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{
"metadata": {
"accession": "IPR031481",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF17039": "Fucosyltransferase, N-terminal"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR031481",
"name": "Fucosyltransferase, N-terminal",
"type": "Domain",
"children": []
},
"name": {
"name": "Fucosyltransferase, N-terminal",
"short": "Glyco_tran_10_N"
},
"description": [
{
"text": "<p>This is the N-terminal domain of a family of fucosyltransferases, known as glycosyltransferase family 10 [[cite:PUB00009409], [cite:PUB00075886]]. This enzyme transfers fucose from GDP-Fucose to GlcNAc in an alpha1,3 linkage [[cite:PUB00001989]]. The N-terminal domain folds as a Rossmann-like domain and is involved in sugar donor interactions [[cite:PUB00155286]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00155286": {
"PMID": 37202521,
"ISBN": null,
"volume": "19",
"issue": "8",
"year": 2023,
"title": "Structural basis for Lewis antigen synthesis by the α1,3-fucosyltransferase FUT9.",
"URL": null,
"raw_pages": "1022-1030",
"medline_journal": "Nat Chem Biol",
"ISO_journal": "Nat Chem Biol",
"authors": [
"Kadirvelraj R",
"Boruah BM",
"Wang S",
"Chapla D",
"Huang C",
"Ramiah A",
"Hudson KL",
"Prudden AR",
"Boons GJ",
"Withers SG",
"Wood ZA",
"Moremen KW."
],
"DOI_URL": "https://doi.org/10.1038/s41589-023-01345-y"
},
"PUB00001989": {
"PMID": 9451017,
"ISBN": null,
"volume": "8",
"issue": "1",
"year": 1998,
"title": "Conserved structural features in eukaryotic and prokaryotic fucosyltransferases.",
"URL": null,
"raw_pages": "87-94",
"medline_journal": "Glycobiology",
"ISO_journal": "Glycobiology",
"authors": [
"Breton C",
"Oriol R",
"Imberty A."
],
"DOI_URL": "http://dx.doi.org/10.1093/glycob/8.1.87"
},
"PUB00009409": {
"PMID": 9334165,
"ISBN": null,
"volume": "326 ( Pt 3)",
"issue": null,
"year": 1997,
"title": "A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities.",
"URL": null,
"raw_pages": "929-39",
"medline_journal": "Biochem J",
"ISO_journal": "Biochem. J.",
"authors": [
"Campbell JA",
"Davies GJ",
"Bulone V",
"Henrissat B."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9334165"
},
"PUB00075886": {
"PMID": 17251184,
"ISBN": null,
"volume": "282",
"issue": "13",
"year": 2007,
"title": "Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design.",
"URL": null,
"raw_pages": "9973-82",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Sun HY",
"Lin SW",
"Ko TP",
"Pan JF",
"Liu CL",
"Lin CN",
"Wang AH",
"Lin CH."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M610285200"
},
"PUB00155244": {
"PMID": 19088067,
"ISBN": null,
"volume": "284",
"issue": "7",
"year": 2009,
"title": "Activity, splice variants, conserved peptide motifs, and phylogeny of two new alpha1,3-fucosyltransferase families (FUT10 and FUT11).",
"URL": null,
"raw_pages": "4723-38",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Mollicone R",
"Moore SE",
"Bovin N",
"Garcia-Rosasco M",
"Candelier JJ",
"Martinez-Duncker I",
"Oriol R."
],
"DOI_URL": "https://doi.org/10.1074/jbc.M809312200"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 162,
"interactions": 0,
"matches": 12381,
"pathways": 14,
"proteins": 12275,
"proteomes": 1343,
"sets": 0,
"structural_models": {
"alphafold": 10904,
"bfvd": 0
},
"structures": 8,
"taxa": 4836
},
"entry_annotations": {
"alignment:seed": 67,
"alignment:full": 8281
},
"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": "2.4.1",
"url": "https://enzyme.expasy.org/EC/2.4.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
