node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
A0A194YRJ8 | C5XIC9_SORBI | A0A194YRJ8 | C5XIC9 | Proton_antipo_M domain-containing protein. | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | 0.973 |
A0A194YRJ8 | C5YUG3_SORBI | A0A194YRJ8 | C5YUG3 | Proton_antipo_M domain-containing protein. | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | 0.973 |
A0A194YRJ8 | Cox1 | A0A194YRJ8 | A0A1Z5RQP5 | Proton_antipo_M domain-containing protein. | Cytochrome c 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. | 0.951 |
A0A194YRJ8 | ndhD | A0A194YRJ8 | A1E9X4 | Proton_antipo_M domain-containing protein. | NAD(P)H-quinone oxidoreductase chain 4, chloroplastic. | 0.963 |
A0A194YRJ8 | ndhK | A0A194YRJ8 | A1E9S8 | Proton_antipo_M domain-containing protein. | NAD(P)H-quinone oxidoreductase subunit K, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Belongs to the complex I 20 kDa subunit family. | 0.981 |
C5XIC9_SORBI | A0A194YRJ8 | C5XIC9 | A0A194YRJ8 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | Proton_antipo_M domain-containing protein. | 0.973 |
C5XIC9_SORBI | C5YUG3_SORBI | C5XIC9 | C5YUG3 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | 0.544 |
C5XIC9_SORBI | Cox1 | C5XIC9 | A0A1Z5RQP5 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | Cytochrome c 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. | 0.955 |
C5XIC9_SORBI | ndhD | C5XIC9 | A1E9X4 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | NAD(P)H-quinone oxidoreductase chain 4, chloroplastic. | 0.962 |
C5XIC9_SORBI | ndhF | C5XIC9 | Q33066 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). | 0.944 |
C5YUG3_SORBI | A0A194YRJ8 | C5YUG3 | A0A194YRJ8 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | Proton_antipo_M domain-containing protein. | 0.973 |
C5YUG3_SORBI | C5XIC9_SORBI | C5YUG3 | C5XIC9 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | 0.544 |
C5YUG3_SORBI | Cox1 | C5YUG3 | A0A1Z5RQP5 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | Cytochrome c 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. | 0.955 |
C5YUG3_SORBI | ndhD | C5YUG3 | A1E9X4 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | NAD(P)H-quinone oxidoreductase chain 4, chloroplastic. | 0.962 |
C5YUG3_SORBI | ndhF | C5YUG3 | Q33066 | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). | 0.944 |
Cox1 | A0A194YRJ8 | A0A1Z5RQP5 | A0A194YRJ8 | Cytochrome c 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. | Proton_antipo_M domain-containing protein. | 0.951 |
Cox1 | C5XIC9_SORBI | A0A1Z5RQP5 | C5XIC9 | Cytochrome c 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. | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | 0.955 |
Cox1 | C5YUG3_SORBI | A0A1Z5RQP5 | C5YUG3 | Cytochrome c 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. | Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. | 0.955 |
Cox1 | ndhD | A0A1Z5RQP5 | A1E9X4 | Cytochrome c 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. | NAD(P)H-quinone oxidoreductase chain 4, chloroplastic. | 0.983 |
Cox1 | ndhF | A0A1Z5RQP5 | Q33066 | Cytochrome c 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. | NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). | 0.951 |