| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Lcin_2944 | Lcin_2945 | Lcin_2944 | Lcin_2945 | Hypothetical protein. | Pyridine nucleotide-disulfide oxidoreductase. | 0.782 |
| Lcin_2944 | eptA_1 | Lcin_2944 | Lcin_2946 | Hypothetical protein. | Sulfatase. | 0.508 |
| Lcin_2944 | glnD | Lcin_2944 | Lcin_2942 | Hypothetical protein. | PII uridylyl-transferase; 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. | 0.429 |
| Lcin_2944 | map_2 | Lcin_2944 | Lcin_2943 | Hypothetical protein. | 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. | 0.454 |
| Lcin_2945 | Lcin_2944 | Lcin_2945 | Lcin_2944 | Pyridine nucleotide-disulfide oxidoreductase. | Hypothetical protein. | 0.782 |
| Lcin_2945 | eptA_1 | Lcin_2945 | Lcin_2946 | Pyridine nucleotide-disulfide oxidoreductase. | Sulfatase. | 0.514 |
| Lcin_2945 | glnD | Lcin_2945 | Lcin_2942 | Pyridine nucleotide-disulfide oxidoreductase. | PII uridylyl-transferase; 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. | 0.424 |
| Lcin_2945 | map_2 | Lcin_2945 | Lcin_2943 | Pyridine nucleotide-disulfide oxidoreductase. | 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. | 0.497 |
| eptA_1 | Lcin_2944 | Lcin_2946 | Lcin_2944 | Sulfatase. | Hypothetical protein. | 0.508 |
| eptA_1 | Lcin_2945 | Lcin_2946 | Lcin_2945 | Sulfatase. | Pyridine nucleotide-disulfide oxidoreductase. | 0.514 |
| glnD | Lcin_2944 | Lcin_2942 | Lcin_2944 | PII uridylyl-transferase; 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. | Hypothetical protein. | 0.429 |
| glnD | Lcin_2945 | Lcin_2942 | Lcin_2945 | PII uridylyl-transferase; 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. | Pyridine nucleotide-disulfide oxidoreductase. | 0.424 |
| glnD | map_2 | Lcin_2942 | Lcin_2943 | PII uridylyl-transferase; 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. | 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. | 0.805 |
| map_2 | Lcin_2944 | Lcin_2943 | Lcin_2944 | 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. | Hypothetical protein. | 0.454 |
| map_2 | Lcin_2945 | Lcin_2943 | Lcin_2945 | 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. | Pyridine nucleotide-disulfide oxidoreductase. | 0.497 |
| map_2 | glnD | Lcin_2943 | Lcin_2942 | 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. | PII uridylyl-transferase; 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. | 0.805 |