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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR005299",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0008168",
"name": "methyltransferase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"panther": {
"PTHR31009": "S-ADENOSYL-L-METHIONINE:CARBOXYL METHYLTRANSFERASE FAMILY PROTEIN"
},
"pfam": {
"PF03492": "SAM dependent carboxyl methyltransferase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR005299",
"name": "SAM dependent carboxyl methyltransferase",
"type": "Family",
"children": []
},
"name": {
"name": "SAM dependent carboxyl methyltransferase",
"short": "MeTrfase_7"
},
"description": [
{
"text": "<p>This family of plant methyltransferases contains enzymes that act on a variety of substrates including salicylic acid, jasmonic acid and 7-methylxanthine. Caffeine is synthesised through sequential three-step methylation of xanthine derivatives at positions 7-N, 3-N, and 1-N [[cite:PUB00040394], [cite:PUB00096633]]. The protein 7-methylxanthine methyltransferase (designated as CaMXMT) catalyses the second step to produce theobromine [[cite:PUB00008390]]. The protein Carlactonoate CLA methyltransferase (CLAMT) catalyses the biosynthesis of (11R)-methyl carlactonoate from (11R)-carlactonoate [[cite:PUB00153148]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00008390": {
"PMID": 11108716,
"ISBN": null,
"volume": "276",
"issue": "11",
"year": 2001,
"title": "7-Methylxanthine methyltransferase of coffee plants. Gene isolation and enzymatic properties.",
"URL": null,
"raw_pages": "8213-8",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Ogawa M",
"Herai Y",
"Koizumi N",
"Kusano T",
"Sano H."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M009480200"
},
"PUB00040394": {
"PMID": 17434991,
"ISBN": null,
"volume": "144",
"issue": "2",
"year": 2007,
"title": "The structure of two N-methyltransferases from the caffeine biosynthetic pathway.",
"URL": null,
"raw_pages": "879-89",
"medline_journal": "Plant Physiol",
"ISO_journal": "Plant Physiol.",
"authors": [
"McCarthy AA",
"McCarthy JG."
],
"DOI_URL": "http://dx.doi.org/10.1104/pp.106.094854"
},
"PUB00096633": {
"PMID": 18068204,
"ISBN": null,
"volume": "69",
"issue": "4",
"year": 2008,
"title": "Caffeine and related purine alkaloids: biosynthesis, catabolism, function and genetic engineering.",
"URL": null,
"raw_pages": "841-56",
"medline_journal": "Phytochemistry",
"ISO_journal": "Phytochemistry",
"authors": [
"Ashihara H",
"Sano H",
"Crozier A."
],
"DOI_URL": null
},
"PUB00153148": {
"PMID": 34586497,
"ISBN": null,
"volume": "254",
"issue": "5",
"year": 2021,
"title": "Specific methylation of (11R)-carlactonoic acid by an Arabidopsis SABATH methyltransferase.",
"URL": null,
"raw_pages": "88",
"medline_journal": "Planta",
"ISO_journal": "Planta",
"authors": [
"Wakabayashi T",
"Yasuhara R",
"Miura K",
"Takikawa H",
"Mizutani M",
"Sugimoto Y."
],
"DOI_URL": "https://doi.org/10.1007/s00425-021-03738-6"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR029063",
"name": "S-adenosyl-L-methionine-dependent methyltransferase superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR042086",
"name": "Methyltransferase, alpha-helical capping domain",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 159,
"interactions": 0,
"matches": 14259,
"pathways": 0,
"proteins": 13427,
"proteomes": 968,
"sets": 0,
"structural_models": {
"alphafold": 11492,
"bfvd": 0
},
"structures": 13,
"taxa": 2863
},
"entry_annotations": {
"alignment:seed": 101,
"alignment:full": 7786
},
"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": "GenProp1420",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1420"
}
]
},
"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": "2.1.1",
"url": "https://enzyme.expasy.org/EC/2.1.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2efj",
"name": "The structure of 1,7 dimethylxanthine methyltransferase"
}
}
}
