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{
"metadata": {
"accession": "IPR022653",
"entry_id": null,
"type": "binding_site",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"prosite": {
"PS00878": "Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR022653",
"name": "Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding site",
"type": "Binding_site",
"children": []
},
"name": {
"name": "Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding site",
"short": "De-COase2_pyr-phos_BS"
},
"description": [
{
"text": "<p>These enzymes are collectively known as group IV decarboxylases [[cite:PUB00001452]]. Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates can be classified into two different families on the basis of sequence similarities [[cite:PUB00003632], [cite:PUB00001452]]. Members of this family while most probably evolutionary related, do not share extensive regions of sequence similarities. This site contains a conserved lysine residue which is known, in mouse ODC [[cite:PUB00002726]], to be the site of attachment of the pyridoxal-phosphate group.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00002726": {
"PMID": 1730582,
"ISBN": null,
"volume": "267",
"issue": "1",
"year": 1992,
"title": "Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites.",
"URL": null,
"raw_pages": "150-8",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Poulin R",
"Lu L",
"Ackermann B",
"Bey P",
"Pegg AE."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/267/1/150.pdf"
},
"PUB00003632": {
"PMID": 3143046,
"ISBN": null,
"volume": "5",
"issue": "5",
"year": 1988,
"title": "Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary relationship with other amino acid decarboxylases.",
"URL": null,
"raw_pages": "549-59",
"medline_journal": "Mol Biol Evol",
"ISO_journal": "Mol. Biol. Evol.",
"authors": [
"Martin C",
"Cami B",
"Yeh P",
"Stragier P",
"Parsot C",
"Patte JC."
],
"DOI_URL": "http://mbe.oxfordjournals.org/cgi/content/abstract/5/5/549.pdf"
},
"PUB00001452": {
"PMID": 8181483,
"ISBN": null,
"volume": "221",
"issue": "3",
"year": 1994,
"title": "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.",
"URL": null,
"raw_pages": "997-1002",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Sandmeier E",
"Hale TI",
"Christen P."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1994.tb18816.x"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 36534,
"pathways": 22,
"proteins": 36501,
"proteomes": 16048,
"sets": 0,
"structural_models": {
"alphafold": 28977,
"bfvd": 1
},
"structures": 40,
"taxa": 29742
},
"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": "4.1.1",
"url": "https://enzyme.expasy.org/EC/4.1.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
