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{
"metadata": {
"accession": "PF00696",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "pfam",
"member_databases": null,
"integrated": "IPR001048",
"hierarchy": null,
"name": {
"name": "Amino acid kinase family",
"short": "AA_kinase"
},
"description": [
{
"text": "<p>This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase [ec:2.7.2.4], [swissprot:P00561]. Acetylglutamate kinase [ec:2.7.2.8], [swissprot:Q07905]. Glutamate 5-kinase [ec:2.7.2.11], [swissprot:P07005]. Uridylate kinase [ec:2.7.4.-], [swissprot:P29464]. Carbamate kinase [ec:2.7.2.2], [swissprot:O96432].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": [
{
"title": "Amino_acid_kinase",
"extract": "<p>In molecular biology, the <b>amino acid kinase</b> domain is a protein domain. It is found in protein kinases with various specificities, including the aspartate, glutamate and uridylate kinase families. In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed-back inhibition of aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS). In <i>Escherichia coli</i>, thrA, metLM, and lysC encode aspartokinase isozymes that show feedback inhibition by threonine, methionine, and lysine, respectively. The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a subunit composition of 4 large and 4 small subunits.</p>",
"thumbnail": null
}
],
"literature": {
"PUB00019080": {
"PMID": 10860751,
"ISBN": null,
"volume": "299",
"issue": "2",
"year": 2000,
"title": "The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases.",
"URL": null,
"raw_pages": "463-76",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Ramon-Maiques S",
"Marina A",
"Uriarte M",
"Fita I",
"Rubio V."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.2000.3779"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 417,
"interactions": 0,
"matches": 152621,
"pathways": 0,
"proteins": 152384,
"proteomes": 21170,
"sets": 0,
"structural_models": {
"alphafold": 120385,
"bfvd": 1
},
"structures": 178,
"taxa": 42167
},
"entry_annotations": {
"hmm": 0,
"logo": 0,
"alignment:seed": 126,
"alignment:full": 57577
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1e19",
"name": "Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP"
}
}
}
