node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFF29725.1 | SFF65628.1 | SAMN04488120_1022 | SAMN04488120_11819 | Hypothetical protein. | Hypothetical protein. | 0.413 |
SFF29725.1 | dapD | SAMN04488120_1022 | SAMN04488120_1024 | Hypothetical protein. | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family. | 0.775 |
SFF29725.1 | dapE | SAMN04488120_1022 | SAMN04488120_1023 | Hypothetical protein. | Succinyldiaminopimelate 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. | 0.825 |
SFF29725.1 | glnD | SAMN04488120_1022 | SAMN04488120_1025 | Hypothetical protein. | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | 0.544 |
SFF29725.1 | map | SAMN04488120_1022 | SAMN04488120_1026 | Hypothetical protein. | Methionine aminopeptidase, type I; 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. | 0.409 |
SFF65628.1 | SFF29725.1 | SAMN04488120_11819 | SAMN04488120_1022 | Hypothetical protein. | Hypothetical protein. | 0.413 |
dapD | SFF29725.1 | SAMN04488120_1024 | SAMN04488120_1022 | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family. | Hypothetical protein. | 0.775 |
dapD | dapE | SAMN04488120_1024 | SAMN04488120_1023 | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family. | Succinyldiaminopimelate 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. | 0.842 |
dapD | glnD | SAMN04488120_1024 | SAMN04488120_1025 | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family. | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | 0.646 |
dapD | map | SAMN04488120_1024 | SAMN04488120_1026 | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family. | Methionine aminopeptidase, type I; 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. | 0.717 |
dapE | SFF29725.1 | SAMN04488120_1023 | SAMN04488120_1022 | Succinyldiaminopimelate 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. | Hypothetical protein. | 0.825 |
dapE | dapD | SAMN04488120_1023 | SAMN04488120_1024 | Succinyldiaminopimelate 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-succinyltransferase; Belongs to the transferase hexapeptide repeat family. | 0.842 |
dapE | glnD | SAMN04488120_1023 | SAMN04488120_1025 | Succinyldiaminopimelate 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. | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | 0.561 |
dapE | map | SAMN04488120_1023 | SAMN04488120_1026 | Succinyldiaminopimelate 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, type I; 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. | 0.464 |
glnD | SFF29725.1 | SAMN04488120_1025 | SAMN04488120_1022 | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | 0.544 |
glnD | dapD | SAMN04488120_1025 | SAMN04488120_1024 | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family. | 0.646 |
glnD | dapE | SAMN04488120_1025 | SAMN04488120_1023 | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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. | Succinyldiaminopimelate 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. | 0.561 |
glnD | map | SAMN04488120_1025 | SAMN04488120_1026 | UTP--GlnB (protein PII) uridylyltransferase, GlnD; 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, type I; 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. | 0.667 |
map | SFF29725.1 | SAMN04488120_1026 | SAMN04488120_1022 | Methionine aminopeptidase, type I; 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. | 0.409 |
map | dapD | SAMN04488120_1026 | SAMN04488120_1024 | Methionine aminopeptidase, type I; 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. | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family. | 0.717 |