node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EKD07191.1 | EKD07192.1 | SPLC1_S490220 | SPLC1_S490230 | Putative cytochrome c oxidase subunit III. | Cytochrome c oxidase subunit I; 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. | 0.999 |
EKD07191.1 | EKD07193.1 | SPLC1_S490220 | SPLC1_S490240 | Putative cytochrome c oxidase subunit III. | Putative cytochrome c oxidase subunit II; 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). | 0.999 |
EKD07191.1 | EKD07194.1 | SPLC1_S490220 | SPLC1_S490250 | Putative cytochrome c oxidase subunit III. | Cytochrome oxidase assembly. | 0.995 |
EKD07191.1 | EKD08058.1 | SPLC1_S490220 | SPLC1_S300790 | Putative cytochrome c oxidase subunit III. | NADH dehydrogenase I subunit F. | 0.997 |
EKD07191.1 | EKD09676.1 | SPLC1_S490220 | SPLC1_S171250 | Putative cytochrome c oxidase subunit III. | Cytochrome d ubiquinol oxidase subunit II. | 0.978 |
EKD07191.1 | ctaB | SPLC1_S490220 | SPLC1_S490260 | Putative cytochrome c oxidase subunit III. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.999 |
EKD07191.1 | ndhA | SPLC1_S490220 | SPLC1_S081900 | Putative cytochrome c oxidase subunit III. | NADH dehydrogenase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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. | 0.994 |
EKD07191.1 | ndhB | SPLC1_S490220 | SPLC1_S170820 | Putative cytochrome c oxidase subunit III. | Proton-translocating NADH-quinone oxidoreductase chain N; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.977 |
EKD07191.1 | petB | SPLC1_S490220 | SPLC1_S541110 | Putative cytochrome c oxidase subunit III. | Cytochrome b/b6 domain protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | 0.999 |
EKD07191.1 | petC | SPLC1_S490220 | SPLC1_S380310 | Putative cytochrome c oxidase subunit III. | Cytochrome b6-f complex Fe-S subunit; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | 0.999 |
EKD07192.1 | EKD07191.1 | SPLC1_S490230 | SPLC1_S490220 | Cytochrome c oxidase subunit I; 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. | Putative cytochrome c oxidase subunit III. | 0.999 |
EKD07192.1 | EKD07193.1 | SPLC1_S490230 | SPLC1_S490240 | Cytochrome c oxidase subunit I; 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. | Putative cytochrome c oxidase subunit II; 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). | 0.999 |
EKD07192.1 | EKD07194.1 | SPLC1_S490230 | SPLC1_S490250 | Cytochrome c oxidase subunit I; 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. | Cytochrome oxidase assembly. | 0.996 |
EKD07192.1 | EKD08058.1 | SPLC1_S490230 | SPLC1_S300790 | Cytochrome c oxidase subunit I; 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. | NADH dehydrogenase I subunit F. | 0.998 |
EKD07192.1 | EKD09676.1 | SPLC1_S490230 | SPLC1_S171250 | Cytochrome c oxidase subunit I; 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. | Cytochrome d ubiquinol oxidase subunit II. | 0.966 |
EKD07192.1 | ctaB | SPLC1_S490230 | SPLC1_S490260 | Cytochrome c oxidase subunit I; 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. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.999 |
EKD07192.1 | ndhA | SPLC1_S490230 | SPLC1_S081900 | Cytochrome c oxidase subunit I; 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. | NADH dehydrogenase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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. | 0.990 |
EKD07192.1 | ndhB | SPLC1_S490230 | SPLC1_S170820 | Cytochrome c oxidase subunit I; 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-translocating NADH-quinone oxidoreductase chain N; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.977 |
EKD07192.1 | petB | SPLC1_S490230 | SPLC1_S541110 | Cytochrome c oxidase subunit I; 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. | Cytochrome b/b6 domain protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | 0.999 |
EKD07192.1 | petC | SPLC1_S490230 | SPLC1_S380310 | Cytochrome c oxidase subunit I; 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. | Cytochrome b6-f complex Fe-S subunit; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | 0.999 |