| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| LO55_1548 | LO55_314 | LO55_1548 | LO55_314 | Glutamine amidotransferases class-II family protein. | Carbon-nitrogen hydrolase family protein. | 0.755 |
| LO55_1548 | LO55_725 | LO55_1548 | LO55_725 | Glutamine amidotransferases class-II family protein. | Nitrogen regulatory P-II family protein; Belongs to the P(II) protein family. | 0.558 |
| LO55_1548 | glnA | LO55_1548 | LO55_332 | Glutamine amidotransferases class-II family protein. | glnA: glutamine synthetase, type I. | 0.966 |
| LO55_1548 | glnB | LO55_1548 | LO55_4758 | Glutamine amidotransferases class-II family protein. | Nitrogen regulatory P-II protein; Belongs to the P(II) protein family. | 0.611 |
| LO55_1548 | glnD | LO55_1548 | LO55_3586 | Glutamine amidotransferases class-II family protein. | protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | 0.558 |
| LO55_1548 | glnE | LO55_1548 | LO55_316 | Glutamine amidotransferases class-II family protein. | Glutamate-ammonia ligase adenylyltransferase family protein; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds th [...] | 0.529 |
| LO55_1548 | nadE | LO55_1548 | LO55_4759 | Glutamine amidotransferases class-II family protein. | NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.798 |
| LO55_1548 | pheA | LO55_1548 | LO55_47 | Glutamine amidotransferases class-II family protein. | CM_P2: chorismate mutase. | 0.509 |
| LO55_314 | LO55_1548 | LO55_314 | LO55_1548 | Carbon-nitrogen hydrolase family protein. | Glutamine amidotransferases class-II family protein. | 0.755 |
| LO55_314 | LO55_315 | LO55_314 | LO55_315 | Carbon-nitrogen hydrolase family protein. | Hypothetical protein. | 0.832 |
| LO55_314 | glnA | LO55_314 | LO55_332 | Carbon-nitrogen hydrolase family protein. | glnA: glutamine synthetase, type I. | 0.621 |
| LO55_314 | glnE | LO55_314 | LO55_316 | Carbon-nitrogen hydrolase family protein. | Glutamate-ammonia ligase adenylyltransferase family protein; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds th [...] | 0.556 |
| LO55_314 | nadE | LO55_314 | LO55_4759 | Carbon-nitrogen hydrolase family protein. | NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.627 |
| LO55_314 | pheA | LO55_314 | LO55_47 | Carbon-nitrogen hydrolase family protein. | CM_P2: chorismate mutase. | 0.686 |
| LO55_315 | LO55_314 | LO55_315 | LO55_314 | Hypothetical protein. | Carbon-nitrogen hydrolase family protein. | 0.832 |
| LO55_315 | glnE | LO55_315 | LO55_316 | Hypothetical protein. | Glutamate-ammonia ligase adenylyltransferase family protein; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds th [...] | 0.548 |
| LO55_725 | LO55_1548 | LO55_725 | LO55_1548 | Nitrogen regulatory P-II family protein; Belongs to the P(II) protein family. | Glutamine amidotransferases class-II family protein. | 0.558 |
| LO55_725 | glnA | LO55_725 | LO55_332 | Nitrogen regulatory P-II family protein; Belongs to the P(II) protein family. | glnA: glutamine synthetase, type I. | 0.572 |
| LO55_725 | glnD | LO55_725 | LO55_3586 | Nitrogen regulatory P-II family protein; Belongs to the P(II) protein family. | protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | 0.967 |
| LO55_725 | glnE | LO55_725 | LO55_316 | Nitrogen regulatory P-II family protein; Belongs to the P(II) protein family. | Glutamate-ammonia ligase adenylyltransferase family protein; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds th [...] | 0.533 |