| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKT37117.1 | AKT43354.1 | CMC5_012470 | CMC5_075860 | Ammonia channel protein. | Uncharacterized protein; Belongs to the P(II) protein family. | 0.999 |
| AKT37117.1 | AKT43632.1 | CMC5_012470 | CMC5_078670 | Ammonia channel protein. | Glutamate synthase. | 0.828 |
| AKT37117.1 | glnA | CMC5_012470 | CMC5_075850 | Ammonia channel protein. | Glutamine synthetase. | 0.864 |
| AKT37117.1 | glnD | CMC5_012470 | CMC5_048360 | Ammonia channel protein. | (protein-PII) 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. | 0.475 |
| AKT39006.1 | AKT43354.1 | CMC5_031520 | CMC5_075860 | Glutamate--ammonia-ligase adenylyltransferase; 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 the signal trans [...] | Uncharacterized protein; Belongs to the P(II) protein family. | 0.615 |
| AKT39006.1 | AKT43632.1 | CMC5_031520 | CMC5_078670 | Glutamate--ammonia-ligase adenylyltransferase; 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 the signal trans [...] | Glutamate synthase. | 0.597 |
| AKT39006.1 | glnA | CMC5_031520 | CMC5_075850 | Glutamate--ammonia-ligase adenylyltransferase; 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 the signal trans [...] | Glutamine synthetase. | 0.827 |
| AKT39006.1 | glnD | CMC5_031520 | CMC5_048360 | Glutamate--ammonia-ligase adenylyltransferase; 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 the signal trans [...] | (protein-PII) 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. | 0.810 |
| AKT39814.1 | glnD | CMC5_039650 | CMC5_048360 | Membrane protein. | (protein-PII) 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. | 0.499 |
| AKT40679.1 | cheR-2 | CMC5_048350 | CMC5_048370 | Uncharacterized protein. | Chemotaxis protein methyltransferase. | 0.773 |
| AKT40679.1 | glnD | CMC5_048350 | CMC5_048360 | Uncharacterized protein. | (protein-PII) 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. | 0.773 |
| AKT40875.1 | AKT43878.1 | CMC5_050320 | CMC5_081150 | Uncharacterized protein. | Surface antigen. | 0.571 |
| AKT40875.1 | glnD | CMC5_050320 | CMC5_048360 | Uncharacterized protein. | (protein-PII) 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. | 0.488 |
| AKT43354.1 | AKT37117.1 | CMC5_075860 | CMC5_012470 | Uncharacterized protein; Belongs to the P(II) protein family. | Ammonia channel protein. | 0.999 |
| AKT43354.1 | AKT39006.1 | CMC5_075860 | CMC5_031520 | Uncharacterized protein; Belongs to the P(II) protein family. | Glutamate--ammonia-ligase adenylyltransferase; 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 the signal trans [...] | 0.615 |
| AKT43354.1 | AKT43632.1 | CMC5_075860 | CMC5_078670 | Uncharacterized protein; Belongs to the P(II) protein family. | Glutamate synthase. | 0.696 |
| AKT43354.1 | glnA | CMC5_075860 | CMC5_075850 | Uncharacterized protein; Belongs to the P(II) protein family. | Glutamine synthetase. | 0.891 |
| AKT43354.1 | glnD | CMC5_075860 | CMC5_048360 | Uncharacterized protein; Belongs to the P(II) protein family. | (protein-PII) 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. | 0.992 |
| AKT43632.1 | AKT37117.1 | CMC5_078670 | CMC5_012470 | Glutamate synthase. | Ammonia channel protein. | 0.828 |
| AKT43632.1 | AKT39006.1 | CMC5_078670 | CMC5_031520 | Glutamate synthase. | Glutamate--ammonia-ligase adenylyltransferase; 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 the signal trans [...] | 0.597 |