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{
"metadata": {
"accession": "IPR042199",
"entry_id": null,
"type": "homologous_superfamily",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"cathgene3d": {
"G3DSA:1.20.120.1320": "Aspartokinase, catalytic domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR042199",
"name": "Aspartokinase/Bifunctional aspartokinase/homoserine dehydrogenase, catalytic domain",
"type": "Homologous_superfamily",
"children": []
},
"name": {
"name": "Aspartokinase/Bifunctional aspartokinase/homoserine dehydrogenase, catalytic domain",
"short": "AsparK_Bifunc_asparK/hSer_DH"
},
"description": [
{
"text": "<p>Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In Bacillus subtilis, YclM is reported to be a single polypeptide of 50 kD. The B. subtilis 168 AKIII is induced by lysine and repressed by threonine, and it is synergistically inhibited by lysine and threonine [[cite:PUB00086232], [cite:PUB00086233]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>The bifunctional enzyme aspartokinase/homoserine dehydrogenase (AK-HSDH), found in bacteria and plant chloroplasts, catalyses the first and third steps of the aspartate pathway. Homoserine dehydrogenase ([ec:1.1.1.3]) catalyses the conversion of L-homoserine to L-aspartate-4-semialdehyde using NAD(P), while aspartate kinase ([ec:2.7.2.4]) catalyses the phosphorylation of L-aspartate to 4-phospho-L-aspartate. There are two genes encoding different isoforms of this bifunctional enzymes; one isoform is threonine-sensitive, while the other is methionine-sensitive [[cite:PUB00014809]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>This superfamily represents the N-terminal catalytic domain found in aspartokinase and in the bifunctional enzyme aspartokinase/homoserine dehydrogenase. It has a key role in amino acid binding.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00086233": {
"PMID": 2152900,
"ISBN": null,
"volume": "172",
"issue": "1",
"year": 1990,
"title": "Aspartokinase III, a new isozyme in Bacillus subtilis 168.",
"URL": null,
"raw_pages": "218-23",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Graves LM",
"Switzer RL."
],
"DOI_URL": "https://doi.org/10.1128/jb.172.1.218-223.1990"
},
"PUB00086232": {
"PMID": 11471740,
"ISBN": null,
"volume": "65",
"issue": "6",
"year": 2001,
"title": "Characterization of aspartate kinase III of Bacillus subtilis.",
"URL": null,
"raw_pages": "1391-4",
"medline_journal": "Biosci Biotechnol Biochem",
"ISO_journal": "Biosci. Biotechnol. Biochem.",
"authors": [
"Kobashi N",
"Nishiyama M",
"Yamane H."
],
"DOI_URL": "https://doi.org/10.1271/bbb.65.1391"
},
"PUB00014809": {
"PMID": 12435751,
"ISBN": null,
"volume": "278",
"issue": "7",
"year": 2003,
"title": "Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine.",
"URL": null,
"raw_pages": "5361-6",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Paris S",
"Viemon C",
"Curien G",
"Dumas R."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M207379200"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036393",
"name": "Acetylglutamate kinase-like superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR001048",
"name": "Aspartate/glutamate/uridylate kinase",
"type": "domain"
},
{
"accession": "IPR001341",
"name": "Aspartate kinase",
"type": "family"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 16244,
"pathways": 11,
"proteins": 16241,
"proteomes": 5422,
"sets": 0,
"structural_models": {
"alphafold": 12826,
"bfvd": 0
},
"structures": 3,
"taxa": 9975
},
"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": "2.7.2.4",
"url": "https://enzyme.expasy.org/EC/2.7.2.4"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
