| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKL38065.1 | AKL38068.1 | AB185_31010 | AB185_31025 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0325 family. | 0.447 |
| AKL38065.1 | dapD | AB185_31010 | AB185_31020 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family. | 0.658 |
| AKL38065.1 | glnD | AB185_31010 | AB185_31015 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 (Probable). | 0.773 |
| AKL38065.1 | map-2 | AB185_31010 | AB185_31005 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 (By similarity). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.678 |
| AKL38068.1 | AKL38065.1 | AB185_31025 | AB185_31010 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0325 family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.447 |
| AKL38068.1 | dapD | AB185_31025 | AB185_31020 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0325 family. | 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family. | 0.577 |
| AKL38068.1 | glnD | AB185_31025 | AB185_31015 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0325 family. | 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 (Probable). | 0.517 |
| AKL38068.1 | map-2 | AB185_31025 | AB185_31005 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0325 family. | 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 (By similarity). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.445 |
| dapD | AKL38065.1 | AB185_31020 | AB185_31010 | 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.658 |
| dapD | AKL38068.1 | AB185_31020 | AB185_31025 | 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0325 family. | 0.577 |
| dapD | glnD | AB185_31020 | AB185_31015 | 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family. | 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 (Probable). | 0.747 |
| dapD | map-2 | AB185_31020 | AB185_31005 | 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family. | 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 (By similarity). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.700 |
| glnD | AKL38065.1 | AB185_31015 | AB185_31010 | 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 (Probable). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.773 |
| glnD | AKL38068.1 | AB185_31015 | AB185_31025 | 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 (Probable). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0325 family. | 0.517 |
| glnD | dapD | AB185_31015 | AB185_31020 | 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 (Probable). | 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family. | 0.747 |
| glnD | map-2 | AB185_31015 | AB185_31005 | 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 (Probable). | 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 (By similarity). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.726 |
| map-2 | AKL38065.1 | AB185_31005 | AB185_31010 | 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 (By similarity). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.678 |
| map-2 | AKL38068.1 | AB185_31005 | AB185_31025 | 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 (By similarity). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0325 family. | 0.445 |
| map-2 | dapD | AB185_31005 | AB185_31020 | 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 (By similarity). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family. | 0.700 |
| map-2 | glnD | AB185_31005 | AB185_31015 | 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 (By similarity). Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 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 (Probable). | 0.726 |