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KML35995.1 | Quinol oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (622 aa) | ||||
KML35736.1 | Quinol oxidase subunit 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. (330 aa) | ||||
KML35735.1 | Quinol oxidase subunit 1; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (658 aa) | ||||
KML35734.1 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (201 aa) | ||||
KML35999.1 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (155 aa) | ||||
KML35997.1 | Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. (111 aa) | ||||
KML35996.1 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (209 aa) | ||||
KML35994.1 | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (358 aa) | ||||
KML36271.1 | Subunit D of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; contains an oxidoreductase domain; catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (497 aa) | ||||
KML36489.1 | Subunit D of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; contains an oxidoreductase domain; catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (496 aa) | ||||
KML39826.1 | Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (488 aa) | ||||
KML39825.1 | Cytochrome c oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (183 aa) | ||||
KML45240.1 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (110 aa) | ||||
KML46305.1 | Cytochrome c oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (123 aa) | ||||
nuoN | NADH:ubiquinone oxidoreductase subunit N; 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; Belongs to the complex I subunit 2 family. (506 aa) | ||||
KML46457.1 | NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (505 aa) | ||||
KML46456.1 | NADH:ubiquinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (622 aa) | ||||
KML46454.1 | NADH:ubiquinone oxidoreductase subunit J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. (173 aa) | ||||
KML46450.1 | NADH-quinone oxidoreductase subunit C; Derived by automated computational analysis using gene prediction method: Protein Homology. (427 aa) | ||||
nqo6 | NADH dehydrogenase; 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. (170 aa) | ||||
nuoA | NADH:ubiquinone oxidoreductase subunit A; 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; Belongs to the complex I subunit 3 family. (124 aa) | ||||
KML46680.1 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (413 aa) | ||||
KML46675.1 | Cytochrome B5; Derived by automated computational analysis using gene prediction method: Protein Homology. (158 aa) |