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{
"metadata": {
"accession": "IPR001451",
"entry_id": null,
"type": "repeat",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF14602": "Hexapeptide repeat of succinyl-transferase",
"PF00132": "Bacterial transferase hexapeptide (six repeats)"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR001451",
"name": "Hexapeptide repeat",
"type": "Repeat",
"children": []
},
"name": {
"name": "Hexapeptide repeat",
"short": "Hexapep"
},
"description": [
{
"text": "<p>A variety of bacterial transferases contain a repeat structure composed of tandem repeats of a [LIV]-G-X(4) hexapeptide, which, in the tertiary structure of LpxA (Acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase) [[cite:PUB00005215]], has been shown to form a left-handed parallel β-helix. A number of different transferase protein families contain this repeat, such as the bifunctional protein GlmU, galactoside acetyltransferase-like proteins [[cite:PUB00013969]], the gamma-class of carbonic anhydrases [[cite:PUB00013970]], and tetrahydrodipicolinate-N-succinlytransferases (DapD), the latter containing an extra N-terminal 3-helical domain [[cite:PUB00013971]]. It has been shown that most hexapeptide acyltransferases form catalytic trimers with three symmetrical active sites [[cite:PUB00094377]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00005215": {
"PMID": 7481807,
"ISBN": null,
"volume": "270",
"issue": "5238",
"year": 1995,
"title": "A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase.",
"URL": null,
"raw_pages": "997-1000",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Raetz CR",
"Roderick SL."
],
"DOI_URL": "http://www.sciencemag.org/cgi/content/abstract/270/5238/997"
},
"PUB00013970": {
"PMID": 10924115,
"ISBN": null,
"volume": "39",
"issue": "31",
"year": 2000,
"title": "A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila.",
"URL": null,
"raw_pages": "9222-31",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Iverson TM",
"Alber BE",
"Kisker C",
"Ferry JG",
"Rees DC."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi000204s"
},
"PUB00013971": {
"PMID": 11910040,
"ISBN": null,
"volume": "11",
"issue": "4",
"year": 2002,
"title": "Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase.",
"URL": null,
"raw_pages": "974-9",
"medline_journal": "Protein Sci",
"ISO_journal": "Protein Sci.",
"authors": [
"Beaman TW",
"Vogel KW",
"Drueckhammer DG",
"Blanchard JS",
"Roderick SL."
],
"DOI_URL": "http://dx.doi.org/10.1110/ps.4310102"
},
"PUB00013969": {
"PMID": 11937062,
"ISBN": null,
"volume": "10",
"issue": "4",
"year": 2002,
"title": "Structure of the lac operon galactoside acetyltransferase.",
"URL": null,
"raw_pages": "581-8",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Wang XG",
"Olsen LR",
"Roderick SL."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(02)00741-4"
},
"PUB00094377": {
"PMID": 17519228,
"ISBN": null,
"volume": "282",
"issue": "30",
"year": 2007,
"title": "Biochemical characterization of the polysialic acid-specific O-acetyltransferase NeuO of Escherichia coli K1.",
"URL": null,
"raw_pages": "22217-27",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Bergfeld AK",
"Claus H",
"Vogel U",
"Muhlenhoff M."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR011004",
"name": "Trimeric LpxA-like superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 815,
"interactions": 0,
"matches": 250724,
"pathways": 5,
"proteins": 189664,
"proteomes": 19579,
"sets": 0,
"structural_models": {
"alphafold": 146134,
"bfvd": 6
},
"structures": 291,
"taxa": 35295
},
"entry_annotations": {
"alignment:seed": 41,
"alignment:full": 18777
},
"cross_references": {
"prositedoc": {
"displayName": "PROSITE Doc",
"description": "PROSITE is a database of protein families and domains.",
"rank": 18,
"accessions": [
{
"accession": "PDOC00094",
"url": "http://prosite.expasy.org/PDOC00094"
}
]
},
"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": "GenProp1468",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1468"
}
]
},
"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": "2.3.1",
"url": "https://enzyme.expasy.org/EC/2.3.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "7s45",
"name": "Crystal structure of an N-acetyltransferase, C80T mutant, from Helicobacter pullorum in the presence of Acetyl Coenzyme A and dTDP"
}
}
}
