| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABO_1140 | glnD | ABO_1140 | ABO_1141 | (N-succinyldiaminopimelate aminotransferase, putative) identified by match to TIGR protein family HMMTIGR01140; putative InterPro: Aminotransferases class-I; High confidence in function and specificity. | 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. | 0.812 |
| ABO_1140 | gltB | ABO_1140 | ABO_2229 | (N-succinyldiaminopimelate aminotransferase, putative) identified by match to TIGR protein family HMMTIGR01140; putative InterPro: Aminotransferases class-I; High confidence in function and specificity. | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | 0.431 |
| ABO_1140 | map | ABO_1140 | ABO_1142 | (N-succinyldiaminopimelate aminotransferase, putative) identified by match to TIGR protein family HMMTIGR01140; putative InterPro: Aminotransferases class-I; High confidence in function and specificity. | 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. | 0.813 |
| ABO_1140 | rpsB | ABO_1140 | ABO_1143 | (N-succinyldiaminopimelate aminotransferase, putative) identified by match to TIGR protein family HMMTIGR01140; putative InterPro: Aminotransferases class-I; High confidence in function and specificity. | 30S ribosomal protein S2; Identified by sequencesimilarity; putative InterPro: Ribosomal protein S2; High confidence in function and specificity; Belongs to the universal ribosomal protein uS2 family. | 0.566 |
| ABO_1140 | tsf | ABO_1140 | ABO_1144 | (N-succinyldiaminopimelate aminotransferase, putative) identified by match to TIGR protein family HMMTIGR01140; putative InterPro: Aminotransferases class-I; High confidence in function and specificity. | Translation elongation factor Ts (EF-Ts); Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family. | 0.566 |
| bamA | glnD | ABO_1151 | ABO_1141 | Outer membrane protein, bacterial surface antigen family protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 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. | 0.716 |
| bamA | map | ABO_1151 | ABO_1142 | Outer membrane protein, bacterial surface antigen family protein; 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. | 0.494 |
| bamA | rpsB | ABO_1151 | ABO_1143 | Outer membrane protein, bacterial surface antigen family protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 30S ribosomal protein S2; Identified by sequencesimilarity; putative InterPro: Ribosomal protein S2; High confidence in function and specificity; Belongs to the universal ribosomal protein uS2 family. | 0.639 |
| bamA | tsf | ABO_1151 | ABO_1144 | Outer membrane protein, bacterial surface antigen family protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | Translation elongation factor Ts (EF-Ts); Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family. | 0.766 |
| glnA | glnD | ABO_2262 | ABO_1141 | (glutamine synthetase type I, glutamate-ammonia ligase) identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00653; High confidence in function and specificity. | 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. | 0.629 |
| glnA | glnE | ABO_2262 | ABO_2302 | (glutamine synthetase type I, glutamate-ammonia ligase) identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00653; High confidence in function and specificity. | 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 [...] | 0.838 |
| glnA | glnK-1 | ABO_2262 | ABO_1123 | (glutamine synthetase type I, glutamate-ammonia ligase) identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00653; High confidence in function and specificity. | Nitrogen regulatory protein P-II; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00543 InterPro: Nitrogen regulatory protein P-II; High confidence in function and specificity; Belongs to the P(II) protein family. | 0.609 |
| glnA | glnK-2 | ABO_2262 | ABO_2530 | (glutamine synthetase type I, glutamate-ammonia ligase) identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00653; High confidence in function and specificity. | Nitrogen regulatory protein P-II; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00543 InterPro: Nitrogen regulatory protein P-II; High confidence in function and specificity; Belongs to the P(II) protein family. | 0.608 |
| glnA | gltB | ABO_2262 | ABO_2229 | (glutamine synthetase type I, glutamate-ammonia ligase) identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00653; High confidence in function and specificity. | Glutamate synthase, large subunit; Identified by sequencesimilarity; putative identified by match to PFAM protein family HMMPF04897 and HMMPF01645 InterPro: Ferredoxin-dependent glutamate synthase; High confidence in function and specificity. | 0.977 |
| glnD | ABO_1140 | ABO_1141 | ABO_1140 | 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. | (N-succinyldiaminopimelate aminotransferase, putative) identified by match to TIGR protein family HMMTIGR01140; putative InterPro: Aminotransferases class-I; High confidence in function and specificity. | 0.812 |
| glnD | bamA | ABO_1141 | ABO_1151 | 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. | Outer membrane protein, bacterial surface antigen family protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.716 |
| glnD | glnA | ABO_1141 | ABO_2262 | 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 type I, glutamate-ammonia ligase) identified by sequence similarity; putative identified by match to TIGRFAM protein family HMMTIGR00653; High confidence in function and specificity. | 0.629 |
| glnD | glnE | ABO_1141 | ABO_2302 | 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. | 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 [...] | 0.834 |
| glnD | glnK-1 | ABO_1141 | ABO_1123 | 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; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00543 InterPro: Nitrogen regulatory protein P-II; High confidence in function and specificity; Belongs to the P(II) protein family. | 0.724 |
| glnD | glnK-2 | ABO_1141 | ABO_2530 | 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; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00543 InterPro: Nitrogen regulatory protein P-II; High confidence in function and specificity; Belongs to the P(II) protein family. | 0.737 |