| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSEEN4213 | bamA | PSEEN4213 | PSEEN4212 | Putative membrane-associated Zn-dependent proteases 1; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Putative outer membrane protein, bacterial surface antigen family; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.936 |
| PSEEN4213 | glnD | PSEEN4213 | PSEEN4222 | Putative membrane-associated Zn-dependent proteases 1; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 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 [...] | 0.486 |
| PSEEN4213 | gltB | PSEEN4213 | PSEEN0337 | Putative membrane-associated Zn-dependent proteases 1; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Glutamate synthase [NADPH] large chain precursor (GOGAT); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.641 |
| PSEEN4213 | map | PSEEN4213 | PSEEN4221 | Putative membrane-associated Zn-dependent proteases 1; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Methionine aminopeptidase; 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. | 0.492 |
| PSEEN4223 | PSEEN4224 | PSEEN4223 | PSEEN4224 | Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Hypothetical protein; No homology to any previously reported sequences. | 0.602 |
| PSEEN4223 | glnD | PSEEN4223 | PSEEN4222 | Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 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 [...] | 0.747 |
| PSEEN4223 | gltB | PSEEN4223 | PSEEN0337 | Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Glutamate synthase [NADPH] large chain precursor (GOGAT); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.538 |
| PSEEN4223 | map | PSEEN4223 | PSEEN4221 | Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Methionine aminopeptidase; 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. | 0.703 |
| PSEEN4224 | PSEEN4223 | PSEEN4224 | PSEEN4223 | Hypothetical protein; No homology to any previously reported sequences. | Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.602 |
| PSEEN4224 | glnD | PSEEN4224 | PSEEN4222 | Hypothetical protein; No homology to any previously reported sequences. | 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 [...] | 0.546 |
| PSEEN4224 | map | PSEEN4224 | PSEEN4221 | Hypothetical protein; No homology to any previously reported sequences. | Methionine aminopeptidase; 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. | 0.487 |
| bamA | PSEEN4213 | PSEEN4212 | PSEEN4213 | Putative outer membrane protein, bacterial surface antigen family; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | Putative membrane-associated Zn-dependent proteases 1; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.936 |
| bamA | glnD | PSEEN4212 | PSEEN4222 | Putative outer membrane protein, bacterial surface antigen family; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 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 [...] | 0.692 |
| bamA | map | PSEEN4212 | PSEEN4221 | Putative outer membrane protein, bacterial surface antigen family; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | Methionine aminopeptidase; 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. | 0.439 |
| glnD | PSEEN4213 | PSEEN4222 | PSEEN4213 | 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 [...] | Putative membrane-associated Zn-dependent proteases 1; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.486 |
| glnD | PSEEN4223 | PSEEN4222 | PSEEN4223 | 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 [...] | Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.747 |
| glnD | PSEEN4224 | PSEEN4222 | PSEEN4224 | 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 [...] | Hypothetical protein; No homology to any previously reported sequences. | 0.546 |
| glnD | bamA | PSEEN4222 | PSEEN4212 | 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 [...] | Putative outer membrane protein, bacterial surface antigen family; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.692 |
| glnD | glnE | PSEEN4222 | PSEEN5144 | 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 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 transducti [...] | 0.792 |
| glnD | glnK | PSEEN4222 | PSEEN5376 | 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; Function of homologous gene experimentally demonstrated in an other organism; regulator; Belongs to the P(II) protein family. | 0.876 |