| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKU10670.1 | AKU13165.1 | AzCIB_0765 | AzCIB_3272 | Bifunctional protein putA; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Isocitrate dehydrogenase, NADP-dependent. | 0.429 |
| AKU10670.1 | aceK | AzCIB_0765 | AzCIB_3274 | Bifunctional protein putA; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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. | 0.402 |
| AKU13165.1 | AKU10670.1 | AzCIB_3272 | AzCIB_0765 | Isocitrate dehydrogenase, NADP-dependent. | Bifunctional protein putA; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.429 |
| AKU13165.1 | AKU13166.1 | AzCIB_3272 | AzCIB_3273 | Isocitrate dehydrogenase, NADP-dependent. | Isocitrate dehydrogenase, NADP-dependent; Belongs to the monomeric-type IDH family. | 0.954 |
| AKU13165.1 | AKU13182.1 | AzCIB_3272 | AzCIB_3289 | Isocitrate dehydrogenase, NADP-dependent. | Isocitrate lyase. | 0.455 |
| AKU13165.1 | aceK | AzCIB_3272 | AzCIB_3274 | Isocitrate dehydrogenase, NADP-dependent. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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. | 0.916 |
| AKU13165.1 | glcB | AzCIB_3272 | AzCIB_3263 | Isocitrate dehydrogenase, NADP-dependent. | 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. | 0.680 |
| AKU13166.1 | AKU13165.1 | AzCIB_3273 | AzCIB_3272 | Isocitrate dehydrogenase, NADP-dependent; Belongs to the monomeric-type IDH family. | Isocitrate dehydrogenase, NADP-dependent. | 0.954 |
| AKU13166.1 | aceK | AzCIB_3273 | AzCIB_3274 | Isocitrate dehydrogenase, NADP-dependent; Belongs to the monomeric-type IDH family. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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. | 0.522 |
| AKU13182.1 | AKU13165.1 | AzCIB_3289 | AzCIB_3272 | Isocitrate lyase. | Isocitrate dehydrogenase, NADP-dependent. | 0.455 |
| AKU13182.1 | aceK | AzCIB_3289 | AzCIB_3274 | Isocitrate lyase. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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. | 0.905 |
| AKU13182.1 | glcB | AzCIB_3289 | AzCIB_3263 | Isocitrate lyase. | 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. | 0.993 |
| aceK | AKU10670.1 | AzCIB_3274 | AzCIB_0765 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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. | Bifunctional protein putA; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.402 |
| aceK | AKU13165.1 | AzCIB_3274 | AzCIB_3272 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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, NADP-dependent. | 0.916 |
| aceK | AKU13166.1 | AzCIB_3274 | AzCIB_3273 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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, NADP-dependent; Belongs to the monomeric-type IDH family. | 0.522 |
| aceK | AKU13182.1 | AzCIB_3274 | AzCIB_3289 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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. | 0.905 |
| aceK | glcB | AzCIB_3274 | AzCIB_3263 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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. | 0.507 |
| glcB | AKU13165.1 | AzCIB_3263 | AzCIB_3272 | 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, NADP-dependent. | 0.680 |
| glcB | AKU13182.1 | AzCIB_3263 | AzCIB_3289 | 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. | 0.993 |
| glcB | aceK | AzCIB_3263 | AzCIB_3274 | 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. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; 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. | 0.507 |
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