| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SDW66182.1 | SDW68829.1 | SAMN05443545_102384 | SAMN05443545_102440 | Glutamate synthase (NADPH) large subunit. | Succinyldiaminopimelate aminotransferase apoenzyme. | 0.950 |
| SDW66182.1 | SDW98723.1 | SAMN05443545_102384 | SAMN05443545_103339 | Glutamate synthase (NADPH) large subunit. | Nitrogen regulatory protein P-II family; Belongs to the P(II) protein family. | 0.580 |
| SDW66182.1 | SDW98808.1 | SAMN05443545_102384 | SAMN05443545_103341 | Glutamate synthase (NADPH) large subunit. | Nitrogen regulatory protein P-II family. | 0.580 |
| SDW66182.1 | SDX64343.1 | SAMN05443545_102384 | SAMN05443545_106255 | Glutamate synthase (NADPH) large subunit. | Glutamate synthase (NADPH/NADH) large chain. | 0.999 |
| SDW66182.1 | SDX92637.1 | SAMN05443545_102384 | SAMN05443545_10898 | Glutamate synthase (NADPH) large subunit. | Two-component system, NtrC family, nitrogen regulation sensor histidine kinase GlnL. | 0.492 |
| SDW66182.1 | glnD | SAMN05443545_102384 | SAMN05443545_102439 | Glutamate synthase (NADPH) large subunit. | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | 0.596 |
| SDW66182.1 | glnE | SAMN05443545_102384 | SAMN05443545_10456 | Glutamate synthase (NADPH) large subunit. | 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 [...] | 0.573 |
| SDW68829.1 | SDW66182.1 | SAMN05443545_102440 | SAMN05443545_102384 | Succinyldiaminopimelate aminotransferase apoenzyme. | Glutamate synthase (NADPH) large subunit. | 0.950 |
| SDW68829.1 | SDW68877.1 | SAMN05443545_102440 | SAMN05443545_102441 | Succinyldiaminopimelate aminotransferase apoenzyme. | Transcriptional regulator, Spx/MgsR family; Belongs to the ArsC family. | 0.852 |
| SDW68829.1 | SDX64343.1 | SAMN05443545_102440 | SAMN05443545_106255 | Succinyldiaminopimelate aminotransferase apoenzyme. | Glutamate synthase (NADPH/NADH) large chain. | 0.950 |
| SDW68829.1 | glnD | SAMN05443545_102440 | SAMN05443545_102439 | Succinyldiaminopimelate aminotransferase apoenzyme. | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | 0.634 |
| SDW68829.1 | map | SAMN05443545_102440 | SAMN05443545_102438 | Succinyldiaminopimelate aminotransferase apoenzyme. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.652 |
| SDW68877.1 | SDW68829.1 | SAMN05443545_102441 | SAMN05443545_102440 | Transcriptional regulator, Spx/MgsR family; Belongs to the ArsC family. | Succinyldiaminopimelate aminotransferase apoenzyme. | 0.852 |
| SDW68877.1 | glnD | SAMN05443545_102441 | SAMN05443545_102439 | Transcriptional regulator, Spx/MgsR family; Belongs to the ArsC family. | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | 0.634 |
| SDW68877.1 | map | SAMN05443545_102441 | SAMN05443545_102438 | Transcriptional regulator, Spx/MgsR family; Belongs to the ArsC family. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.630 |
| SDW98723.1 | SDW66182.1 | SAMN05443545_103339 | SAMN05443545_102384 | Nitrogen regulatory protein P-II family; Belongs to the P(II) protein family. | Glutamate synthase (NADPH) large subunit. | 0.580 |
| SDW98723.1 | SDX64343.1 | SAMN05443545_103339 | SAMN05443545_106255 | Nitrogen regulatory protein P-II family; Belongs to the P(II) protein family. | Glutamate synthase (NADPH/NADH) large chain. | 0.580 |
| SDW98723.1 | SDX92637.1 | SAMN05443545_103339 | SAMN05443545_10898 | Nitrogen regulatory protein P-II family; Belongs to the P(II) protein family. | Two-component system, NtrC family, nitrogen regulation sensor histidine kinase GlnL. | 0.963 |
| SDW98723.1 | glnD | SAMN05443545_103339 | SAMN05443545_102439 | Nitrogen regulatory protein P-II family; Belongs to the P(II) protein family. | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | 0.907 |
| SDW98723.1 | glnE | SAMN05443545_103339 | SAMN05443545_10456 | Nitrogen regulatory protein P-II family; 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 transd [...] | 0.423 |