| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMF_834 | atpB | AMF_834 | AMF_839 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 0.814 |
| AMF_834 | coxA | AMF_834 | AMF_767 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | Cytochrome c oxidase subunit I (coxA); 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. | 0.447 |
| AMF_834 | coxB | AMF_834 | AMF_766 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | Cytochrome c oxidase subunit II (coxB); 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). | 0.995 |
| AMF_834 | coxC | AMF_834 | AMF_982 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | Cytochrome C oxidase, subunit III (coxC); Psort: bacterial inner membrane --- Certainty= 0.370(Affirmative); COG1845 CyoC heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.995 |
| AMF_834 | ctaB | AMF_834 | AMF_768 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | Cytochrome c oxidase assembly factor (ctaB); 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. | 0.821 |
| AMF_834 | cycM | AMF_834 | AMF_142 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | Cytochrome C (cycM); Psort: bacterial inner membrane --- Certainty= 0.412(Affirmative); COG3303 NrfA formate-dependent nitrite reductase, periplasmic cytochrome c552 subunit. | 0.919 |
| AMF_834 | nuoH | AMF_834 | AMF_477 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | NADH dehydrogenase I chain H (nuoH); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | 0.921 |
| AMF_834 | nuoM | AMF_834 | AMF_550 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | NADH dehydrogenase I chain M (nuoM); Psort: bacterial inner membrane --- Certainty= 0.711(Affirmative); COG1008 NuoM NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.930 |
| AMF_834 | petB | AMF_834 | AMF_580 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | Cytochrome B (petB); Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.974 |
| AMF_834 | petC | AMF_834 | AMF_578 | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | Cytochrome c1, heme protein precursor; Psort: bacterial inner membrane --- Certainty= 0.317(Affirmative); COG2857 CYT1 cytochrome c1. | 0.913 |
| atpB | AMF_834 | AMF_839 | AMF_834 | ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | 0.814 |
| atpB | coxA | AMF_839 | AMF_767 | ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Cytochrome c oxidase subunit I (coxA); 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. | 0.836 |
| atpB | coxB | AMF_839 | AMF_766 | ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Cytochrome c oxidase subunit II (coxB); 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). | 0.980 |
| atpB | coxC | AMF_839 | AMF_982 | ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Cytochrome C oxidase, subunit III (coxC); Psort: bacterial inner membrane --- Certainty= 0.370(Affirmative); COG1845 CyoC heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.998 |
| atpB | nuoH | AMF_839 | AMF_477 | ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | NADH dehydrogenase I chain H (nuoH); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | 0.986 |
| atpB | nuoM | AMF_839 | AMF_550 | ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | NADH dehydrogenase I chain M (nuoM); Psort: bacterial inner membrane --- Certainty= 0.711(Affirmative); COG1008 NuoM NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.986 |
| atpB | petB | AMF_839 | AMF_580 | ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Cytochrome B (petB); Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.982 |
| coxA | AMF_834 | AMF_767 | AMF_834 | Cytochrome c oxidase subunit I (coxA); 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. | Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | 0.447 |
| coxA | atpB | AMF_767 | AMF_839 | Cytochrome c oxidase subunit I (coxA); 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. | ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 0.836 |
| coxA | coxB | AMF_767 | AMF_766 | Cytochrome c oxidase subunit I (coxA); 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 subunit II (coxB); 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 |