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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR017145",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pirsf": {
"PIRSF037227": "Aminobenzoyl-glutamate utilization protein B"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR017145",
"name": "Aminobenzoyl-glutamate utilization protein B",
"type": "Family",
"children": []
},
"name": {
"name": "Aminobenzoyl-glutamate utilization protein B",
"short": "Aminobenzoyl-glu_utiliz_pB"
},
"description": [
{
"text": "<p>This entry contains proteins that are related to glutamate carboxypeptidase and classed as non-peptidase homologues belonging to MEROPS peptidase family M20 (glutamate carboxypeptidase, clan MH) [[cite:PUB00003579]].</p>\r\n\r\n<p>The bacterial amidohydrolase abgB catalyses the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate is a natural end product of folate catabolism, and its utilization is initiated by the abg region gene product, AbgT, by enabling uptake of its into the cell in a concentration-dependent, saturable manner. It is subsequently cleaved by AbgA and AbgB (sometimes referred to as AbgAB) [[cite:PUB00060288], [cite:PUB00033912]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00003579": {
"PMID": 7674922,
"ISBN": null,
"volume": "248",
"issue": null,
"year": 1995,
"title": "Evolutionary families of metallopeptidases.",
"URL": null,
"raw_pages": "183-228",
"medline_journal": "Methods Enzymol",
"ISO_journal": "Meth. Enzymol.",
"authors": [
"Rawlings ND",
"Barrett AJ."
],
"DOI_URL": "http://dx.doi.org/10.1016/0076-6879(95)48015-3"
},
"PUB00060288": {
"PMID": 17307853,
"ISBN": null,
"volume": "189",
"issue": "9",
"year": 2007,
"title": "Escherichia coli abg genes enable uptake and cleavage of the folate catabolite p-aminobenzoyl-glutamate.",
"URL": null,
"raw_pages": "3329-34",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Carter EL",
"Jager L",
"Gardner L",
"Hall CC",
"Willis S",
"Green JM."
],
"DOI_URL": "http://dx.doi.org/10.1128/JB.01940-06"
},
"PUB00033912": {
"PMID": 9829935,
"ISBN": null,
"volume": "180",
"issue": "23",
"year": 1998,
"title": "Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli.",
"URL": null,
"raw_pages": "6260-8",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Hussein MJ",
"Green JM",
"Nichols BP."
],
"DOI_URL": "http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=9829935&action=stream&blobtype=pdf"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 3771,
"pathways": 0,
"proteins": 3771,
"proteomes": 1994,
"sets": 0,
"structural_models": {
"alphafold": 2763,
"bfvd": 0
},
"structures": 0,
"taxa": 3559
},
"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": "GenProp1119",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1119"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
