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{
"metadata": {
"accession": "IPR020888",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0000287",
"name": "magnesium ion binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0016984",
"name": "ribulose-bisphosphate carboxylase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0015977",
"name": "carbon fixation",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd08212": "Ribulose bisphosphate carboxylase large chain, Form I"
},
"hamap": {
"MF_01338": "Ribulose bisphosphate carboxylase large chain [rbcL]"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR033966",
"name": "RuBisCO",
"type": "Family",
"children": [
{
"accession": "IPR017712",
"name": "Ribulose bisphosphate carboxylase, type III",
"type": "Family",
"children": []
},
{
"accession": "IPR017717",
"name": "2,3-diketo-5-methylthiopentyl-1-phosphate enolase",
"type": "Family",
"children": []
},
{
"accession": "IPR020871",
"name": "Ribulose bisphosphate carboxylase large subunit, type II",
"type": "Family",
"children": []
},
{
"accession": "IPR020888",
"name": "Ribulose bisphosphate carboxylase large subunit, type I",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Ribulose bisphosphate carboxylase large subunit, type I",
"short": "RuBisCO_lsuI"
},
"description": [
{
"text": "<p>Ribulose bisphosphate carboxylase (RuBisCO) [[cite:PUB00000034], [cite:PUB00004038]] catalyses the initial step in Calvin's reductive pentose phosphate cycle in plants as well as purple and green bacteria. It catalyzes the primary CO2 fixation step. RuBisCO consists of a large catalytic unit and a small subunit of undetermined function. In plants, the large subunit is coded by the chloroplastic genome while the small subunit is encoded in the nuclear genome. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate [[cite:PUB00015291], [cite:PUB00020282]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Members of the Rubisco family can be divided into 4 subgroups, form I-IV , which differ in their taxonomic distribution and subunit composition [[cite:PUB00080670], [cite:PUB00049187]]. Form I is the most abundant class, present in plants, algae, and bacteria, and forms large complexes composed of 8 large and 8 small subunits.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00015291": {
"PMID": 1969412,
"ISBN": null,
"volume": "265",
"issue": "11",
"year": 1990,
"title": "Examination of the intersubunit interaction between glutamate-48 and lysine-168 of ribulose-bisphosphate carboxylase/oxygenase by site-directed mutagenesis.",
"URL": null,
"raw_pages": "6501-5",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Mural RJ",
"Soper TS",
"Larimer FW",
"Hartman FC."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/265/11/6501"
},
"PUB00004038": {
"PMID": 12221984,
"ISBN": null,
"volume": "53",
"issue": null,
"year": 2002,
"title": "Rubisco: structure, regulatory interactions, and possibilities for a better enzyme.",
"URL": null,
"raw_pages": "449-75",
"medline_journal": "Annu Rev Plant Biol",
"ISO_journal": null,
"authors": [
"Spreitzer RJ",
"Salvucci ME."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.arplant.53.100301.135233"
},
"PUB00049187": {
"PMID": 18063718,
"ISBN": null,
"volume": "71",
"issue": "4",
"year": 2007,
"title": "Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.",
"URL": null,
"raw_pages": "576-99",
"medline_journal": "Microbiol Mol Biol Rev",
"ISO_journal": "Microbiol. Mol. Biol. Rev.",
"authors": [
"Tabita FR",
"Hanson TE",
"Li H",
"Satagopan S",
"Singh J",
"Chan S."
],
"DOI_URL": "http://dx.doi.org/10.1128/MMBR.00015-07"
},
"PUB00080670": {
"PMID": 18281717,
"ISBN": null,
"volume": "59",
"issue": "7",
"year": 2008,
"title": "Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships.",
"URL": null,
"raw_pages": "1515-24",
"medline_journal": "J Exp Bot",
"ISO_journal": "J. Exp. Bot.",
"authors": [
"Tabita FR",
"Satagopan S",
"Hanson TE",
"Kreel NE",
"Scott SS."
],
"DOI_URL": "http://dx.doi.org/10.1093/jxb/erm361"
},
"PUB00020282": {
"PMID": 9034362,
"ISBN": null,
"volume": "265",
"issue": "4",
"year": 1997,
"title": "The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate.",
"URL": null,
"raw_pages": "432-44",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Taylor TC",
"Andersson I."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.1996.0738"
},
"PUB00000034": {
"PMID": 6351728,
"ISBN": null,
"volume": "52",
"issue": null,
"year": 1983,
"title": "Ribulose-1,5-bisphosphate carboxylase-oxygenase.",
"URL": null,
"raw_pages": "507-35",
"medline_journal": "Annu Rev Biochem",
"ISO_journal": "Annu. Rev. Biochem.",
"authors": [
"Miziorko HM",
"Lorimer GH."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.bi.52.070183.002451"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036376",
"name": "Ribulose bisphosphate carboxylase, large subunit, C-terminal domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 66548,
"pathways": 2,
"proteins": 66548,
"proteomes": 1502,
"sets": 0,
"structural_models": {
"alphafold": 59488,
"bfvd": 0
},
"structures": 103,
"taxa": 63636
},
"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": "4.1.1.39",
"url": "https://enzyme.expasy.org/EC/4.1.1.39"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "9iqo",
"name": "Cryo-EM structure of the Rubisco from thermophilic purple bacterial Rubisco"
}
}
}
