node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ctaB | ctaC | BSU14880 | BSU14890 | Protoheme IX farnesyltransferase 2; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | Cytochrome caa3 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 |
ctaB | ctaD | BSU14880 | BSU14900 | Protoheme IX farnesyltransferase 2; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | Cytochrome caa3 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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | 0.999 |
ctaB | ctaE | BSU14880 | BSU14910 | Protoheme IX farnesyltransferase 2; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | Cytochrome caa3 oxidase (subunit III); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase subunit 3 family. | 0.999 |
ctaB | ctaF | BSU14880 | BSU14920 | Protoheme IX farnesyltransferase 2; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | Cytochrome caa3 oxidase (subunit IV); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase bacterial subunit 4 family. | 0.997 |
ctaB | qcrB | BSU14880 | BSU22550 | Protoheme IX farnesyltransferase 2; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | Menaquinol:cytochrome c oxidoreductase (cytochrome b subunit); Component of the menaquinol-cytochrome c reductase complex. | 0.467 |
ctaC | ctaB | BSU14890 | BSU14880 | Cytochrome caa3 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). | Protoheme IX farnesyltransferase 2; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | 0.999 |
ctaC | ctaD | BSU14890 | BSU14900 | Cytochrome caa3 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). | Cytochrome caa3 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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | 0.999 |
ctaC | ctaE | BSU14890 | BSU14910 | Cytochrome caa3 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). | Cytochrome caa3 oxidase (subunit III); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase subunit 3 family. | 0.999 |
ctaC | ctaF | BSU14890 | BSU14920 | Cytochrome caa3 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). | Cytochrome caa3 oxidase (subunit IV); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase bacterial subunit 4 family. | 0.999 |
ctaC | qcrA | BSU14890 | BSU22560 | Cytochrome caa3 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). | Menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit); Component of the menaquinol-cytochrome c reductase complex. The Rieske protein is a high potential 2Fe-2S protein. | 0.999 |
ctaC | qcrB | BSU14890 | BSU22550 | Cytochrome caa3 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). | Menaquinol:cytochrome c oxidoreductase (cytochrome b subunit); Component of the menaquinol-cytochrome c reductase complex. | 0.999 |
ctaC | qcrC | BSU14890 | BSU22540 | Cytochrome caa3 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). | Menaquinol:cytochrome c oxidoreductase (cytochrome cc subunit); Component of the menaquinol-cytochrome c reductase complex. | 0.999 |
ctaC | sdhB | BSU14890 | BSU28430 | Cytochrome caa3 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). | Succinate dehydrogenase (iron-sulfur protein); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. | 0.999 |
ctaC | sdhC | BSU14890 | BSU28450 | Cytochrome caa3 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). | Succinate dehydrogenase (cytochrome b558 subunit); Di-heme cytochrome of the succinate dehydrogenase complex. | 0.999 |
ctaC | yhfW | BSU14890 | BSU10390 | Cytochrome caa3 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). | Putative Rieske [2Fe-2S] oxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.999 |
ctaD | ctaB | BSU14900 | BSU14880 | Cytochrome caa3 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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | Protoheme IX farnesyltransferase 2; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | 0.999 |
ctaD | ctaC | BSU14900 | BSU14890 | Cytochrome caa3 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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | Cytochrome caa3 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 |
ctaD | ctaE | BSU14900 | BSU14910 | Cytochrome caa3 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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | Cytochrome caa3 oxidase (subunit III); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase subunit 3 family. | 0.999 |
ctaD | ctaF | BSU14900 | BSU14920 | Cytochrome caa3 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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | Cytochrome caa3 oxidase (subunit IV); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase bacterial subunit 4 family. | 0.999 |
ctaD | qcrA | BSU14900 | BSU22560 | Cytochrome caa3 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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | Menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit); Component of the menaquinol-cytochrome c reductase complex. The Rieske protein is a high potential 2Fe-2S protein. | 0.990 |