| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPA1930 | RPA1932 | RPA1930 | RPA1932 | Two-component transcriptional regulator, winged helix family. | Sensor histidine kinase. | 0.940 |
| RPA1930 | glnE | RPA1930 | RPA1933 | Two-component transcriptional regulator, winged helix family. | Putative 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 sign [...] | 0.596 |
| RPA1932 | RPA1930 | RPA1932 | RPA1930 | Sensor histidine kinase. | Two-component transcriptional regulator, winged helix family. | 0.940 |
| RPA1932 | glnE | RPA1932 | RPA1933 | Sensor histidine kinase. | Putative 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 sign [...] | 0.870 |
| RPA2456 | glnE | RPA2456 | RPA1933 | Possible bacterioferritin co-migratory protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative 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 sign [...] | 0.654 |
| glnA | glnB | RPA2967 | RPA2966 | Glutamine synthetase I; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the P(II) protein family. | 0.948 |
| glnA | glnD | RPA2967 | RPA0591 | Glutamine synthetase I; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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 fixation and metabolism. | 0.666 |
| glnA | glnE | RPA2967 | RPA1933 | Glutamine synthetase I; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative 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 sign [...] | 0.711 |
| glnA | glnK1 | RPA2967 | RPA0272 | Glutamine synthetase I; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | GlnK, nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the P(II) protein family. | 0.676 |
| glnA | glnK2 | RPA2967 | RPA0274 | Glutamine synthetase I; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | GlnK, nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the P(II) protein family. | 0.763 |
| glnA | gltB | RPA2967 | RPA0891 | Glutamine synthetase I; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Glutamate synthase, large subunit; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.969 |
| glnB | glnA | RPA2966 | RPA2967 | Nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the P(II) protein family. | Glutamine synthetase I; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.948 |
| glnB | glnD | RPA2966 | RPA0591 | Nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; 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 fixation and metabolism. | 0.990 |
| glnB | glnE | RPA2966 | RPA1933 | Nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the P(II) protein family. | Putative 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 sign [...] | 0.627 |
| glnB | gltB | RPA2966 | RPA0891 | Nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the P(II) protein family. | Glutamate synthase, large subunit; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.670 |
| glnD | glnA | RPA0591 | RPA2967 | 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 fixation and metabolism. | Glutamine synthetase I; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.666 |
| glnD | glnB | RPA0591 | RPA2966 | 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 fixation and metabolism. | Nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the P(II) protein family. | 0.990 |
| glnD | glnE | RPA0591 | RPA1933 | 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 fixation and metabolism. | Putative 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 sign [...] | 0.877 |
| glnD | glnK1 | RPA0591 | RPA0272 | 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 fixation and metabolism. | GlnK, nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the P(II) protein family. | 0.721 |
| glnD | glnK2 | RPA0591 | RPA0274 | 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 fixation and metabolism. | GlnK, nitrogen regulatory protein P-II; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the P(II) protein family. | 0.717 |
