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{
"metadata": {
"accession": "IPR010737",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF07005": "Sugar-binding N-terminal domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR010737",
"name": "Four-carbon acid sugar kinase, N-terminal domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Four-carbon acid sugar kinase, N-terminal domain",
"short": "4-carb_acid_sugar_kinase_N"
},
"description": [
{
"text": "<p>This conserved region is found in four-carbon acid sugar kinases from a range of Proteobacteria as well as the Gram-positive Oceanobacillus iheyensis. These four-carbon acid sugar kinases are composed of two domains: an N-terminal domain and a C-terminal domain connected by a variable linker sequence. The N-terminal domain exhibits an α/β-fold composed of an eight-stranded parallel β-sheet. The C-terminal domain also exhibits an α/β-fold composed of a seven-stranded mixed β-sheet. The acid sugar is bound by the N-terminal domain, while nucleotide by the C-terminal domain [[cite:PUB00085179]].</p>\n\n<p>Proteins containing this domain include D-threonate kinase from Salmonella typhimurium (DtnK), 3-oxo-tetronate kinase from Methylobacterium radiotolerans, 3-oxo-isoapionate kinase from Paraburkholderia graminis and D-erythronate kinase from Heliobacterium modesticaldum. DtnK catalyzes the ATP-dependent phosphorylation of D-threonate to D-threonate 4-phosphate and is also able to phosphorylate 4-hydroxy-L-threonine, which may serve to deal with the toxicity of this compound [[cite:PUB00085179], [cite:PUB00083215]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00085179": {
"PMID": 27402745,
"ISBN": null,
"volume": "113",
"issue": "29",
"year": 2016,
"title": "Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars.",
"URL": null,
"raw_pages": "E4161-9",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Zhang X",
"Carter MS",
"Vetting MW",
"San Francisco B",
"Zhao S",
"Al-Obaidi NF",
"Solbiati JO",
"Thiaville JJ",
"de Crecy-Lagard V",
"Jacobson MP",
"Almo SC",
"Gerlt JA."
],
"DOI_URL": "https://doi.org/10.1073/pnas.1605546113"
},
"PUB00083215": {
"PMID": 27294475,
"ISBN": null,
"volume": "11",
"issue": "8",
"year": 2016,
"title": "Members of a Novel Kinase Family (DUF1537) Can Recycle Toxic Intermediates into an Essential Metabolite.",
"URL": null,
"raw_pages": "2304-11",
"medline_journal": "ACS Chem Biol",
"ISO_journal": "ACS Chem. Biol.",
"authors": [
"Thiaville JJ",
"Flood J",
"Yurgel S",
"Prunetti L",
"Elbadawi-Sidhu M",
"Hutinet G",
"Forouhar F",
"Zhang X",
"Ganesan V",
"Reddy P",
"Fiehn O",
"Gerlt JA",
"Hunt JF",
"Copley SD",
"de Crecy-Lagard V."
],
"DOI_URL": "http://dx.doi.org/10.1021/acschembio.6b00279"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR037051",
"name": "Four-carbon acid sugar kinase, N-terminal domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 104,
"interactions": 0,
"matches": 14036,
"pathways": 2,
"proteins": 13982,
"proteomes": 5812,
"sets": 0,
"structural_models": {
"alphafold": 10431,
"bfvd": 0
},
"structures": 7,
"taxa": 11023
},
"entry_annotations": {
"alignment:seed": 165,
"alignment:full": 4846
},
"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": "2.7.1.217",
"url": "https://enzyme.expasy.org/EC/2.7.1.217"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "4xg0",
"name": "Crystal structure of a domain of unknown function (DUF1537) from Bordetella bronchiseptica (BB3215), Target EFI-511620, with bound citrate, domain swapped dimer, space group C2221"
}
}
}
