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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR034291",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004789",
"name": "thiamine-phosphate diphosphorylase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0009228",
"name": "thiamine biosynthetic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"ncbifam": {
"TIGR00693": "thiamine phosphate synthase"
},
"hamap": {
"MF_00097": "Thiamine-phosphate synthase [thiE]"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR034291",
"name": "Thiamine phosphate synthase",
"type": "Family",
"children": [
{
"accession": "IPR016229",
"name": "Thiamine-phosphate synthase, cyanobacterial/bacterial",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Thiamine phosphate synthase",
"short": "TMP_synthase"
},
"description": [
{
"text": "<p>Thiamine phosphate synthase (TPS), also known as thiamin phosphate pyrophosphorylase (TMP-PPase), catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate in the thiamine biosynthesis pathway [[cite:PUB00005784]]. This family includes the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria [[cite:PUB00005854]], and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase ThiM [[cite:PUB00002882]]. The plant enzyme is also bifunctional [[cite:PUB00017548]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00005784": {
"PMID": 9139923,
"ISBN": null,
"volume": "179",
"issue": "9",
"year": 1997,
"title": "Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis.",
"URL": null,
"raw_pages": "3030-5",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Zhang Y",
"Taylor SV",
"Chiu HJ",
"Begley TP."
],
"DOI_URL": "http://jb.asm.org/cgi/content/abstract/179/9/3030"
},
"PUB00017548": {
"PMID": 9700068,
"ISBN": null,
"volume": "37",
"issue": "6",
"year": 1998,
"title": "A Brassica cDNA clone encoding a bifunctional hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase involved in thiamin biosynthesis.",
"URL": null,
"raw_pages": "955-66",
"medline_journal": "Plant Mol Biol",
"ISO_journal": "Plant Mol. Biol.",
"authors": [
"Kim YS",
"Nosaka K",
"Downs DM",
"Kwak JM",
"Park D",
"Chung IK",
"Nam HG."
],
"DOI_URL": "http://dx.doi.org/10.1023/A:1006030617502"
},
"PUB00002882": {
"PMID": 7982968,
"ISBN": null,
"volume": "269",
"issue": "48",
"year": 1994,
"title": "Isolation and characterization of the THI6 gene encoding a bifunctional thiamin-phosphate pyrophosphorylase/hydroxyethylthiazole kinase from Saccharomyces cerevisiae.",
"URL": null,
"raw_pages": "30510-6",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Nosaka K",
"Nishimura H",
"Kawasaki Y",
"Tsujihara T",
"Iwashima A."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/269/48/30510.pdf"
},
"PUB00005854": {
"PMID": 10382260,
"ISBN": null,
"volume": "171",
"issue": "5",
"year": 1999,
"title": "Thiamin biosynthesis in prokaryotes.",
"URL": null,
"raw_pages": "293-300",
"medline_journal": "Arch Microbiol",
"ISO_journal": "Arch. Microbiol.",
"authors": [
"Begley TP",
"Downs DM",
"Ealick SE",
"McLafferty FW",
"Van Loon AP",
"Taylor S",
"Campobasso N",
"Chiu HJ",
"Kinsland C",
"Reddick JJ",
"Xi J."
],
"DOI_URL": "http://dx.doi.org/10.1007/s002030050713"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036206",
"name": "Thiamin phosphate synthase superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR013785",
"name": "Aldolase-type TIM barrel",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 24762,
"pathways": 7,
"proteins": 24756,
"proteomes": 15428,
"sets": 0,
"structural_models": {
"alphafold": 19285,
"bfvd": 0
},
"structures": 18,
"taxa": 26761
},
"entry_annotations": {},
"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": "GenProp0254",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0254"
}
]
},
"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": "2.5.1.3",
"url": "https://enzyme.expasy.org/EC/2.5.1.3"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1xi3",
"name": "Thiamine phosphate pyrophosphorylase from Pyrococcus furiosus Pfu-1255191-001"
}
}
}
