00005266]]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) website.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00004183": {
"PMID": 8008071,
"ISBN": null,
"volume": "369",
"issue": "6483",
"year": 1994,
"title": "Three-dimensional structure of beta-galactosidase from E. coli.",
"URL": null,
"raw_pages": "761-6",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Jacobson RH",
"Zhang XJ",
"DuBose RF",
"Matthews BW."
],
"DOI_URL": "http://dx.doi.org/10.1038/369761a0"
},
"PUB00002709": {
"PMID": 1350782,
"ISBN": null,
"volume": "267",
"issue": "16",
"year": 1992,
"title": "Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli.",
"URL": null,
"raw_pages": "11126-30",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Gebler JC",
"Aebersold R",
"Withers SG."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/267/16/11126.pdf"
},
"PUB00004870": {
"PMID": 7624375,
"ISBN": null,
"volume": "92",
"issue": "15",
"year": 1995,
"title": "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"URL": null,
"raw_pages": "7090-4",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Henrissat B",
"Callebaut I",
"Fabrega S",
"Lehn P",
"Mornon JP",
"Davies G."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf"
},
"PUB00005266": {
"PMID": 8535779,
"ISBN": null,
"volume": "3",
"issue": "9",
"year": 1995,
"title": "Structures and mechanisms of glycosyl hydrolases.",
"URL": null,
"raw_pages": "853-9",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Davies G",
"Henrissat B."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(01)00220-9"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR013783",
"name": "Immunoglobulin-like fold",
"type": "homologous_superfamily"
},
{
"accession": "IPR006102",
"name": "Glycoside hydrolase family 2, immunoglobulin-like beta-sandwich",
"type": "domain"
},
{
"accession": "IPR032312",
"name": "Beta-galactosidase, domain 4",
"type": "domain"
},
{
"accession": "IPR041625",
"name": "Beta-mannosidase, Ig-fold domain",
"type": "domain"
},
{
"accession": "IPR041351",
"name": "Exo-beta-D-glucosaminidase, Ig-fold domain",
"type": "domain"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 95102,
"pathways": 19,
"proteins": 64649,
"proteomes": 11466,
"sets": 0,
"structural_models": {
"alphafold": 48737,
"bfvd": 0
},
"structures": 259,
"taxa": 22793
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "3.2.1",
"url": "https://enzyme.expasy.org/EC/3.2.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
