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InterPro-Version: 108.0
InterPro-Version-Minor: 0
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{
"metadata": {
"accession": "IPR005921",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004397",
"name": "histidine ammonia-lyase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006548",
"name": "L-histidine catabolic process",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0005737",
"name": "cytoplasm",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"source_database": "interpro",
"member_databases": {
"hamap": {
"MF_00229": "Histidine ammonia-lyase [hutH]"
},
"ncbifam": {
"TIGR01225": "histidine ammonia-lyase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR001106",
"name": "Aromatic amino acid lyase",
"type": "Family",
"children": [
{
"accession": "IPR005921",
"name": "Histidine ammonia-lyase",
"type": "Family",
"children": []
},
{
"accession": "IPR005922",
"name": "Phenylalanine ammonia-lyase",
"type": "Family",
"children": [
{
"accession": "IPR031008",
"name": "Phenylalanine aminomutase (L-beta-phenylalanine forming)",
"type": "Family",
"children": []
}
]
},
{
"accession": "IPR022314",
"name": "Tyrosine 2,3-aminomutase, putative",
"type": "Family",
"children": []
},
{
"accession": "IPR031007",
"name": "Phenylalanine aminomutase (D-beta-phenylalanine forming)",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Histidine ammonia-lyase",
"short": "HutH"
},
"description": [
{
"text": "<p>Histidine ammonia-lyase deaminates histidine to urocanic acid, the first step in histidine degradation. It is closely related to the plant enzyme phenylalanine ammonia-lyase [[cite:PUB00023551]] but is absent in plants and viruses. This enzyme contains a unique cofactor called 4-methylidene-imidazole-5-one group (MIO), which is produced autocatalytically by a cyclisation and dehydration of the three amino-acid residues alanine, serine and glycine, for its chain folding [[cite:PUB00021475]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00023551": {
"PMID": 10220322,
"ISBN": null,
"volume": "38",
"issue": "17",
"year": 1999,
"title": "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.",
"URL": null,
"raw_pages": "5355-61",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Schwede TF",
"Retey J",
"Schulz GE."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi982929q"
},
"PUB00021475": {
"PMID": 11796111,
"ISBN": null,
"volume": "10",
"issue": "1",
"year": 2002,
"title": "Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase.",
"URL": null,
"raw_pages": "61-7",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Baedeker M",
"Schulz GE."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(01)00692-X"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR008948",
"name": "L-Aspartase-like",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 15713,
"pathways": 8,
"proteins": 15713,
"proteomes": 10214,
"sets": 0,
"structural_models": {
"alphafold": 11749,
"bfvd": 0
},
"structures": 8,
"taxa": 17252
},
"entry_annotations": {},
"cross_references": {
"gp": {
"displayName": "Genome Properties",
"description": "Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.",
"rank": 45,
"accessions": [
{
"accession": "GenProp1619",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1619"
}
]
},
"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": "4.3.1.3",
"url": "https://enzyme.expasy.org/EC/4.3.1.3"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1gkm",
"name": "HISTIDINE AMMONIA-LYASE (HAL) FROM PSEUDOMONAS PUTIDA INHIBITED WITH L-CYSTEINE"
}
}
}
