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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR007431",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0008770",
"name": "[acyl-carrier-protein] phosphodiesterase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006633",
"name": "fatty acid biosynthetic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"panther": {
"PTHR38764": "ACYL CARRIER PROTEIN PHOSPHODIESTERASE"
},
"pirsf": {
"PIRSF011489": "Uncharacterised conserved protein, UCP011489 type"
},
"pfam": {
"PF04336": "Acyl carrier protein phosphodiesterase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR007431",
"name": "Acyl carrier protein phosphodiesterase",
"type": "Family",
"children": [
{
"accession": "IPR023491",
"name": "Acyl carrier protein phosphodiesterase, gammaproteobacteria",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Acyl carrier protein phosphodiesterase",
"short": "ACP_PD"
},
"description": [
{
"text": "<p>This entry contains the Escherichia coli gene yajB, now renamed acpH, which encodes an ACP hydrolase. AcpH converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP [[cite:PUB00044655]].</p>\r\n<p>A mutant E. coli strain having a total deletion of the acpH grows normally, showing that phosphodiesterase activity is not essential for growth, although it is required for turnover of the ACP prosthetic group in vivo. AcpH is found only in Gram-negative organisms suggesting that it plays a role in some aspect of lipid metabolism that is unique to these organisms. The most obvious of which is biosynthesis of lipid A. Because AcpH is a hydrolase, it could possibly be an editing enzyme that intercepts acyl-ACPs that would give an inappropriate lipid A structure if used as acyl donors [[cite:PUB00044655]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00044655": {
"PMID": 16107329,
"ISBN": null,
"volume": "280",
"issue": "41",
"year": 2005,
"title": "The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization.",
"URL": null,
"raw_pages": "34675-83",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Thomas J",
"Cronan JE."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M505736200"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 4,
"interactions": 0,
"matches": 5680,
"pathways": 1,
"proteins": 5678,
"proteomes": 3810,
"sets": 0,
"structural_models": {
"alphafold": 4231,
"bfvd": 0
},
"structures": 0,
"taxa": 6040
},
"entry_annotations": {
"alignment:seed": 946,
"alignment:full": 1520
},
"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": "3.1.4.14",
"url": "https://enzyme.expasy.org/EC/3.1.4.14"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
