{"metadata":{"accession":"PF02578","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR003730","hierarchy":null,"name":{"name":"Multi-copper polyphenol oxidoreductase laccase","short":"Cu-oxidase_4"},"description":[{"text":"<p>Laccases are multi-copper oxidoreductases able to oxidise a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms [[cite:PUB00044734]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Multicopper_oxidase","extract":"<p>In molecular biology, <b>multicopper oxidases</b> are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre; dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. There are three spectroscopically different copper centres found in multicopper oxidases: type 1, type 2 and type 3. Multicopper oxidases consist of 2, 3 or 6 of these homologous domains, which also share homology with the cupredoxins azurin and plastocyanin. Structurally, these domains consist of a cupredoxin-like fold, a beta-sandwich consisting of 7 strands in 2 beta-sheets, arranged in a Greek-key beta-barrel.</p>","thumbnail":null}],"literature":{"PUB00044734":{"PMID":16740638,"ISBN":null,"volume":"281","issue":"32","year":2006,"title":"Novel polyphenol oxidase mined from a metagenome expression library of bovine rumen: biochemical properties, structural analysis, and phylogenetic relationships.","URL":null,"raw_pages":"22933-42","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Beloqui A","Pita M","Polaina J","Martinez-Arias A","Golyshina OV","Zumarraga M","Yakimov MM","Garcia-Arellano H","Alcalde M","Fernandez VM","Elborough K","Andreu JM","Ballesteros A","Plou FJ","Timmis KN","Ferrer M","Golyshin PN."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M600577200"}},"set_info":{"accession":"CL0663","name":"CNF1_YfiH"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":16,"interactions":0,"matches":15292,"pathways":0,"proteins":15217,"proteomes":14656,"sets":1,"structural_models":{"alphafold":9887},"structures":13,"taxa":22070},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":360,"alignment:full":8198},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1rw0","name":"Crystal structure of protein yfiH from Salmonella enterica serovar Typhi, Pfam DUF152"}}}