| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa1306 | PSHAa1308 | PSHAa1306 | PSHAa1308 | Putative transcriptional regulator of the LysR family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; regulator; Belongs to the LysR transcriptional regulatory family. | Putative quinone oxidoreductase, NADPH-dependent; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.418 |
| PSHAa1306 | aceK1 | PSHAa1306 | PSHAa1307 | Putative transcriptional regulator of the LysR family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; regulator; Belongs to the LysR transcriptional regulatory 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. | 0.609 |
| PSHAa1308 | PSHAa1306 | PSHAa1308 | PSHAa1306 | Putative quinone oxidoreductase, NADPH-dependent; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative transcriptional regulator of the LysR family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; regulator; Belongs to the LysR transcriptional regulatory family. | 0.418 |
| PSHAa1308 | aceK1 | PSHAa1308 | PSHAa1307 | Putative quinone oxidoreductase, NADPH-dependent; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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. | 0.539 |
| aceA | aceK1 | PSHAb0062 | PSHAa1307 | Isocitrate lyase 2; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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. | 0.730 |
| aceA | glcB | PSHAb0062 | PSHAb0061 | Isocitrate lyase 2; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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. | 0.999 |
| aceA | icd | PSHAb0062 | PSHAa1303 | Isocitrate lyase 2; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Isocitrate dehydrogenase, specific for NADP+; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.866 |
| aceK1 | PSHAa1306 | PSHAa1307 | PSHAa1306 | 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 transcriptional regulator of the LysR family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; regulator; Belongs to the LysR transcriptional regulatory family. | 0.609 |
| aceK1 | PSHAa1308 | PSHAa1307 | PSHAa1308 | 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 quinone oxidoreductase, NADPH-dependent; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.539 |
| aceK1 | aceA | PSHAa1307 | PSHAb0062 | 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 2; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.730 |
| aceK1 | glcB | PSHAa1307 | PSHAb0061 | 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. | 0.446 |
| aceK1 | icd | PSHAa1307 | PSHAa1303 | 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 dehydrogenase, specific for NADP+; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.823 |
| glcB | aceA | PSHAb0061 | PSHAb0062 | 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. | Isocitrate lyase 2; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.999 |
| glcB | aceK1 | PSHAb0061 | PSHAa1307 | 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. | 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. | 0.446 |
| glcB | icd | PSHAb0061 | PSHAa1303 | 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. | Isocitrate dehydrogenase, specific for NADP+; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.637 |
| icd | aceA | PSHAa1303 | PSHAb0062 | Isocitrate dehydrogenase, specific for NADP+; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Isocitrate lyase 2; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.866 |
| icd | aceK1 | PSHAa1303 | PSHAa1307 | Isocitrate dehydrogenase, specific for NADP+; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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. | 0.823 |
| icd | glcB | PSHAa1303 | PSHAb0061 | Isocitrate dehydrogenase, specific for NADP+; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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. | 0.637 |