| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPA0789 | aceA | RPA0789 | RPA4394 | Putative serine-glyoxylate aminotransferase. | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.917 |
| RPA0789 | glcB | RPA0789 | RPA4216 | Putative serine-glyoxylate aminotransferase. | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | 0.929 |
| RPA0789 | glcF | RPA0789 | RPA1132 | Putative serine-glyoxylate aminotransferase. | Glycolate oxidase subunit, (Fe-S)protein, GlcF. | 0.932 |
| RPA0789 | prpB | RPA0789 | RPA2395 | Putative serine-glyoxylate aminotransferase. | Putative carboxyphosphonoenolpyruvate phosphonomutase; Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate. | 0.494 |
| RPA0789 | pta | RPA0789 | RPA4567 | Putative serine-glyoxylate aminotransferase. | Putative phosphate acetyltransferase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.494 |
| aceA | RPA0789 | RPA4394 | RPA0789 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative serine-glyoxylate aminotransferase. | 0.917 |
| aceA | aceK | RPA4394 | RPA0347 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.964 |
| aceA | ackA | RPA4394 | RPA4566 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative acetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family. | 0.939 |
| aceA | acnA | RPA4394 | RPA0202 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Aconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. | 0.939 |
| aceA | glcB | RPA4394 | RPA4216 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | 0.997 |
| aceA | glcF | RPA4394 | RPA1132 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Glycolate oxidase subunit, (Fe-S)protein, GlcF. | 0.937 |
| aceA | prpB | RPA4394 | RPA2395 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative carboxyphosphonoenolpyruvate phosphonomutase; Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate. | 0.926 |
| aceA | pta | RPA4394 | RPA4567 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative phosphate acetyltransferase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.963 |
| aceA | sucC | RPA4394 | RPA0191 | Isocitrate lyase; 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. | 0.958 |
| aceA | sucD | RPA4394 | RPA0190 | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | succinyl-CoA synthetase alpha-subunit; 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 alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. | 0.922 |
| aceK | aceA | RPA0347 | RPA4394 | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.964 |
| aceK | ackA | RPA0347 | RPA4566 | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Putative acetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family. | 0.437 |
| aceK | glcB | RPA0347 | RPA4216 | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | 0.545 |
| ackA | aceA | RPA4566 | RPA4394 | Putative acetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family. | Isocitrate lyase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.939 |
| ackA | aceK | RPA4566 | RPA0347 | Putative acetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family. | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.437 |