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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR043702",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004359",
"name": "glutaminase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0071555",
"name": "cell wall organization",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"hamap": {
"MF_02213": "Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD [gatD]"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR043702",
"name": "Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD",
"type": "Family",
"children": []
},
"name": {
"name": "Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD",
"short": "Lipid_II_synth_GatD"
},
"description": [
{
"text": "<p>Amidated peptidoglycan of Gram-positive bacteria is essential for peptidoglycan (PG) cross-linking, playing an important role in homeostasis, antibiotic resistance and cell survival. The bi-enzymatic complex MurT-GatD catalyses the amidation process in PG stem peptides, in which GatD is the glutamine amidotransferase member. GatD metabolises glutamine and provides ammonia to MurT, the ligase that catalises the convertion of D-glutamate residue in Lipid II to D-isoglutamine. Sequence analysis of this subunit from S. aureus is similar to the catalytic domain in CobB/CobQ-like glutamine amidotransferases (GatD) (enzymes involved in cobalamin biosynthesis), being grouped in a new sub-family of glutamine amidotransferases [[cite:PUB00094477], [cite:PUB00094478]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00094478": {
"PMID": 22303291,
"ISBN": null,
"volume": "8",
"issue": "1",
"year": 2012,
"title": "Identification of genetic determinants and enzymes involved with the amidation of glutamic acid residues in the peptidoglycan of Staphylococcus aureus.",
"URL": null,
"raw_pages": "e1002508",
"medline_journal": "PLoS Pathog",
"ISO_journal": "PLoS Pathog.",
"authors": [
"Figueiredo TA",
"Sobral RG",
"Ludovice AM",
"Almeida JM",
"Bui NK",
"Vollmer W",
"de Lencastre H",
"Tomasz A."
],
"DOI_URL": null
},
"PUB00094477": {
"PMID": 29593310,
"ISBN": null,
"volume": "8",
"issue": "1",
"year": 2018,
"title": "First insights of peptidoglycan amidation in Gram-positive bacteria - the high-resolution crystal structure of Staphylococcus aureus glutamine amidotransferase GatD.",
"URL": null,
"raw_pages": "5313",
"medline_journal": "Sci Rep",
"ISO_journal": "Sci Rep",
"authors": [
"Leisico F",
"V Vieira D",
"Figueiredo TA",
"Silva M",
"Cabrita EJ",
"Sobral RG",
"Ludovice AM",
"Trincao J",
"Romao MJ",
"de Lencastre H",
"Santos-Silva T."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR029062",
"name": "Class I glutamine amidotransferase-like",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 6375,
"pathways": 3,
"proteins": 6375,
"proteomes": 4250,
"sets": 0,
"structural_models": {
"alphafold": 4791,
"bfvd": 0
},
"structures": 7,
"taxa": 6863
},
"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": "3.5.1.2",
"url": "https://enzyme.expasy.org/EC/3.5.1.2"
},
{
"accession": "6.3.5.13",
"url": "https://enzyme.expasy.org/EC/6.3.5.13"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "5n9m",
"name": "Crystal structure of GatD - a glutamine amidotransferase from Staphylococcus aureus involved in peptidoglycan amidation"
}
}
}
