| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CEL27071.1 | glnA_1 | SRM1_00396 | SRM1_00397 | Hypothetical protein. | Glutamine synthetase. | 0.570 |
| glnA_1 | CEL27071.1 | SRM1_00397 | SRM1_00396 | Glutamine synthetase. | Hypothetical protein. | 0.570 |
| glnA_1 | glnD | SRM1_00397 | SRM1_01127 | Glutamine synthetase. | Bifunctional uridylyltransferase/uridylyl-removing enzyme; 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 assimilation and met [...] | 0.535 |
| glnA_1 | glnE | SRM1_00397 | SRM1_00518 | Glutamine synthetase. | 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 transd [...] | 0.714 |
| glnA_1 | glnG | SRM1_00397 | SRM1_00392 | Glutamine synthetase. | Nitrogen regulation protein NR(I); Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. | 0.599 |
| glnA_1 | glnK | SRM1_00397 | SRM1_05645 | Glutamine synthetase. | Nitrogen regulatory protein P-II 2; Belongs to the P(II) protein family. | 0.752 |
| glnA_1 | glnL | SRM1_00397 | SRM1_00393 | Glutamine synthetase. | Nitrogen regulation protein NR(II). | 0.611 |
| glnA_1 | gltB | SRM1_00397 | SRM1_00466 | Glutamine synthetase. | Glutamate synthase [NADPH] large chain precursor. | 0.794 |
| glnA_1 | mrcB | SRM1_00397 | SRM1_04838 | Glutamine synthetase. | Penicillin-binding protein 1B; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | 0.605 |
| glnA_1 | pheA | SRM1_00397 | SRM1_04023 | Glutamine synthetase. | Prephenate dehydratase. | 0.544 |
| glnA_1 | polA | SRM1_00397 | SRM1_00115 | Glutamine synthetase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.510 |
| glnD | glnA_1 | SRM1_01127 | SRM1_00397 | Bifunctional uridylyltransferase/uridylyl-removing enzyme; 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 assimilation and met [...] | Glutamine synthetase. | 0.535 |
| glnD | glnE | SRM1_01127 | SRM1_00518 | Bifunctional uridylyltransferase/uridylyl-removing enzyme; 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 assimilation and met [...] | 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 transd [...] | 0.806 |
| glnD | glnK | SRM1_01127 | SRM1_05645 | Bifunctional uridylyltransferase/uridylyl-removing enzyme; 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 assimilation and met [...] | Nitrogen regulatory protein P-II 2; Belongs to the P(II) protein family. | 0.934 |
| glnD | glnL | SRM1_01127 | SRM1_00393 | Bifunctional uridylyltransferase/uridylyl-removing enzyme; 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 assimilation and met [...] | Nitrogen regulation protein NR(II). | 0.746 |
| glnD | gltB | SRM1_01127 | SRM1_00466 | Bifunctional uridylyltransferase/uridylyl-removing enzyme; 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 assimilation and met [...] | Glutamate synthase [NADPH] large chain precursor. | 0.847 |
| glnE | glnA_1 | SRM1_00518 | SRM1_00397 | 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 transd [...] | Glutamine synthetase. | 0.714 |
| glnE | glnD | SRM1_00518 | SRM1_01127 | 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 transd [...] | Bifunctional uridylyltransferase/uridylyl-removing enzyme; 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 assimilation and met [...] | 0.806 |
| glnE | glnK | SRM1_00518 | SRM1_05645 | 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 transd [...] | Nitrogen regulatory protein P-II 2; Belongs to the P(II) protein family. | 0.560 |
| glnE | gltB | SRM1_00518 | SRM1_00466 | 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 transd [...] | Glutamate synthase [NADPH] large chain precursor. | 0.660 |