node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
coxB | ctaC | PputUW4_02715 | PputUW4_00049 | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 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). | 0.980 |
coxB | ctaE1 | PputUW4_02715 | PputUW4_00052 | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | [C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.962 |
coxB | ctaE2 | PputUW4_02715 | PputUW4_02712 | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | [C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.999 |
coxB | cyoB | PputUW4_02715 | PputUW4_00852 | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | [C] COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1; Belongs to the heme-copper respiratory oxidase family. | 0.946 |
coxB | cyoC | PputUW4_02715 | PputUW4_00853 | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | [C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.923 |
coxB | cyoD | PputUW4_02715 | PputUW4_00854 | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | [C] COG3125 Heme/copper-type cytochrome/quinol oxidase, subunit 4. | 0.907 |
coxB | cyoE2 | PputUW4_02715 | PputUW4_00855 | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 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. | 0.810 |
coxB | nuoCD | PputUW4_02715 | PputUW4_01800 | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | NADH-quinone oxidoreductase subunit C/D; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.970 |
coxB | nuoH | PputUW4_02715 | PputUW4_01796 | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | NADH-quinone oxidoreductase 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. | 0.875 |
ctaC | coxB | PputUW4_00049 | PputUW4_02715 | 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). | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 0.980 |
ctaC | ctaE1 | PputUW4_00049 | PputUW4_00052 | 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). | [C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.999 |
ctaC | ctaE2 | PputUW4_00049 | PputUW4_02712 | 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). | [C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.993 |
ctaC | cyoA | PputUW4_00049 | PputUW4_00851 | 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). | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 0.485 |
ctaC | cyoB | PputUW4_00049 | PputUW4_00852 | 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). | [C] COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1; Belongs to the heme-copper respiratory oxidase family. | 0.992 |
ctaC | cyoC | PputUW4_00049 | PputUW4_00853 | 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). | [C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.984 |
ctaC | cyoD | PputUW4_00049 | PputUW4_00854 | 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). | [C] COG3125 Heme/copper-type cytochrome/quinol oxidase, subunit 4. | 0.933 |
ctaC | cyoE2 | PputUW4_00049 | PputUW4_00855 | 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). | 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. | 0.813 |
ctaC | nuoCD | PputUW4_00049 | PputUW4_01800 | 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). | NADH-quinone oxidoreductase subunit C/D; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.989 |
ctaC | nuoH | PputUW4_00049 | PputUW4_01796 | 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). | NADH-quinone oxidoreductase 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. | 0.877 |
ctaE1 | coxB | PputUW4_00052 | PputUW4_02715 | [C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | [C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 0.962 |