| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CEK14728.1 | CEK14731.1 | CP488_00932 | CP488_00933 | PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: caa(3)-type oxidase, subunit IV; JGI identifier:CP488_00932. | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | 0.990 |
| CEK14728.1 | CEK14734.1 | CP488_00932 | CP488_00934 | PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: caa(3)-type oxidase, subunit IV; JGI identifier:CP488_00932. | Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; JGI identifier:CP488_00934; Belongs to the heme-copper respiratory oxidase family. | 0.984 |
| CEK14728.1 | CEK14738.1 | CP488_00932 | CP488_00935 | PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: caa(3)-type oxidase, subunit IV; JGI identifier:CP488_00932. | 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). | 0.990 |
| CEK14728.1 | CEK14747.1 | CP488_00932 | CP488_00936 | PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: caa(3)-type oxidase, subunit IV; JGI identifier:CP488_00932. | Protein SCO1; JGI identifier:CP488_00936. | 0.914 |
| CEK14728.1 | CEK14766.1 | CP488_00932 | CP488_00942 | PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: caa(3)-type oxidase, subunit IV; JGI identifier:CP488_00932. | Quinol:cytochrome c oxidoreductase iron-sulfur protein precursor; PFAM: 4Fe-4S dicluster domain; JGI identifier:CP488_00942. | 0.836 |
| CEK14728.1 | CEK14769.1 | CP488_00932 | CP488_00943 | PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: caa(3)-type oxidase, subunit IV; JGI identifier:CP488_00932. | Quinol:cytochrome c oxidoreductase pentaheme cytochrome subunit; PFAM: Class III cytochrome C family; Cytochrome c7; JGI identifier:CP488_00943. | 0.816 |
| CEK14728.1 | ctaB | CP488_00932 | CP488_02817 | PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: caa(3)-type oxidase, subunit IV; JGI identifier:CP488_00932. | 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. | 0.915 |
| CEK14731.1 | CEK14728.1 | CP488_00933 | CP488_00932 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: caa(3)-type oxidase, subunit IV; JGI identifier:CP488_00932. | 0.990 |
| CEK14731.1 | CEK14734.1 | CP488_00933 | CP488_00934 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; JGI identifier:CP488_00934; Belongs to the heme-copper respiratory oxidase family. | 0.999 |
| CEK14731.1 | CEK14738.1 | CP488_00933 | CP488_00935 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | 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 |
| CEK14731.1 | CEK14747.1 | CP488_00933 | CP488_00936 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | Protein SCO1; JGI identifier:CP488_00936. | 0.930 |
| CEK14731.1 | CEK14766.1 | CP488_00933 | CP488_00942 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | Quinol:cytochrome c oxidoreductase iron-sulfur protein precursor; PFAM: 4Fe-4S dicluster domain; JGI identifier:CP488_00942. | 0.823 |
| CEK14731.1 | CEK14769.1 | CP488_00933 | CP488_00943 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | Quinol:cytochrome c oxidoreductase pentaheme cytochrome subunit; PFAM: Class III cytochrome C family; Cytochrome c7; JGI identifier:CP488_00943. | 0.979 |
| CEK14731.1 | CEK18859.1 | CP488_00933 | CP488_02326 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; JGI identifier:CP488_02326. | 0.980 |
| CEK14731.1 | ctaB | CP488_00933 | CP488_02817 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | 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. | 0.998 |
| CEK14731.1 | nuoA | CP488_00933 | CP488_02315 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | NADH:ubiquinone oxidoreductase subunit 3 (chain A); 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; Belongs to the complex I subunit 3 family. | 0.980 |
| CEK14731.1 | nuoH | CP488_00933 | CP488_02322 | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | NADH dehydrogenase subunit H; 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. | 0.978 |
| CEK14734.1 | CEK14728.1 | CP488_00934 | CP488_00932 | Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; JGI identifier:CP488_00934; Belongs to the heme-copper respiratory oxidase family. | PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: caa(3)-type oxidase, subunit IV; JGI identifier:CP488_00932. | 0.984 |
| CEK14734.1 | CEK14731.1 | CP488_00934 | CP488_00933 | Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; JGI identifier:CP488_00934; Belongs to the heme-copper respiratory oxidase family. | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; JGI identifier:CP488_00933. | 0.999 |
| CEK14734.1 | CEK14738.1 | CP488_00934 | CP488_00935 | Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; JGI identifier:CP488_00934; Belongs to the heme-copper respiratory oxidase family. | 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 |