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{
"metadata": {
"accession": "IPR027350",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"profile": {
"PS51659": "Glycosyltransferase family 23 (GT23) domain profile"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR027350",
"name": "Glycosyltransferase family 23 (GT23) domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Glycosyltransferase family 23 (GT23) domain",
"short": "GT23_dom"
},
"description": [
{
"text": "<p>The fucosylation of glycoconjugates in mammalian organisms is related to a wide variety of biological processes, including cell adhesion, blood antigens, and some severe diseases including cancer metastasis, congenital disorders of glycosylation, and various microbial and virus infections. Fucosylation via alpha1,2-, alpha1,3- alpha1,4, and alpha1,6-linkages, and protein O-fucosylation are accomplished by the cation of specific individual fucosyltransferases [[cite:PUB00040227]].</p>\n\n<p>FUT8, a eukaryotic alpha1,6-fucosyltransferase, catalyses the transfer of a fucosyl residue from guanine nucleotide diphosphate (GDP)-beta-L-fucose to the reducing terminal N-acetylglucosamine (GlcNAc) of asparagine-linked oligosaccharides (N-glycan). The catalytic domain of FUT8 is structurally similar to that of BodZ, a bacterial alpha1,6-fucosyltransferase. NodZ plays a role in the synthesis of the Nod factor, which is involved in the nodulation of legume roots for nitrogen fixing, and is known to catalyse the alpha1,6- fucosylation of lipo-chitooligosaccharides and variations thereof, including chitooligosaccharides. Both the eukaryotic and bacterial fucoslytransferase are classified into the GT23 family of Carbohydrate-Active enZYmes and share GDP-beta-L-fucose as the donor substrate. Although the acceptor substrates are different, a \"common\" chitobiose unit is contained in the reducing terminals of both substrates [[cite:PUB00063920]].</p>\n\n<p>The GT23 domain is comprised of two structures, a N-terminal open sheet α/β structure and a C-terminal Rossmann fold which is frequently found in nucleotide binding proteins including glycosyltransferases [[cite:PUB00040227], [cite:PUB00047601], [cite:PUB00058386]]. The entry represents the GT23 domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00040227": {
"PMID": 17172260,
"ISBN": null,
"volume": "17",
"issue": "5",
"year": 2007,
"title": "Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8.",
"URL": null,
"raw_pages": "455-66",
"medline_journal": "Glycobiology",
"ISO_journal": "Glycobiology",
"authors": [
"Ihara H",
"Ikeda Y",
"Toma S",
"Wang X",
"Suzuki T",
"Gu J",
"Miyoshi E",
"Tsukihara T",
"Honke K",
"Matsumoto A",
"Nakagawa A",
"Taniguchi N."
],
"DOI_URL": "http://dx.doi.org/10.1093/glycob/cwl079"
},
"PUB00063920": {
"PMID": 20466647,
"ISBN": null,
"volume": "20",
"issue": "8",
"year": 2010,
"title": "Fucosylation of chitooligosaccharides by human alpha1,6-fucosyltransferase requires a nonreducing terminal chitotriose unit as a minimal structure.",
"URL": null,
"raw_pages": "1021-33",
"medline_journal": "Glycobiology",
"ISO_journal": "Glycobiology",
"authors": [
"Ihara H",
"Hanashima S",
"Okada T",
"Ito R",
"Yamaguchi Y",
"Taniguchi N",
"Ikeda Y."
],
"DOI_URL": "http://dx.doi.org/10.1093/glycob/cwq064"
},
"PUB00047601": {
"PMID": 17762900,
"ISBN": null,
"volume": "54",
"issue": "3",
"year": 2007,
"title": "High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor.",
"URL": null,
"raw_pages": "537-49",
"medline_journal": "Acta Biochim Pol",
"ISO_journal": "Acta Biochim. Pol.",
"authors": [
"Brzezinski K",
"Stepkowski T",
"Panjikar S",
"Bujacz G",
"Jaskolski M."
],
"DOI_URL": null
},
"PUB00058386": {
"PMID": 22281745,
"ISBN": null,
"volume": "68",
"issue": "Pt 2",
"year": 2012,
"title": "Structures of NodZ α1,6-fucosyltransferase in complex with GDP and GDP-fucose.",
"URL": null,
"raw_pages": "160-8",
"medline_journal": "Acta Crystallogr D Biol Crystallogr",
"ISO_journal": "Acta Crystallogr. D Biol. Crystallogr.",
"authors": [
"Brzezinski K",
"Dauter Z",
"Jaskolski M."
],
"DOI_URL": "http://dx.doi.org/10.1107/S0907444911053157"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 3488,
"pathways": 8,
"proteins": 3449,
"proteomes": 1257,
"sets": 0,
"structural_models": {
"alphafold": 3144,
"bfvd": 0
},
"structures": 16,
"taxa": 4720
},
"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": "2.4.1.68",
"url": "https://enzyme.expasy.org/EC/2.4.1.68"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2hhc",
"name": "Crystal structure of fucosyltransferase NodZ from Bradyrhizobium"
}
}
}
