{"metadata":{"accession":"A0A1X0JCH9","id":"A0A1X0JCH9_9MYCO","source_organism":{"taxId":"75922","scientificName":"Mycolicibacterium tusciae","fullName":"Mycolicibacterium tusciae"},"name":"NADH-quinone oxidoreductase subunit K","description":["NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient"],"length":100,"sequence":"MTLQTVLLAAAAVFSVGLYGALSQQVVVMVMMGLELMINAIILAAAGFWWFVMPAPSGQVLLLVVIAAMTVEMAMGFAIATALHRERRTDMTDTAADLSG","proteome":"UP000192411","gene":"nuoK","go_terms":[{"identifier":"GO:0016651","name":"oxidoreductase activity, acting on NAD(P)H","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0042773","name":"ATP synthesis coupled electron transport","category":{"code":"P","name":"biological_process"}}],"protein_evidence":3,"source_database":"unreviewed","is_fragment":false,"in_alphafold":true,"ida_accession":"5c384e151efd07be17d94f5774ea581a4dbdd6cf","counters":{"domain_architectures":33116,"entries":5,"isoforms":0,"proteomes":1,"sets":0,"structures":0,"taxa":1,"dbEntries":{"cathgene3d":1,"hamap":1,"pfam":1,"interpro":2},"proteome":1,"taxonomy":1,"similar_proteins":33116}}}