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"metadata": {
"accession": "PS50999",
"entry_id": null,
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"integrated": "IPR011759",
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"name": {
"name": "Cytochrome oxidase subunit II transmembrane region profile",
"short": "COX2_TM"
},
"description": [
{
"text": "<p>Cytochrome c oxidase (EC 1.9.3.1) [[cite:PUB00000581]] is an oligomeric enzymatic complex\nwhich is a component of the respiratory chain and is involved in the transfer\nof electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is\nlocated in the mitochondrial inner membrane; in aerobic prokaryotes it is\nfound in the plasma membrane. The enzyme complex consists of 3-4 subunits\n(prokaryotes) to up to 13 polypeptides (mammals).\n\nSubunit 2 (CO II) transfers the electrons from cytochrome c to the catalytic\nsubunit 1. It contains two adjacent transmembrane regions in its N-terminus\nand the major part of the protein is exposed to the periplasmic or to the\nmitochondrial intermembrane space, respectively. CO II provides the substrate-\nbinding site and contains a copper center called Cu(A), located in the\nextramembrane domain, probably the primary acceptor in\ncytochrome c oxidase. An exception is the corresponding subunit of the\ncbb3-type oxidase which lacks the copper A redox-center. Several bacterial CO\nII have a C-terminal extension that contains a covalently bound heme c.\n\nIt has been shown [[cite:PUB00001426]] that nitrous oxide reductase (EC 1.7.99.6) (gene nosZ)\nof Pseudomonas has sequence similarity in its C-terminus to CO II. This enzyme\nis part of the bacterial respiratory system which is activated under anaerobic\nconditions in the presence of nitrate or nitrous oxide. NosZ is a periplasmic\nhomodimer that contains a dinuclear copper center, probably located in a 3-\ndimensional fold similar to the cupredoxin-like fold that has been suggested\nfor the copper-binding site of CO II [3].\n\nThe dinuclear purple copper center is formed by 2 histidines and 2 cysteines\n[5]. We used this region as a signature pattern. The conserved valine and the\nconserved methionine are said to be involved in stabilizing the copper-binding\nfold by interacting with each other. We also developed two profiles, one\ndirected against the transmembrane region and one against the copper center.</p>",
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"literature": {
"PUB00000581": {
"PMID": 6307356,
"ISBN": null,
"volume": "726",
"issue": "2",
"year": 1983,
"title": "Structure of cytochrome c oxidase.",
"URL": null,
"raw_pages": "135-48",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Capaldi RA",
"Malatesta F",
"Darley-Usmar VM."
],
"DOI_URL": "http://dx.doi.org/10.1016/0304-4173(83)90003-4"
},
"PUB00001426": {
"PMID": 1324835,
"ISBN": null,
"volume": "208",
"issue": "1",
"year": 1992,
"title": "Derived amino acid sequences of the nosZ gene (respiratory N2O reductase) from Alcaligenes eutrophus, Pseudomonas aeruginosa and Pseudomonas stutzeri reveal potential copper-binding residues. Implications for the CuA site of N2O reductase and cytochrome-c oxidase.",
"URL": null,
"raw_pages": "31-40",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Zumft WG",
"Dreusch A",
"Lochelt S",
"Cuypers H",
"Friedrich B",
"Schneider B."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1992.tb17156.x"
}
},
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"alphafold": 81074,
"bfvd": 0
},
"structures": 179,
"taxa": 89953
},
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"is_llm": false,
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"representative_structure": null
}
}
