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{
"metadata": {
"accession": "IPR026575",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004112",
"name": "cyclic-nucleotide phosphodiesterase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd07402": "Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR026575",
"name": "Cyclic nucleotide phosphodiesterase GpdQ/CpdA-like",
"type": "Family",
"children": [
{
"accession": "IPR046379",
"name": "3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Cyclic nucleotide phosphodiesterase GpdQ/CpdA-like",
"short": "GpdQ/CpdA-like"
},
"description": [
{
"text": "<p>This entry includes a group of cyclic nucleotide phosphodiesterases, including GpdQ and CpdA. They belong to the metallophosphatase (MPP) superfamily.</p>\n\n<p>GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents [[cite:PUB00051193]]. The GpdQ homologue, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity [[cite:PUB00083156]].</p>\n\n<p>CpdA hydrolyses cAMP to 5'-AMP. It plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes [[cite:PUB00060663]]. In Pseudomonas is specifically required for regulation of virulence factors and can also hydrolyse cGMP [[cite:PUB00060664]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00060663": {
"PMID": 8810311,
"ISBN": null,
"volume": "271",
"issue": "41",
"year": 1996,
"title": "Identification of the cpdA gene encoding cyclic 3',5'-adenosine monophosphate phosphodiesterase in Escherichia coli.",
"URL": null,
"raw_pages": "25423-9",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Imamura R",
"Yamanaka K",
"Ogura T",
"Hiraga S",
"Fujita N",
"Ishihama A",
"Niki H."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.271.41.25423"
},
"PUB00060664": {
"PMID": 20348254,
"ISBN": null,
"volume": "192",
"issue": "11",
"year": 2010,
"title": "In vitro and in vivo characterization of the Pseudomonas aeruginosa cyclic AMP (cAMP) phosphodiesterase CpdA, required for cAMP homeostasis and virulence factor regulation.",
"URL": null,
"raw_pages": "2779-90",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Fuchs EL",
"Brutinel ED",
"Klem ER",
"Fehr AR",
"Yahr TL",
"Wolfgang MC."
],
"DOI_URL": "http://dx.doi.org/10.1128/JB.00168-10"
},
"PUB00083156": {
"PMID": 18757371,
"ISBN": null,
"volume": "283",
"issue": "45",
"year": 2008,
"title": "A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activity.",
"URL": null,
"raw_pages": "30942-9",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Keppetipola N",
"Shuman S."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M805064200"
},
"PUB00051193": {
"PMID": 18831553,
"ISBN": null,
"volume": "130",
"issue": "43",
"year": 2008,
"title": "Substrate-promoted formation of a catalytically competent binuclear center and regulation of reactivity in a glycerophosphodiesterase from Enterobacter aerogenes.",
"URL": null,
"raw_pages": "14129-38",
"medline_journal": "J Am Chem Soc",
"ISO_journal": "J. Am. Chem. Soc.",
"authors": [
"Hadler KS",
"Tanifum EA",
"Yip SH",
"Mitic N",
"Guddat LW",
"Jackson CJ",
"Gahan LR",
"Nguyen K",
"Carr PD",
"Ollis DL",
"Hengge AC",
"Larrabee JA",
"Schenk G."
],
"DOI_URL": "http://dx.doi.org/10.1021/ja803346w"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR029052",
"name": "Metallo-dependent phosphatase-like",
"type": "homologous_superfamily"
},
{
"accession": "IPR042283",
"name": "GpdQ, catalytic alpha/beta sandwich domain",
"type": "homologous_superfamily"
},
{
"accession": "IPR042281",
"name": "GpdQ, beta-strand dimerisation domain",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 7980,
"pathways": 0,
"proteins": 7980,
"proteomes": 4139,
"sets": 0,
"structural_models": {
"alphafold": 6057,
"bfvd": 0
},
"structures": 10,
"taxa": 6867
},
"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": "3.1.4",
"url": "https://enzyme.expasy.org/EC/3.1.4"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3d03",
"name": "1.9A structure of Glycerophoshphodiesterase (GpdQ) from Enterobacter aerogenes"
}
}
}
