node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
COLO4_02670 | COLO4_06081 | A0A1R3L0N6 | A0A1R3KP43 | 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. | Thioredoxin-like 2Fe-2S ferredoxin. | 0.973 |
COLO4_02670 | COLO4_15792 | A0A1R3L0N6 | A0A1R3JL75 | 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. | Zinc finger, CCHC-type. | 0.973 |
COLO4_02670 | COLO4_17137 | A0A1R3L0N6 | A0A1R3JE13 | 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. | Glycerol-3-phosphate dehydrogenase; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. | 0.784 |
COLO4_02670 | COLO4_25931 | A0A1R3L0N6 | A0A1R3HZD9 | 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. | Uncharacterized protein. | 0.980 |
COLO4_02670 | COLO4_31625 | A0A1R3L0N6 | A0A1R3H3W0 | 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. | Protein kinase domain-containing protein. | 0.646 |
COLO4_02670 | ndhJ | A0A1R3L0N6 | A0A1R3KZH0 | 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 J, 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. | 0.992 |
COLO4_04173 | COLO4_06081 | A0A1R3KUZ0 | A0A1R3KP43 | 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. | Thioredoxin-like 2Fe-2S ferredoxin. | 0.973 |
COLO4_04173 | COLO4_15792 | A0A1R3KUZ0 | A0A1R3JL75 | 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. | Zinc finger, CCHC-type. | 0.973 |
COLO4_04173 | COLO4_17137 | A0A1R3KUZ0 | A0A1R3JE13 | 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. | Glycerol-3-phosphate dehydrogenase; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. | 0.784 |
COLO4_04173 | COLO4_25931 | A0A1R3KUZ0 | A0A1R3HZD9 | 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. | Uncharacterized protein. | 0.980 |
COLO4_04173 | COLO4_31625 | A0A1R3KUZ0 | A0A1R3H3W0 | 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. | Protein kinase domain-containing protein. | 0.646 |
COLO4_04173 | ndhJ | A0A1R3KUZ0 | A0A1R3KZH0 | 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 J, 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. | 0.992 |
COLO4_06081 | COLO4_02670 | A0A1R3KP43 | A0A1R3L0N6 | Thioredoxin-like 2Fe-2S ferredoxin. | 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. | 0.973 |
COLO4_06081 | COLO4_04173 | A0A1R3KP43 | A0A1R3KUZ0 | Thioredoxin-like 2Fe-2S ferredoxin. | 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. | 0.973 |
COLO4_06081 | COLO4_25931 | A0A1R3KP43 | A0A1R3HZD9 | Thioredoxin-like 2Fe-2S ferredoxin. | Uncharacterized protein. | 0.999 |
COLO4_06081 | COLO4_31625 | A0A1R3KP43 | A0A1R3H3W0 | Thioredoxin-like 2Fe-2S ferredoxin. | Protein kinase domain-containing protein. | 0.654 |
COLO4_06081 | ndhJ | A0A1R3KP43 | A0A1R3KZH0 | Thioredoxin-like 2Fe-2S ferredoxin. | NAD(P)H-quinone oxidoreductase subunit J, 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. | 0.999 |
COLO4_15792 | COLO4_02670 | A0A1R3JL75 | A0A1R3L0N6 | Zinc finger, CCHC-type. | 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. | 0.973 |
COLO4_15792 | COLO4_04173 | A0A1R3JL75 | A0A1R3KUZ0 | Zinc finger, CCHC-type. | 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. | 0.973 |
COLO4_15792 | COLO4_25931 | A0A1R3JL75 | A0A1R3HZD9 | Zinc finger, CCHC-type. | Uncharacterized protein. | 0.999 |