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{
"metadata": {
"accession": "IPR004810",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0008864",
"name": "formyltetrahydrofolate deformylase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006189",
"name": "'de novo' IMP biosynthetic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"ncbifam": {
"NF004684": "formyltetrahydrofolate deformylase",
"TIGR00655": "formyltetrahydrofolate deformylase"
},
"panther": {
"PTHR42706": "FORMYLTETRAHYDROFOLATE DEFORMYLASE"
},
"hamap": {
"MF_01927": "Formyltetrahydrofolate deformylase [purU]"
},
"prints": {
"PR01575": "FFH4HYDRLASE"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR004810",
"name": "Formyltetrahydrofolate deformylase",
"type": "Family",
"children": []
},
"name": {
"name": "Formyltetrahydrofolate deformylase",
"short": "PurU"
},
"description": [
{
"text": "<p>An Escherichia coli gene designated purU has been identified and characterised. The gene codes for a 280-amino-acid protein, PurU ([swissprot:P37051], [ec:3.5.1.10]). PurU is an enzyme that catalyses the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate \n[[cite:PUB00007025], [cite:PUB00007026]].</p>\n\n<p><reaction>10-formyltetrahydrofolate + H(2)O = formate +tetrahydrofolate</reaction></p>\n\n<p>Formyl-FH4 hydrolase generates the formate that is used by purT-encoded 5'-phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase, a hexamer of 32kDa subunits, is activated by methionine and inhibited by glycine. Heterotropic cooperativity is observed for activation by methionine in the presence of glycine and for inhibition by glycine in the presence of methionine. These results suggest that formyl-FH4 hydrolase is a regulatory enzyme whose main function is to balance the pools of FH4 and C1-FH4 in response to changing growth conditions. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively.</p>\n\n<p>This entry also includes PurU from Arabidopsis, which is involved in photorespiration. It prevents the excessive accumulation of 5-formyl tetrahydrofolate (THF), a potent inhibitor of the Gly decarboxylase/Ser hydroxymethyltransferase complex [[cite:PUB00099957]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00007025": {
"PMID": 7868604,
"ISBN": null,
"volume": "177",
"issue": "5",
"year": 1995,
"title": "Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts in Escherichia coli.",
"URL": null,
"raw_pages": "1292-8",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Nagy PL",
"Marolewski A",
"Benkovic SJ",
"Zalkin H."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=7868604"
},
"PUB00007026": {
"PMID": 8226647,
"ISBN": null,
"volume": "175",
"issue": "21",
"year": 1993,
"title": "purU, a source of formate for purT-dependent phosphoribosyl-N-formylglycinamide synthesis.",
"URL": null,
"raw_pages": "7066-73",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Nagy PL",
"McCorkle GM",
"Zalkin H."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8226647"
},
"PUB00099957": {
"PMID": 18628352,
"ISBN": null,
"volume": "20",
"issue": "7",
"year": 2008,
"title": "Arabidopsis 10-formyl tetrahydrofolate deformylases are essential for photorespiration.",
"URL": null,
"raw_pages": "1818-32",
"medline_journal": "Plant Cell",
"ISO_journal": "Plant Cell",
"authors": [
"Collakova E",
"Goyer A",
"Naponelli V",
"Krassovskaya I",
"Gregory JF 3rd",
"Hanson AD",
"Shachar-Hill Y."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036477",
"name": "Formyl transferase, N-terminal domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 21854,
"pathways": 3,
"proteins": 21535,
"proteomes": 12347,
"sets": 0,
"structural_models": {
"alphafold": 16084,
"bfvd": 0
},
"structures": 6,
"taxa": 19968
},
"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": "3.5.1.10",
"url": "https://enzyme.expasy.org/EC/3.5.1.10"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3obi",
"name": "Crystal structure of a formyltetrahydrofolate deformylase (NP_949368) from RHODOPSEUDOMONAS PALUSTRIS CGA009 at 1.95 A resolution"
}
}
}
