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{
"metadata": {
"accession": "IPR036100",
"entry_id": null,
"type": "homologous_superfamily",
"go_terms": [
{
"identifier": "GO:0016740",
"name": "transferase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0016853",
"name": "isomerase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"ssf": {
"SSF111337": "QueA-like"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR036100",
"name": "S-adenosylmethionine:tRNA ribosyltransferase-isomerase, QueA superfamily",
"type": "Homologous_superfamily",
"children": []
},
"name": {
"name": "S-adenosylmethionine:tRNA ribosyltransferase-isomerase, QueA superfamily",
"short": "QueA_sf"
},
"description": [
{
"text": "<p>This entry represents the S-adenosylmethionine:tRNA ribosyltransferase-isomerase, QueA. Queuosine is a hypermodified nucleoside that usually occurs in the first position of the anticodon of tRNAs specifying the amino acids asparagine, aspartate, histidine, and tyrosine. The hypermodified nucleoside is found in bacteria and eukaryotes [[cite:PUB00008181]]. Queuosine is synthesized<i>de novo</i>exclusively in bacteria; for eukaryotes the compound is a nutrient factor. Queuosine biosynthesis protein, or S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (QueA) catalyses the formation of the 2,3-epoxy-4,5-dihydroxycyclopentane ring of the Q precursor epoxyqueuosine (oQ). S-adenosyl-L-methionine (AdoMet) reacts with 7-aminomethyl-7-deazaguanine of tRNA at position 34 to yield adenine, methionine, and a modified tRNA with oQ at position 34.</p>\n\n<p>QueA consists of two domains: domain 1 has three layers (α/β/α)), while domain 2 is a closed β-barrel with Greek-key topology [[cite:PUB00032106]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00008181": {
"PMID": 8347586,
"ISBN": null,
"volume": "32",
"issue": "30",
"year": 1993,
"title": "A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine.",
"URL": null,
"raw_pages": "7811-7",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Slany RK",
"Bosl M",
"Crain PF",
"Kersten H."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi00081a028"
},
"PUB00032106": {
"PMID": 15822125,
"ISBN": null,
"volume": "59",
"issue": "4",
"year": 2005,
"title": "Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new fold.",
"URL": null,
"raw_pages": "869-74",
"medline_journal": "Proteins",
"ISO_journal": "Proteins",
"authors": [
"Mathews I",
"Schwarzenbacher R",
"McMullan D",
"Abdubek P",
"Ambing E",
"Axelrod H",
"Biorac T",
"Canaves JM",
"Chiu HJ",
"Deacon AM",
"DiDonato M",
"Elsliger MA",
"Godzik A",
"Grittini C",
"Grzechnik SK",
"Hale J",
"Hampton E",
"Han GW",
"Haugen J",
"Hornsby M",
"Jaroszewski L",
"Klock HE",
"Koesema E",
"Kreusch A",
"Kuhn P",
"Lesley SA",
"Levin I",
"Miller MD",
"Moy K",
"Nigoghossian E",
"Ouyang J",
"Paulsen J",
"Quijano K",
"Reyes R",
"Spraggon G",
"Stevens RC",
"van den Bedem H",
"Velasquez J",
"Vincent J",
"White A",
"Wolf G",
"Xu Q",
"Hodgson KO",
"Wooley J",
"Wilson IA."
],
"DOI_URL": "http://dx.doi.org/10.1002/prot.20419"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR003699",
"name": "S-adenosylmethionine:tRNA ribosyltransferase-isomerase, QueA",
"type": "family"
},
{
"accession": "IPR042118",
"name": "QueA, domain 1",
"type": "homologous_superfamily"
},
{
"accession": "IPR042119",
"name": "QueA, domain 2",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 24721,
"pathways": 2,
"proteins": 24590,
"proteomes": 14035,
"sets": 0,
"structural_models": {
"alphafold": 19463,
"bfvd": 0
},
"structures": 3,
"taxa": 24391
},
"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": "2.4.99.17",
"url": "https://enzyme.expasy.org/EC/2.4.99.17"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1vky",
"name": "Crystal structure of S-adenosylmethionine tRNA ribosyltransferase (TM0574) from Thermotoga maritima at 2.00 A resolution"
}
}
}
