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{
"metadata": {
"accession": "IPR000807",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004424",
"name": "imidazoleglycerol-phosphate dehydratase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0000105",
"name": "L-histidine biosynthetic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd07914": "Imidazoleglycerol-phosphate dehydratase"
},
"panther": {
"PTHR23133": "IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7"
},
"hamap": {
"MF_00076": "Imidazoleglycerol-phosphate dehydratase [hisB]"
},
"pfam": {
"PF00475": "Imidazoleglycerol-phosphate dehydratase"
}
},
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"accession": "IPR000807",
"name": "Imidazoleglycerol-phosphate dehydratase",
"type": "Family",
"children": [
{
"accession": "IPR020566",
"name": "Histidine biosynthesis bifunctional protein HisB",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Imidazoleglycerol-phosphate dehydratase",
"short": "ImidazoleglycerolP_deHydtase"
},
"description": [
{
"text": "<p>Imidazoleglycerol-phosphate dehydratase (IGPD; [ec:4.2.1.19]) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by pseudo-dyad symmetry, perhaps as a result of an ancient gene duplication. The apo-form of IGPD exists as a catalytically inactive trimer which, in the presence of specific divalent metal cations such as manganese (Mn2+), cobalt (Co2+), cadmium (Cd2+), nickel (Ni2+), iron (Fe2+) and zinc (Zn2+), assembles to form a biologically active high molecular weight metalloenzyme; a 24-mer with 4-3-2 symmetry. Each 24-mer has 24 active sites, and contains around 1.5 metal ions per monomer, each monomer contributing residues to three separate active sites.</p>\r\n\r\n<p>IGPD enzymes are monofunctional in fungi, plants, archaea and some eubacteria while they are encoded as bifunctional enzymes in other eubacteria, such that the enzyme is fused to histidinol-phosphate phosphatase, the penultimate enzyme of the histidine biosynthesis pathway. The histidine biosynthesis pathway is a potential target for development of herbicides, and IGPD is a target for the triazole phosphonate herbicides [[cite:PUB00040491], [cite:PUB00022600], [cite:PUB00046135], [cite:PUB00079788], [cite:PUB00079789], [cite:PUB00079790], [cite:PUB00079791], [cite:PUB00079792], [cite:PUB00079793], [cite:PUB00079794], [cite:PUB00079795], [cite:PUB00009674]].</p>",
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"year": 2005,
"title": "Structure and mechanism of imidazoleglycerol-phosphate dehydratase.",
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"raw_pages": "1809-17",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Glynn SE",
"Baker PJ",
"Sedelnikova SE",
"Davies CL",
"Eadsforth TC",
"Levy CW",
"Rodgers HF",
"Blackburn GM",
"Hawkes TR",
"Viner R",
"Rice DW."
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"DOI_URL": "http://dx.doi.org/10.1016/j.str.2005.08.012"
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"volume": "61",
"issue": "Pt 8",
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"title": "Purification, crystallization and preliminary crystallographic analysis of Arabidopsis thaliana imidazoleglycerol-phosphate dehydratase.",
"URL": null,
"raw_pages": "776-8",
"medline_journal": "Acta Crystallogr Sect F Struct Biol Cryst Commun",
"ISO_journal": "Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.",
"authors": [
"Glynn SE",
"Baker PJ",
"Sedelnikova SE",
"Levy CW",
"Rodgers HF",
"Blank J",
"Hawkes TR",
"Rice DW."
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"issue": "1-2",
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"title": "Oxo-vanadium as a spin probe for the investigation of the metal coordination environment of imidazole glycerol phosphate dehydratase.",
"URL": null,
"raw_pages": "161-8",
"medline_journal": "J Inorg Biochem",
"ISO_journal": "J. Inorg. Biochem.",
"authors": [
"Petersen J",
"Hawkes TR",
"Lowe DJ."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0162-0134(00)00025-8"
},
"PUB00079795": {
"PMID": 2664449,
"ISBN": null,
"volume": "216",
"issue": "2-3",
"year": 1989,
"title": "Cloning of histidine genes of Azospirillum brasilense: organization of the ABFH gene cluster and nucleotide sequence of the hisB gene.",
"URL": null,
"raw_pages": "224-9",
"medline_journal": "Mol Gen Genet",
"ISO_journal": "Mol. Gen. Genet.",
"authors": [
"Fani R",
"Bazzicalupo M",
"Damiani G",
"Bianchi A",
"Schipani C",
"Sgaramella V",
"Polsinelli M."
],
"DOI_URL": "http://dx.doi.org/10.1007/BF00334360"
},
"PUB00079793": {
"PMID": 9767718,
"ISBN": null,
"volume": "37",
"issue": "5",
"year": 1998,
"title": "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes of histidine biosynthesis.",
"URL": null,
"raw_pages": "356-8",
"medline_journal": "Curr Microbiol",
"ISO_journal": "Curr. Microbiol.",
"authors": [
"Clark MA",
"Baumann L",
"Baumann P."
],
"DOI_URL": "http://dx.doi.org/10.1007/s002849900392"
},
"PUB00079794": {
"PMID": 8511965,
"ISBN": null,
"volume": "9",
"issue": "4",
"year": 1993,
"title": "Molecular genetics in Saccharomyces kluyveri: the HIS3 homolog and its use as a selectable marker gene in S. kluyveri and Saccharomyces cerevisiae.",
"URL": null,
"raw_pages": "351-61",
"medline_journal": "Yeast",
"ISO_journal": "Yeast",
"authors": [
"Weinstock KG",
"Strathern JN."
],
"DOI_URL": "http://dx.doi.org/10.1002/yea.320090405"
},
"PUB00009674": {
"PMID": 3007936,
"ISBN": null,
"volume": "202",
"issue": "1",
"year": 1986,
"title": "Gene structure in the histidine operon of Escherichia coli. Identification and nucleotide sequence of the hisB gene.",
"URL": null,
"raw_pages": "42-7",
"medline_journal": "Mol Gen Genet",
"ISO_journal": "Mol. Gen. Genet.",
"authors": [
"Chiariotti L",
"Nappo AG",
"Carlomagno MS",
"Bruni CB."
],
"DOI_URL": "http://dx.doi.org/10.1007/BF00330514"
},
"PUB00079791": {
"PMID": 8066131,
"ISBN": null,
"volume": "105",
"issue": "2",
"year": 1994,
"title": "Isolation and characterization of cDNAs encoding imidazoleglycerolphosphate dehydratase from Arabidopsis thaliana.",
"URL": null,
"raw_pages": "579-83",
"medline_journal": "Plant Physiol",
"ISO_journal": "Plant Physiol.",
"authors": [
"Tada S",
"Volrath S",
"Guyer D",
"Scheidegger A",
"Ryals J",
"Ohta D",
"Ward E."
],
"DOI_URL": "http://dx.doi.org/10.1104/pp.105.2.579"
},
"PUB00022600": {
"PMID": 14724278,
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"volume": "279",
"issue": "15",
"year": 2004,
"title": "Crystal structure of imidazole glycerol-phosphate dehydratase: duplication of an unusual fold.",
"URL": null,
"raw_pages": "15491-8",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Sinha SC",
"Chaudhuri BN",
"Burgner JW",
"Yakovleva G",
"Davisson VJ",
"Smith JL."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M312733200"
},
"PUB00079792": {
"PMID": 3001645,
"ISBN": null,
"volume": "13",
"issue": "23",
"year": 1985,
"title": "Nucleotide sequence and transcriptional mapping of the yeast pet56-his3-ded1 gene region.",
"URL": null,
"raw_pages": "8587-601",
"medline_journal": "Nucleic Acids Res",
"ISO_journal": "Nucleic Acids Res.",
"authors": [
"Struhl K."
],
"DOI_URL": "http://dx.doi.org/10.1093/nar/13.23.8587"
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"volume": "9",
"issue": "14",
"year": 1999,
"title": "Design and synthesis of beta-carboxamido phosphonates as potent inhibitors of imidazole glycerol phosphate dehydratase.",
"URL": null,
"raw_pages": "2053-8",
"medline_journal": "Bioorg Med Chem Lett",
"ISO_journal": "Bioorg. Med. Chem. Lett.",
"authors": [
"Schweitzer BA",
"Loida PJ",
"Thompson-Mize RL",
"CaJacob CA",
"Hegde SG."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0960-894X(99)00338-8"
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"title": "Molecular evolution of hisB genes.",
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"raw_pages": "225-37",
"medline_journal": "J Mol Evol",
"ISO_journal": "J. Mol. Evol.",
"authors": [
"Brilli M",
"Fani R."
],
"DOI_URL": "http://dx.doi.org/10.1007/s00239-003-2547-x"
}
},
"set_info": null,
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"name": "Imidazole glycerol phosphate dehydratase domain superfamily",
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"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.",
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"name": "Crystal structure of Imidazole Glycerol Phosphate Dehydratase from Mycobacterium tuberculosis at 1.61 A resolution"
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