| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CC_1871 | glnE | CC_1871 | CC_2753 | Bacterioferritin comigratory protein; Identified by match to PFAM protein family HMM PF00578. | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | 0.640 |
| CC_1969 | CC_3607 | CC_1969 | CC_3607 | Glutamine synthetase, class I; Identified by match to TIGR protein family HMM TIGR00653. | Glutamate synthase, large subunit; Identified by match to PFAM protein family HMM PF01645. | 0.979 |
| CC_1969 | glnE | CC_1969 | CC_2753 | Glutamine synthetase, class I; Identified by match to TIGR protein family HMM TIGR00653. | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | 0.597 |
| CC_1969 | nadE | CC_1969 | CC_3619 | Glutamine synthetase, class I; Identified by match to TIGR protein family HMM TIGR00653. | NAD(+) synthetase, putative; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.489 |
| CC_2751 | glnE | CC_2751 | CC_2753 | RNA polymerase sigma-70 factor, ECF subfamily; Identified by match to protein family HMM; Belongs to the sigma-70 factor family. ECF subfamily. | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | 0.467 |
| CC_2754 | glnE | CC_2754 | CC_2753 | Hypothetical protein; Identified by Glimmer2; putative. | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | 0.590 |
| CC_3607 | CC_1969 | CC_3607 | CC_1969 | Glutamate synthase, large subunit; Identified by match to PFAM protein family HMM PF01645. | Glutamine synthetase, class I; Identified by match to TIGR protein family HMM TIGR00653. | 0.979 |
| CC_3607 | glnD | CC_3607 | CC_0013 | Glutamate synthase, large subunit; Identified by match to PFAM protein family HMM PF01645. | [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 assimilation and metabolism. | 0.549 |
| CC_3607 | glnE | CC_3607 | CC_2753 | Glutamate synthase, large subunit; Identified by match to PFAM protein family HMM PF01645. | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | 0.485 |
| glnD | CC_3607 | CC_0013 | CC_3607 | [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 assimilation and metabolism. | Glutamate synthase, large subunit; Identified by match to PFAM protein family HMM PF01645. | 0.549 |
| glnD | glnE | CC_0013 | CC_2753 | [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 assimilation and metabolism. | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | 0.919 |
| glnE | CC_1871 | CC_2753 | CC_1871 | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | Bacterioferritin comigratory protein; Identified by match to PFAM protein family HMM PF00578. | 0.640 |
| glnE | CC_1969 | CC_2753 | CC_1969 | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | Glutamine synthetase, class I; Identified by match to TIGR protein family HMM TIGR00653. | 0.597 |
| glnE | CC_2751 | CC_2753 | CC_2751 | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | RNA polymerase sigma-70 factor, ECF subfamily; Identified by match to protein family HMM; Belongs to the sigma-70 factor family. ECF subfamily. | 0.467 |
| glnE | CC_2754 | CC_2753 | CC_2754 | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | Hypothetical protein; Identified by Glimmer2; putative. | 0.590 |
| glnE | CC_3607 | CC_2753 | CC_3607 | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | Glutamate synthase, large subunit; Identified by match to PFAM protein family HMM PF01645. | 0.485 |
| glnE | glnD | CC_2753 | CC_0013 | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | [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 assimilation and metabolism. | 0.919 |
| glnE | kynA | CC_2753 | CC_2886 | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | Conserved hypothetical protein; Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety. | 0.708 |
| glnE | nadE | CC_2753 | CC_3619 | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | NAD(+) synthetase, putative; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.474 |
| glnE | suhB | CC_2753 | CC_3269 | Glutamate-ammonia-ligase adenylyltransferase, putative; 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 sig [...] | Extragenic suppressor protein SuhB; Identified by match to PFAM protein family HMM PF00459; Belongs to the inositol monophosphatase superfamily. | 0.513 |