| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPA2863 | RPA2866 | RPA2863 | RPA2866 | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | 0.999 |
| RPA2863 | RPA3771 | RPA2863 | RPA3771 | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.811 |
| RPA2863 | RPA3922 | RPA2863 | RPA3922 | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative acetoin dehydrogenase (TPP-dependent) beta chain. | 0.969 |
| RPA2863 | RPA3923 | RPA2863 | RPA3923 | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative acetoin dehydrogenase (TPP-dependent) alpha chain. | 0.893 |
| RPA2863 | dldH | RPA2863 | RPA0185 | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Dihydrolipoamide dehydrogenase, E3 component of 2-oxoglutarate and pyruvate dehydrogenase complexes; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.910 |
| RPA2863 | nuoCD | RPA2863 | RPA4262 | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | NADH-ubiquinone dehydrogenase chain 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 N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.723 |
| RPA2863 | pdhA | RPA2863 | RPA2867 | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Pyruvate dehydrogenase E1 alpha subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | 0.995 |
| RPA2863 | sucA | RPA2863 | RPA0189 | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative alpha-ketoglutarate dehydrogenase (E1 subunit); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.991 |
| RPA2863 | sucC | RPA2863 | RPA0191 | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | succinyl-coA synthetase beta chain; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. | 0.695 |
| RPA2866 | RPA2863 | RPA2866 | RPA2863 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.999 |
| RPA2866 | RPA3771 | RPA2866 | RPA3771 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.838 |
| RPA2866 | RPA3922 | RPA2866 | RPA3922 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Putative acetoin dehydrogenase (TPP-dependent) beta chain. | 0.869 |
| RPA2866 | RPA3923 | RPA2866 | RPA3923 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Putative acetoin dehydrogenase (TPP-dependent) alpha chain. | 0.999 |
| RPA2866 | dldH | RPA2866 | RPA0185 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Dihydrolipoamide dehydrogenase, E3 component of 2-oxoglutarate and pyruvate dehydrogenase complexes; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.999 |
| RPA2866 | gor | RPA2866 | RPA1983 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Putative glutathione reductase; Maintains high levels of reduced glutathione. | 0.997 |
| RPA2866 | nuoCD | RPA2866 | RPA4262 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | NADH-ubiquinone dehydrogenase chain 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 N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.980 |
| RPA2866 | pdhA | RPA2866 | RPA2867 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Pyruvate dehydrogenase E1 alpha subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | 0.999 |
| RPA2866 | sucA | RPA2866 | RPA0189 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Putative alpha-ketoglutarate dehydrogenase (E1 subunit); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.997 |
| RPA2866 | sucC | RPA2866 | RPA0191 | Pyruvate dehydrogenase E1 beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | succinyl-coA synthetase beta chain; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. | 0.944 |
| RPA3771 | RPA2863 | RPA3771 | RPA2863 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Dihydrolipoamide dehydrogenase, E3 Component of Pyruvate dehydrogenase multienzyme complex; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.811 |