| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| atpE | bfmBAB | BVIR_2683 | BVIR_1927 | ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 2-oxoisovalerate dehydrogenase subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | 0.559 |
| atpE | pepQ | BVIR_2683 | BVIR_425 | ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Xaa-Pro dipeptidase. | 0.494 |
| bfmBAB | atpE | BVIR_1927 | BVIR_2683 | 2-oxoisovalerate dehydrogenase subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.559 |
| bfmBAB | pepQ | BVIR_1927 | BVIR_425 | 2-oxoisovalerate dehydrogenase subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Xaa-Pro dipeptidase. | 0.501 |
| bfmBAB | pheT | BVIR_1927 | BVIR_3095 | 2-oxoisovalerate dehydrogenase subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Phenylalanine--tRNA ligase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.493 |
| bfmBAB | porB | BVIR_1927 | BVIR_2292 | 2-oxoisovalerate dehydrogenase subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | Pyruvate-flavodoxin oxidoreductase. | 0.953 |
| bfmBAB | tme | BVIR_1927 | BVIR_2823 | 2-oxoisovalerate dehydrogenase subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. | NADP-dependent malic enzyme. | 0.995 |
| csgA | panD_1 | BVIR_424 | BVIR_423 | C-factor; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | Aspartate 1-decarboxylase precursor; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | 0.663 |
| csgA | pepQ | BVIR_424 | BVIR_425 | C-factor; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | Xaa-Pro dipeptidase. | 0.762 |
| efp_1 | map | BVIR_2980 | BVIR_442 | Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | 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. | 0.794 |
| efp_1 | pepQ | BVIR_2980 | BVIR_425 | Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | Xaa-Pro dipeptidase. | 0.494 |
| efp_1 | pheT | BVIR_2980 | BVIR_3095 | Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | Phenylalanine--tRNA ligase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.604 |
| map | efp_1 | BVIR_442 | BVIR_2980 | 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. | Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | 0.794 |
| map | pepN | BVIR_442 | BVIR_2328 | 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. | Aminopeptidase N. | 0.443 |
| map | pepQ | BVIR_442 | BVIR_425 | 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. | Xaa-Pro dipeptidase. | 0.612 |
| map | pheT | BVIR_442 | BVIR_3095 | 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. | Phenylalanine--tRNA ligase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.647 |
| panD_1 | csgA | BVIR_423 | BVIR_424 | Aspartate 1-decarboxylase precursor; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | C-factor; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.663 |
| panD_1 | pepQ | BVIR_423 | BVIR_425 | Aspartate 1-decarboxylase precursor; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | Xaa-Pro dipeptidase. | 0.696 |
| pepN | map | BVIR_2328 | BVIR_442 | Aminopeptidase N. | 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. | 0.443 |
| pepN | pepQ | BVIR_2328 | BVIR_425 | Aminopeptidase N. | Xaa-Pro dipeptidase. | 0.523 |