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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR006318",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0016772",
"name": "transferase activity, transferring phosphorus-containing groups",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"ncbifam": {
"TIGR01417": "phosphoenolpyruvate--protein phosphotransferase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR006318",
"name": "Phosphotransferase system, enzyme I-like",
"type": "Domain",
"children": []
},
"name": {
"name": "Phosphotransferase system, enzyme I-like",
"short": "PTS_EI-like"
},
"description": [
{
"text": "<p>Most proteins with this domain are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferases (or enzyme I) of PTS sugar transport systems. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). This domain is also found in enzyme I-Ntr, which transfers the phosphoryl group from PEP to the phosphoryl carrier protein NPr, and is involved in regulating nitrogen metabolism [[cite:PUB00070136]], indicating that not all phosphotransferase system components are associated directly with sugar transport. In Xanthomonas campestris, FruB is a multiphosphoryl transfer protein involved in fructose transport that consists of three domains: a fructose-specific enzyme-IIA-like N-terminal domain, followed by an HPr-like domain and an enzyme-I-like C-terminal domain, represented by this entry [[cite:PUB00076910]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00076910": {
"PMID": 7496537,
"ISBN": null,
"volume": "141 ( Pt 9)",
"issue": null,
"year": 1995,
"title": "Fructose phosphotransferase system of Xanthomonas campestris pv. campestris: characterization of the fruB gene.",
"URL": null,
"raw_pages": "2253-60",
"medline_journal": "Microbiology",
"ISO_journal": "Microbiology (Reading, Engl.)",
"authors": [
"de Crecy-Lagard V",
"Binet M",
"Danchin A."
],
"DOI_URL": null
},
"PUB00070136": {
"PMID": 18421563,
"ISBN": null,
"volume": "35",
"issue": "3",
"year": 2008,
"title": "Solution structure of NPr, a bacterial signal-transducing protein that controls the phosphorylation state of the potassium transporter-regulating protein IIA Ntr.",
"URL": null,
"raw_pages": "531-9",
"medline_journal": "Amino Acids",
"ISO_journal": "Amino Acids",
"authors": [
"Li X",
"Peterkofsky A",
"Wang G."
],
"DOI_URL": "http://dx.doi.org/10.1007/s00726-008-0079-9"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR040442",
"name": "Pyruvate kinase-like domain superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR015813",
"name": "Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR036618",
"name": "PtsI, HPr-binding domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 27857,
"pathways": 0,
"proteins": 27857,
"proteomes": 13010,
"sets": 0,
"structural_models": {
"alphafold": 21464,
"bfvd": 0
},
"structures": 24,
"taxa": 21035
},
"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": "GenProp0119",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0119"
}
]
},
"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": "2.7.3.9",
"url": "https://enzyme.expasy.org/EC/2.7.3.9"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "6vbj",
"name": "CRYSTAL STRUCTURE OF THE HYBRID C-TERMINAL DOMAIN OF ENZYME I OF THE BACTERIAL PHOSPHOTRANSFERASE SYSTEM FORMED BY HYBRIDIZING THE SCAFFOLD OF THE THERMOANAEROBACTER TENGCONGENSIS ENZYME WITH THE ACTIVE SITE LOOPS FROM THE ESCHERICHIA COLI ENZYME"
}
}
}
