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{
"metadata": {
"accession": "IPR044138",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd03695": "Domain II of the large subunit of ATP sulfurylase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR044138",
"name": "Sulfate adenylyltransferase subunit CysN, Domain II",
"type": "Domain",
"children": []
},
"name": {
"name": "Sulfate adenylyltransferase subunit CysN, Domain II",
"short": "CysN_II"
},
"description": [
{
"text": "<p>CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN [[cite:PUB00034488]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>This entryvrepresents the central domain (domain II) of CysN.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00034488": {
"PMID": 16387658,
"ISBN": null,
"volume": "21",
"issue": "1",
"year": 2006,
"title": "Molecular basis for G protein control of the prokaryotic ATP sulfurylase.",
"URL": null,
"raw_pages": "109-22",
"medline_journal": "Mol Cell",
"ISO_journal": "Mol. Cell",
"authors": [
"Mougous JD",
"Lee DH",
"Hubbard SC",
"Schelle MW",
"Vocadlo DJ",
"Berger JM",
"Bertozzi CR."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.molcel.2005.10.034"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR009000",
"name": "Translation protein, beta-barrel domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 15148,
"pathways": 5,
"proteins": 15148,
"proteomes": 9484,
"sets": 0,
"structural_models": {
"alphafold": 11068,
"bfvd": 0
},
"structures": 1,
"taxa": 14289
},
"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": "2.7.7.4",
"url": "https://enzyme.expasy.org/EC/2.7.7.4"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
