GET /api/entry/panther/PTHR21363/?format=api
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{
"metadata": {
"accession": "PTHR21363",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "panther",
"member_databases": null,
"integrated": "IPR050812",
"hierarchy": null,
"name": {
"name": "Prephenate/Arogenate Dehydrogenase",
"short": "Preph/Arog_dehydrog"
},
"description": [
{
"text": "The prephenate/arogenate dehydrogenase family consists of enzymes involved in the biosynthesis of aromatic amino acids, primarily tyrosine. Members of this family catalyze the NAD(+)-dependent oxidative decarboxylation of prephenate to form 4-hydroxyphenylpyruvate, a key step in the pathway. Some enzymes within this family can also catalyze the conversion of arogenate to tyrosine. These enzymes play a regulatory role in controlling the levels of tyrosine within the cell. Additionally, certain members are involved in the biosynthesis of secondary metabolites, such as antibiotics like novobiocin and chloramphenicol, by catalyzing the formation of specific intermediates. The family is characterized by a lack of chorismate mutase activity in some bacterial members, distinguishing them from bifunctional enzymes that possess both prephenate dehydrogenase and chorismate mutase activities.",
"llm": true,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": null,
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 1,
"domain_architectures": 0,
"interactions": 0,
"matches": 26088,
"pathways": 0,
"proteins": 26088,
"proteomes": 16622,
"sets": 0,
"structural_models": {
"alphafold": 20089,
"bfvd": 0
},
"structures": 15,
"taxa": 28043
},
"entry_annotations": {
"hmm": 0,
"logo": 0
},
"cross_references": {},
"is_llm": true,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2g5c",
"name": "Crystal Structure of Prephenate Dehydrogenase from Aquifex aeolicus"
}
}
}