| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RMCT_4266 | RMCT_4269 | RMCT_4266 | RMCT_4269 | Phenylacetic acid degradation-like protein. | Putative uncharacterized protein. | 0.522 |
| RMCT_4266 | RMCT_4270 | RMCT_4266 | RMCT_4270 | Phenylacetic acid degradation-like protein. | Membrane protein. | 0.563 |
| RMCT_4266 | cobQ | RMCT_4266 | RMCT_4268 | Phenylacetic acid degradation-like protein. | Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | 0.570 |
| RMCT_4266 | map-2 | RMCT_4266 | RMCT_4267 | Phenylacetic acid degradation-like 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. | 0.578 |
| RMCT_4269 | RMCT_4266 | RMCT_4269 | RMCT_4266 | Putative uncharacterized protein. | Phenylacetic acid degradation-like protein. | 0.522 |
| RMCT_4269 | RMCT_4270 | RMCT_4269 | RMCT_4270 | Putative uncharacterized protein. | Membrane protein. | 0.615 |
| RMCT_4269 | cobQ | RMCT_4269 | RMCT_4268 | Putative uncharacterized protein. | Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | 0.771 |
| RMCT_4269 | map-2 | RMCT_4269 | RMCT_4267 | Putative uncharacterized 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. | 0.701 |
| RMCT_4270 | RMCT_4266 | RMCT_4270 | RMCT_4266 | Membrane protein. | Phenylacetic acid degradation-like protein. | 0.563 |
| RMCT_4270 | RMCT_4269 | RMCT_4270 | RMCT_4269 | Membrane protein. | Putative uncharacterized protein. | 0.615 |
| RMCT_4270 | cobQ | RMCT_4270 | RMCT_4268 | Membrane protein. | Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | 0.655 |
| RMCT_4270 | map-2 | RMCT_4270 | RMCT_4267 | Membrane 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. | 0.622 |
| cobQ | RMCT_4266 | RMCT_4268 | RMCT_4266 | Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | Phenylacetic acid degradation-like protein. | 0.570 |
| cobQ | RMCT_4269 | RMCT_4268 | RMCT_4269 | Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | Putative uncharacterized protein. | 0.771 |
| cobQ | RMCT_4270 | RMCT_4268 | RMCT_4270 | Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | Membrane protein. | 0.655 |
| cobQ | map-2 | RMCT_4268 | RMCT_4267 | Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ 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. | 0.821 |
| map-2 | RMCT_4266 | RMCT_4267 | RMCT_4266 | 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. | Phenylacetic acid degradation-like protein. | 0.578 |
| map-2 | RMCT_4269 | RMCT_4267 | RMCT_4269 | 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. | Putative uncharacterized protein. | 0.701 |
| map-2 | RMCT_4270 | RMCT_4267 | RMCT_4270 | 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. | Membrane protein. | 0.622 |
| map-2 | cobQ | RMCT_4267 | RMCT_4268 | 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. | Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. | 0.821 |