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InterPro-Version: 107.0
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{
"metadata": {
"accession": "IPR030668",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0006595",
"name": "polyamine metabolic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"pirsf": {
"PIRSF000502": "Spermidine synthase/putrescine N-methyltransferase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR001045",
"name": "Spermidine/spermine synthases",
"type": "Family",
"children": [
{
"accession": "IPR015576",
"name": "Spermine synthase, animal",
"type": "Family",
"children": []
},
{
"accession": "IPR025803",
"name": "Putrescine N-methyltransferase",
"type": "Family",
"children": []
},
{
"accession": "IPR030668",
"name": "Spermidine/spermine synthase, eukaryotes",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Spermidine/spermine synthase, eukaryotes",
"short": "Spermi_synthase_euk"
},
"description": [
{
"text": "<p>The ubiquitous polyamines spermidine and spermine are involved in numerous cellular functions and they are essential for cell growth and proliferation. Spermidine synthase ([ec:2.5.1.16]) (putrescine aminopropyltransferase) catalyses the last step in the biosynthesis of spermidine from arginine and methionine; the conversion of putrescine to spermidine using decarboxylated S-adenosylmethionine as the cofactor [[cite:PUB00048416]]. Spermine synthase ([ec:2.5.1.22]) (spermidine aminopropyltransferase) converts spermidine into spermine using decarboxylated S-adenosylmethionine as the cofactor [[cite:PUB00073569]].</p>\n\n<p>This entry consists of spermidine and spermine synthases from eukaryotes.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00073569": {
"PMID": 19859664,
"ISBN": null,
"volume": "67",
"issue": "1",
"year": 2010,
"title": "Spermine synthase.",
"URL": null,
"raw_pages": "113-21",
"medline_journal": "Cell Mol Life Sci",
"ISO_journal": "Cell. Mol. Life Sci.",
"authors": [
"Pegg AE",
"Michael AJ."
],
"DOI_URL": "http://dx.doi.org/10.1007/s00018-009-0165-5"
},
"PUB00048416": {
"PMID": 17585781,
"ISBN": null,
"volume": "46",
"issue": "28",
"year": 2007,
"title": "Structure and mechanism of spermidine synthases.",
"URL": null,
"raw_pages": "8331-9",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Wu H",
"Min J",
"Ikeguchi Y",
"Zeng H",
"Dong A",
"Loppnau P",
"Pegg AE",
"Plotnikov AN."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi602498k"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR029063",
"name": "S-adenosyl-L-methionine-dependent methyltransferase superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 2958,
"pathways": 5,
"proteins": 2958,
"proteomes": 1786,
"sets": 0,
"structural_models": {
"alphafold": 2764,
"bfvd": 0
},
"structures": 12,
"taxa": 5033
},
"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": "2.5.1.16",
"url": "https://enzyme.expasy.org/EC/2.5.1.16"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "8iyi",
"name": "Spermidine synthase from Kluyveromyces lactis"
}
}
}
