HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"metadata": {
"accession": "IPR001576",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004618",
"name": "phosphoglycerate kinase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006096",
"name": "glycolytic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd00318": "Phosphoglycerate_kinase"
},
"hamap": {
"MF_00145": "Phosphoglycerate kinase [pgk]"
},
"panther": {
"PTHR11406": "PHOSPHOGLYCERATE KINASE"
},
"pirsf": {
"PIRSF000724": "Phosphoglycerate kinase"
},
"pfam": {
"PF00162": "Phosphoglycerate kinase"
},
"prints": {
"PR00477": "PHGLYCKINASE"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR001576",
"name": "Phosphoglycerate kinase",
"type": "Family",
"children": [
{
"accession": "IPR027250",
"name": "Phosphoglycerate kinase, euglenozoa",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Phosphoglycerate kinase",
"short": "Phosphoglycerate_kinase"
},
"description": [
{
"text": "<p>Phosphoglycerate kinase ([ec:2.7.2.3]) (PGK) is an enzyme that catalyses the formation of ATP to ADP and vice versa. In the second step of the second phase in glycolysis, 1,3-diphosphoglycerate is converted to 3-phosphoglycerate, forming one molecule of ATP. If the reverse were to occur, one molecule of ADP would be formed. This reaction is essential in most cells for the generation of ATP in aerobes, for fermentation in anaerobes and for carbon fixation in plants.</p>\n\n<p>PGK is found in all living organisms and its sequence has been highly conserved throughout evolution. The enzyme exists as a monomer containing two nearly equal-sized domains that correspond to the N-and C-termini of the protein (the last 15 C-terminal residues loop back into the N-terminal domain). 3-phosphoglycerate (3-PG) binds to the N-terminal, while the nucleotide substrates, MgATP or MgADP, bind to the C-terminal domain of the enzyme. This extended two-domain structure is associated with large-scale 'hinge-bending' conformational changes, similar to those found in hexokinase [[cite:PUB00006511]]. At the core of each domain is a 6-stranded parallel β-sheet surrounded by α helices. Domain 1 has a parallel β-sheet of six strands with an order of 342156, while domain 2 has a parallel β-sheet of six strands with an order of 321456. Analysis of the reversible unfolding of yeast phosphoglycerate kinase leads to the conclusion that the two lobes are capable of folding independently, consistent with the presence of intermediates on the folding pathway with a single domain folded [[cite:PUB00006255]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00006511": {
"PMID": 10593256,
"ISBN": null,
"volume": "31",
"issue": "2",
"year": 1999,
"title": "Folding funnels and conformational transitions via hinge-bending motions.",
"URL": null,
"raw_pages": "141-64",
"medline_journal": "Cell Biochem Biophys",
"ISO_journal": "Cell Biochem. Biophys.",
"authors": [
"Kumar S",
"Ma B",
"Tsai CJ",
"Wolfson H",
"Nussinov R."
],
"DOI_URL": null
},
"PUB00006482": {
"PMID": 6689547,
"ISBN": null,
"volume": "42",
"issue": "11-12",
"year": 1983,
"title": "Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects.",
"URL": null,
"raw_pages": "S263-7",
"medline_journal": "Biomed Biochim Acta",
"ISO_journal": "Biomed. Biochim. Acta",
"authors": [
"Yoshida A",
"Tani K."
],
"DOI_URL": null
},
"PUB00006255": {
"PMID": 2124145,
"ISBN": null,
"volume": "72",
"issue": "6-7",
"year": 1990,
"title": "Flexibility and folding of phosphoglycerate kinase.",
"URL": null,
"raw_pages": "417-29",
"medline_journal": "Biochimie",
"ISO_journal": "Biochimie",
"authors": [
"Yon JM",
"Desmadril M",
"Betton JM",
"Minard P",
"Ballery N",
"Missiakas D",
"Gaillard-Miran S",
"Perahia D",
"Mouawad L."
],
"DOI_URL": "http://dx.doi.org/10.1016/0300-9084(90)90066-P"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036043",
"name": "Phosphoglycerate kinase superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR015824",
"name": "Phosphoglycerate kinase, N-terminal",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 195,
"interactions": 0,
"matches": 38873,
"pathways": 32,
"proteins": 38226,
"proteomes": 21083,
"sets": 0,
"structural_models": {
"alphafold": 30977,
"bfvd": 0
},
"structures": 68,
"taxa": 40771
},
"entry_annotations": {
"alignment:seed": 596,
"alignment:full": 15444
},
"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": "GenProp1612",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1612"
},
{
"accession": "GenProp1344",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1344"
},
{
"accession": "GenProp1306",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1306"
},
{
"accession": "GenProp1599",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1599"
},
{
"accession": "GenProp1407",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1407"
},
{
"accession": "GenProp0691",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0691"
}
]
},
"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": "2.7.2.3",
"url": "https://enzyme.expasy.org/EC/2.7.2.3"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1v6s",
"name": "Crystal Structure of Phosphoglycerate Kinase from Thermus thermophilus HB8"
}
}
}
