node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
fixB | nuoC | b0042 | b2286 | Electron transfer flavoprotein alpha subunit; Required for anaerobic carnitine reduction. May bring reductant to CaiA | Nadh:ubiquinone oxidoreductase, fused cd subunit; 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 | 0.663 |
fixB | ygcR | b0042 | b2770 | Electron transfer flavoprotein alpha subunit; Required for anaerobic carnitine reduction. May bring reductant to CaiA | Putative flavoprotein; May play a role in a redox process | 0.851 |
grcA | slyD | b2579 | b3349 | Stress-induced alternate pyruvate formate-lyase subunit; Acts as a radical domain for damaged PFL and possibly other radical proteins | Fkbp-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...] | 0.489 |
grcA | yfbU | b2579 | b2294 | Stress-induced alternate pyruvate formate-lyase subunit; Acts as a radical domain for damaged PFL and possibly other radical proteins | annotation not available | 0.821 |
grcA | ygcR | b2579 | b2770 | Stress-induced alternate pyruvate formate-lyase subunit; Acts as a radical domain for damaged PFL and possibly other radical proteins | Putative flavoprotein; May play a role in a redox process | 0.813 |
nuoC | fixB | b2286 | b0042 | Nadh:ubiquinone oxidoreductase, fused cd subunit; 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 | Electron transfer flavoprotein alpha subunit; Required for anaerobic carnitine reduction. May bring reductant to CaiA | 0.663 |
nuoC | ydiR | b2286 | b1698 | Nadh:ubiquinone oxidoreductase, fused cd subunit; 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 | Putative electron transfer flavoprotein, fad-binding subunit; May play a role in a redox process | 0.663 |
nuoC | ygcQ | b2286 | b2769 | Nadh:ubiquinone oxidoreductase, fused cd subunit; 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 | Putative flavoprotein; May play a role in a redox process | 0.663 |
nuoC | ygcR | b2286 | b2770 | Nadh:ubiquinone oxidoreductase, fused cd subunit; 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 | Putative flavoprotein; May play a role in a redox process | 0.775 |
rbn | yfbU | b2268 | b2294 | Rnase bn, trna processing enzyme; Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities, depending on the nature of the substrate and of the added divalent cation, and on its 3'-terminal structure. Can process the 3' termini of both CCA-less and CCA-containing tRNA precursors. CCA-less tRNAs are cleaved endonucleolytically after the discriminator base, whereas residues following the CCA sequence can be removed exonucleolytically or endonucleolytically in CCA-containing molecules. Does not remove the CCA sequence. May also be involved in the degradation [...] | annotation not available | 0.610 |
rbn | ygcR | b2268 | b2770 | Rnase bn, trna processing enzyme; Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities, depending on the nature of the substrate and of the added divalent cation, and on its 3'-terminal structure. Can process the 3' termini of both CCA-less and CCA-containing tRNA precursors. CCA-less tRNAs are cleaved endonucleolytically after the discriminator base, whereas residues following the CCA sequence can be removed exonucleolytically or endonucleolytically in CCA-containing molecules. Does not remove the CCA sequence. May also be involved in the degradation [...] | Putative flavoprotein; May play a role in a redox process | 0.735 |
slyD | grcA | b3349 | b2579 | Fkbp-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...] | Stress-induced alternate pyruvate formate-lyase subunit; Acts as a radical domain for damaged PFL and possibly other radical proteins | 0.489 |
slyD | yfbU | b3349 | b2294 | Fkbp-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...] | annotation not available | 0.680 |
slyD | ygcR | b3349 | b2770 | Fkbp-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...] | Putative flavoprotein; May play a role in a redox process | 0.828 |
ydiR | nuoC | b1698 | b2286 | Putative electron transfer flavoprotein, fad-binding subunit; May play a role in a redox process | Nadh:ubiquinone oxidoreductase, fused cd subunit; 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 | 0.663 |
ydiR | ygcR | b1698 | b2770 | Putative electron transfer flavoprotein, fad-binding subunit; May play a role in a redox process | Putative flavoprotein; May play a role in a redox process | 0.881 |
yfbU | grcA | b2294 | b2579 | annotation not available | Stress-induced alternate pyruvate formate-lyase subunit; Acts as a radical domain for damaged PFL and possibly other radical proteins | 0.821 |
yfbU | rbn | b2294 | b2268 | annotation not available | Rnase bn, trna processing enzyme; Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities, depending on the nature of the substrate and of the added divalent cation, and on its 3'-terminal structure. Can process the 3' termini of both CCA-less and CCA-containing tRNA precursors. CCA-less tRNAs are cleaved endonucleolytically after the discriminator base, whereas residues following the CCA sequence can be removed exonucleolytically or endonucleolytically in CCA-containing molecules. Does not remove the CCA sequence. May also be involved in the degradation [...] | 0.610 |
yfbU | slyD | b2294 | b3349 | annotation not available | Fkbp-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...] | 0.680 |
yfbU | ygcR | b2294 | b2770 | annotation not available | Putative flavoprotein; May play a role in a redox process | 0.878 |