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{
"metadata": {
"accession": "IPR005201",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0033925",
"name": "mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0005737",
"name": "cytoplasm",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF03644": "Glycosyl hydrolase family 85"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR005201",
"name": "Cytosolic endo-beta-N-acetylglucosaminidase, TIM barrel domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Cytosolic endo-beta-N-acetylglucosaminidase, TIM barrel domain",
"short": "TIM_ENGase"
},
"description": [
{
"text": "<p>This describes the TIM barrel fold in ENGase, which contains a β/α fold [[cite:PUB00051965]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Endo-β-N-acetylglucosaminidase (ENGase) is a glycosyl hydrolase that cleaves the β-1,4-glycosidic bond within the di-N-acetylchitobiose core of N-glycosylated proteins, leaving one N-acetylglucosamine residue attached to the protein and releasing the remainder of the glycan. It plays a key role in the cytosolic degradation of free oligosaccharides derived from the endoplasmic reticulum, aiding in the recycling of sugars. ENGases possess an eight-stranded α/β barrel structure and belong to glycosyl hydrolase family 85 (GH85), sharing sequence similarity with [cazy:GH18] chitinases [[cite:PUB00160853]].</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": {
"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"
},
"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"
},
"PUB00160853": {
"PMID": 1233211,
"ISBN": null,
"volume": "8",
"issue": "2",
"year": 1975,
"title": "The measurement of drug consumption. Drugs for diabetes in Northern Ireland, Norway and Sweden.",
"URL": null,
"raw_pages": "83-9",
"medline_journal": "Eur J Clin Pharmacol",
"ISO_journal": "Eur J Clin Pharmacol",
"authors": [
"Bergman U",
"Elmes P",
"Halse M",
"Halvorsen T",
"Hood H",
"Lunde PK",
"Sjoqvist F",
"Wade OL",
"Westerholm B."
],
"DOI_URL": "https://doi.org/10.1007/BF00561555"
},
"PUB00051965": {
"PMID": 19252736,
"ISBN": null,
"volume": "4",
"issue": "3",
"year": 2009,
"title": "Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A.",
"URL": null,
"raw_pages": "e4658",
"medline_journal": "PLoS One",
"ISO_journal": "PLoS ONE",
"authors": [
"Yin J",
"Li L",
"Shaw N",
"Li Y",
"Song JK",
"Zhang W",
"Xia C",
"Zhang R",
"Joachimiak A",
"Zhang HC",
"Wang LX",
"Liu ZJ",
"Wang P."
],
"DOI_URL": "http://dx.doi.org/10.1371/journal.pone.0004658"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 222,
"interactions": 0,
"matches": 5401,
"pathways": 3,
"proteins": 5258,
"proteomes": 2940,
"sets": 0,
"structural_models": {
"alphafold": 4039,
"bfvd": 0
},
"structures": 6,
"taxa": 8093
},
"entry_annotations": {
"alignment:seed": 72,
"alignment:full": 2891
},
"cross_references": {
"cazy": {
"displayName": "CAZy",
"description": "Description of data source (to be defined in API)",
"rank": 20,
"accessions": [
{
"accession": "GH85",
"url": "http://www.cazy.org/GH85.html"
}
]
},
"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": "3.2.1.96",
"url": "https://enzyme.expasy.org/EC/3.2.1.96"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
