node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
XCC1386 | dapD | XCC1386 | XCC1384 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the ArsC family. | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succin; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the transferase hexapeptide repeat family. | 0.709 |
XCC1386 | dapE | XCC1386 | XCC1387 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the ArsC family. | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | 0.799 |
XCC1386 | glnD | XCC1386 | XCC1383 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the ArsC 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 assimilation and metabolism. | 0.665 |
XCC1386 | map | XCC1386 | XCC1382 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the ArsC 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; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.665 |
amtB | glnB | XCC0187 | XCC0186 | Ammonium transporter; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark. | Nitrogen regulatory protein P-II; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the P(II) protein family. | 0.999 |
amtB | glnB-2 | XCC0187 | XCC3872 | Ammonium transporter; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark. | Nitrogen regulatory protein P-II; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the P(II) protein family. | 0.990 |
amtB | glnD | XCC0187 | XCC1383 | Ammonium transporter; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark. | 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 assimilation and metabolism. | 0.900 |
amtB | glnE | XCC0187 | XCC3599 | Ammonium transporter; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark. | 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 [...] | 0.534 |
amtB | gltB | XCC0187 | XCC0032 | Ammonium transporter; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark. | Glutamate synthase, alpha subunit; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark. | 0.859 |
dapD | XCC1386 | XCC1384 | XCC1386 | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succin; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the transferase hexapeptide repeat family. | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the ArsC family. | 0.709 |
dapD | dapE | XCC1384 | XCC1387 | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succin; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the transferase hexapeptide repeat family. | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | 0.830 |
dapD | glnD | XCC1384 | XCC1383 | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succin; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; 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 assimilation and metabolism. | 0.831 |
dapD | map | XCC1384 | XCC1382 | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succin; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; 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; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.849 |
dapE | XCC1386 | XCC1387 | XCC1386 | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the ArsC family. | 0.799 |
dapE | dapD | XCC1387 | XCC1384 | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succin; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the transferase hexapeptide repeat family. | 0.830 |
dapE | glnD | XCC1387 | XCC1383 | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE 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 assimilation and metabolism. | 0.662 |
dapE | map | XCC1387 | XCC1382 | Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily. | 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. | 0.633 |
glnB | amtB | XCC0186 | XCC0187 | Nitrogen regulatory protein P-II; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the P(II) protein family. | Ammonium transporter; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark. | 0.999 |
glnB | glnB-2 | XCC0186 | XCC3872 | Nitrogen regulatory protein P-II; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the P(II) protein family. | Nitrogen regulatory protein P-II; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the P(II) protein family. | 0.901 |
glnB | glnD | XCC0186 | XCC1383 | Nitrogen regulatory protein P-II; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the P(II) protein 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 assimilation and metabolism. | 0.975 |