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LOCUS WP_010989325 659 aa linear BCT 04-JUN-2024 ACCESSION WP_010989325 VERSION WP_010989325.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes ORGANISM Listeria monocytogenes Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 659) AUTHORS Lemma,E., Simon,J., Schagger,H. and Kroger,A. TITLE Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of Bacillus subtilis JOURNAL Arch Microbiol 163 (6), 432-438 (1995) PUBMED 7575098 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR02882.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..659 /organism="Listeria monocytogenes" /db_xref="taxon:1639" gene 1..659 /gene="qoxB" Protein 1..659 /product="cytochrome aa3 quinol oxidase subunit I" /GO_component="GO:0016020 - membrane [Evidence IEA]" /GO_function="GO:0004129 - cytochrome-c oxidase activity [Evidence IEA]" /GO_function="GO:0005507 - copper ion binding [Evidence IEA]" /GO_function="GO:0020037 - heme binding [Evidence IEA]" /GO_process="GO:0015990 - electron transport coupled proton transport [Evidence IEA]" /calculated_mol_wt=74784 Region 2..641 /region_name="Heme_Cu_Oxidase_I" /note="Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is...; cl00275" /db_xref="CDD:469701" Site order(58,119,129,136,139,193..194,200,204) /site_type="active" /note="D-pathway [active]" /db_xref="CDD:238832" Site order(68,72,75..76,92,95..97) /site_type="other" /note="Putative ubiquinol binding site [chemical binding]" /db_xref="CDD:238832" Site order(100,414,418,460,499) /site_type="other" /note="Low-spin heme (heme b) binding site [chemical binding]" /db_xref="CDD:238832" Site order(264,269..270,400,404..405,474) /site_type="other" /note="Putative water exit pathway" /db_xref="CDD:238832" Site order(277,326..327,412) /site_type="other" /note="Binuclear center (heme o3/CuB) [ion binding]" /db_xref="CDD:238832" Site order(277,281,292,326..327,352,355) /site_type="active" /note="K-pathway [active]" /db_xref="CDD:238832" Site order(327,404..405,474..475) /site_type="other" /note="Putative proton exit pathway" /db_xref="CDD:238832" ORIGIN 1 mkwnefivtg dpmilgaqis ivlvsigvva lltytkkwkw lmkewissvd hkkigimyll 61 aavlmffrgg vdalmmrtql alpdmkflda qhynevfsth gtimilfmam pfiiglmnia 121 vplqigardv afpflnnlsf wtffmgamlf nlsfviggsp dagwtnyapl atdfsagygi 181 nfyllgvqia gigtlmtgin ffvtilrmrt kgmtlmkmpm ftwsslitsl iiifafpvlt 241 valalmsfdr lfgtafftlt ngglpmmwan lfwvwghpev yivilpafgi fseiistfsr 301 kklfgypamv aamavislls flvwvhhfft mgsgalvnsf fsittmmiai ptgikifnwl 361 ftmykgritf ttpmlwslaf ipnfvvggvt gvmlamaaad yqyhntyflv shfhyvliag 421 tvfscfaglt ywypkmvgyr lnekigkwff wifvvgfnvc ffpqyflgld gmprriytyv 481 qgdgwttlnf istvggflmg vaflvlcyni yysyknskre vtgdpwdart lewatssavp 541 pkynfavlpe wndlddfwnr kqkgdpyvnd knykpihmps ntmvgfvmsv fffiagfglv 601 fywywmgiig lvgilgcmiy rsfqnndgyh veveeikate ehnarelatg vkegnpwnl