node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EU91_0617 | EU91_0618 | EU91_0617 | EU91_0618 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | Cytochrome c oxidase polypeptide 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 |
EU91_0617 | EU91_0619 | EU91_0617 | EU91_0619 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | Cytochrome c oxidase polypeptide 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 |
EU91_0617 | EU91_0773 | EU91_0617 | EU91_0773 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | Insulinase family (Peptidase family M16); Alternative locus ID: PGP2_1079. | 0.902 |
EU91_0617 | EU91_0774 | EU91_0617 | EU91_0774 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | Mitochondrial processing peptidase-like protein; Alternative locus ID: PGP2_1080; Belongs to the peptidase M16 family. | 0.902 |
EU91_0617 | ndhH | EU91_0617 | EU91_0342 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | NAD(P)H-quinone oxidoreductase chain 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.964 |
EU91_0617 | ndhI | EU91_0617 | EU91_0329 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | NAD(P)H-quinone oxidoreductase chain I; 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; Belongs to the complex I 23 kDa subunit family. | 0.963 |
EU91_0617 | ndhJ | EU91_0617 | EU91_0461 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | NAD(P)H-quinone oxidoreductase chain J; 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. | 0.963 |
EU91_0617 | ndhK | EU91_0617 | EU91_0462 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | NAD(P)H-quinone oxidoreductase chain K; 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; Belongs to the complex I 20 kDa subunit family. | 0.957 |
EU91_0617 | petB | EU91_0617 | EU91_0496 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | Cytochrome b6-f complex 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 |
EU91_0617 | petC | EU91_0617 | EU91_0636 | Cytochrome c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | Cytochrome b6-f complex iron-sulfur subunit PetC1; 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 |
EU91_0618 | EU91_0617 | EU91_0618 | EU91_0617 | Cytochrome c oxidase polypeptide 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 c oxidase polypeptide III; Alternative locus ID: PGP2_0939. | 0.999 |
EU91_0618 | EU91_0619 | EU91_0618 | EU91_0619 | Cytochrome c oxidase polypeptide 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 c oxidase polypeptide 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 |
EU91_0618 | EU91_0773 | EU91_0618 | EU91_0773 | Cytochrome c oxidase polypeptide 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. | Insulinase family (Peptidase family M16); Alternative locus ID: PGP2_1079. | 0.890 |
EU91_0618 | EU91_0774 | EU91_0618 | EU91_0774 | Cytochrome c oxidase polypeptide 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. | Mitochondrial processing peptidase-like protein; Alternative locus ID: PGP2_1080; Belongs to the peptidase M16 family. | 0.890 |
EU91_0618 | ndhH | EU91_0618 | EU91_0342 | Cytochrome c oxidase polypeptide 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. | NAD(P)H-quinone oxidoreductase chain 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.974 |
EU91_0618 | ndhI | EU91_0618 | EU91_0329 | Cytochrome c oxidase polypeptide 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. | NAD(P)H-quinone oxidoreductase chain I; 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; Belongs to the complex I 23 kDa subunit family. | 0.957 |
EU91_0618 | ndhJ | EU91_0618 | EU91_0461 | Cytochrome c oxidase polypeptide 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. | NAD(P)H-quinone oxidoreductase chain J; 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. | 0.975 |
EU91_0618 | ndhK | EU91_0618 | EU91_0462 | Cytochrome c oxidase polypeptide 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. | NAD(P)H-quinone oxidoreductase chain K; 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; Belongs to the complex I 20 kDa subunit family. | 0.963 |
EU91_0618 | petB | EU91_0618 | EU91_0496 | Cytochrome c oxidase polypeptide 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 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 |
EU91_0618 | petC | EU91_0618 | EU91_0636 | Cytochrome c oxidase polypeptide 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 iron-sulfur subunit PetC1; 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. | 0.998 |