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{
"metadata": {
"accession": "cd13881",
"entry_id": null,
"type": "domain",
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"source_database": "cdd",
"member_databases": null,
"integrated": null,
"hierarchy": null,
"name": {
"name": "The second cupredoxin domain of a multicopper oxidase McoC and similar proteins",
"short": "CuRO_2_McoC_like"
},
"description": [
{
"text": "<p>This family includes bacterial multicopper oxidases (MCOs) represented by McoC from the pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic MCO, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with the reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. They are composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. [[cite:PUB00035913], [cite:PUB00083025], [cite:PUB00083026], [cite:PUB00001382], [cite:PUB00083027], [cite:PUB00083028], [cite:PUB00083029], [cite:PUB00130776], [cite:PUB00067282]]</p>",
"llm": false,
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"wikipedia": null,
"literature": {
"PUB00001382": {
"PMID": 2404764,
"ISBN": null,
"volume": "187",
"issue": "2",
"year": 1990,
"title": "The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships.",
"URL": null,
"raw_pages": "341-52",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Messerschmidt A",
"Huber R."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1990.tb15311.x"
},
"PUB00083025": {
"PMID": 17639274,
"ISBN": null,
"volume": "64",
"issue": "19-20",
"year": 2007,
"title": "Structure and function of type I copper in multicopper oxidases.",
"URL": null,
"raw_pages": "2642-56",
"medline_journal": "Cell Mol Life Sci",
"ISO_journal": "Cell. Mol. Life Sci.",
"authors": [
"Sakurai T",
"Kataoka K."
],
"DOI_URL": "http://dx.doi.org/10.1007/s00018-007-7183-y"
},
"PUB00130776": {
"PMID": 18931123,
"ISBN": null,
"volume": "190",
"issue": "24",
"year": 2008,
"title": "A Multicopper oxidase (Cj1516) and a CopA homologue (Cj1161) are major components of the copper homeostasis system of Campylobacter jejuni.",
"URL": null,
"raw_pages": "8075-85",
"medline_journal": "J Bacteriol",
"ISO_journal": "J Bacteriol",
"authors": [
"Hall SJ",
"Hitchcock A",
"Butler CS",
"Kelly DJ."
],
"DOI_URL": null
},
"PUB00067282": {
"PMID": 22127520,
"ISBN": null,
"volume": "4",
"issue": "1",
"year": 2012,
"title": "Crystal structure of the multicopper oxidase from the pathogenic bacterium Campylobacter jejuni CGUG11284: characterization of a metallo-oxidase.",
"URL": null,
"raw_pages": "37-47",
"medline_journal": "Metallomics",
"ISO_journal": "Metallomics",
"authors": [
"Silva CS",
"Durao P",
"Fillat A",
"Lindley PF",
"Martins LO",
"Bento I."
],
"DOI_URL": "http://dx.doi.org/10.1039/c1mt00156f"
},
"PUB00083027": {
"PMID": 16650005,
"ISBN": null,
"volume": "273",
"issue": "10",
"year": 2006,
"title": "Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences.",
"URL": null,
"raw_pages": "2308-26",
"medline_journal": "FEBS J",
"ISO_journal": "FEBS J.",
"authors": [
"Hoegger PJ",
"Kilaru S",
"James TY",
"Thacker JR",
"Kues U."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1742-4658.2006.05247.x"
},
"PUB00083028": {
"PMID": 21498547,
"ISBN": null,
"volume": "2011",
"issue": null,
"year": 2011,
"title": "The Laccase Engineering Database: a classification and analysis system for laccases and related multicopper oxidases.",
"URL": null,
"raw_pages": "bar006",
"medline_journal": "Database (Oxford)",
"ISO_journal": "Database (Oxford)",
"authors": [
"Sirim D",
"Wagner F",
"Wang L",
"Schmid RD",
"Pleiss J."
],
"DOI_URL": "http://dx.doi.org/10.1093/database/bar006"
},
"PUB00035913": {
"PMID": 16234932,
"ISBN": null,
"volume": null,
"issue": "21",
"year": 2005,
"title": "Dioxygen reduction by multi-copper oxidases; a structural perspective.",
"URL": null,
"raw_pages": "3507-13",
"medline_journal": "Dalton Trans",
"ISO_journal": null,
"authors": [
"Bento I",
"Martins LO",
"Gato Lopes G",
"Armenia Carrondo M",
"Lindley PF."
],
"DOI_URL": "http://dx.doi.org/10.1039/b504806k"
},
"PUB00083029": {
"PMID": 19844659,
"ISBN": null,
"volume": "67",
"issue": "3",
"year": 2010,
"title": "Laccases: a never-ending story.",
"URL": null,
"raw_pages": "369-85",
"medline_journal": "Cell Mol Life Sci",
"ISO_journal": "Cell. Mol. Life Sci.",
"authors": [
"Giardina P",
"Faraco V",
"Pezzella C",
"Piscitelli A",
"Vanhulle S",
"Sannia G."
],
"DOI_URL": "http://dx.doi.org/10.1007/s00018-009-0169-1"
},
"PUB00083026": {
"PMID": 19816718,
"ISBN": null,
"volume": "15",
"issue": "1",
"year": 2010,
"title": "Multicopper oxidases: a workshop on copper coordination chemistry, electron transfer, and metallophysiology.",
"URL": null,
"raw_pages": "15-28",
"medline_journal": "J Biol Inorg Chem",
"ISO_journal": "J. Biol. Inorg. Chem.",
"authors": [
"Kosman DJ."
],
"DOI_URL": "http://dx.doi.org/10.1007/s00775-009-0590-9"
}
},
"set_info": {
"accession": "cl19115",
"name": "Cupredoxin"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 924,
"pathways": 0,
"proteins": 924,
"proteomes": 507,
"sets": 1,
"structural_models": {
"alphafold": 727,
"bfvd": 0
},
"structures": 40,
"taxa": 1027
},
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"is_llm": false,
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}
}
