| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Lfee_2740 | Lfee_2742 | Lfee_2740 | Lfee_2742 | Queuine/archaeosine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribo [...] | Cytochrome c5. | 0.688 |
| Lfee_2740 | dsbB | Lfee_2740 | Lfee_2741 | Queuine/archaeosine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribo [...] | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.688 |
| Lfee_2740 | ppiB | Lfee_2740 | Lfee_2739 | Queuine/archaeosine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribo [...] | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.823 |
| Lfee_2742 | Lfee_2740 | Lfee_2742 | Lfee_2740 | Cytochrome c5. | Queuine/archaeosine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribo [...] | 0.688 |
| Lfee_2742 | Lfee_2743 | Lfee_2742 | Lfee_2743 | Cytochrome c5. | Nitropropane dioxygenase/trans-enoyl-CoA reductase. | 0.527 |
| Lfee_2742 | dsbB | Lfee_2742 | Lfee_2741 | Cytochrome c5. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.860 |
| Lfee_2742 | ppiB | Lfee_2742 | Lfee_2739 | Cytochrome c5. | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.671 |
| Lfee_2742 | sspH2 | Lfee_2742 | Lfee_2744 | Cytochrome c5. | Leucine rich repeat protein. | 0.527 |
| Lfee_2743 | Lfee_2742 | Lfee_2743 | Lfee_2742 | Nitropropane dioxygenase/trans-enoyl-CoA reductase. | Cytochrome c5. | 0.527 |
| Lfee_2743 | dsbB | Lfee_2743 | Lfee_2741 | Nitropropane dioxygenase/trans-enoyl-CoA reductase. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.527 |
| Lfee_2743 | sspH2 | Lfee_2743 | Lfee_2744 | Nitropropane dioxygenase/trans-enoyl-CoA reductase. | Leucine rich repeat protein. | 0.773 |
| ccmG | dsbA | Lfee_0366 | Lfee_1700 | Cytochrome C biogenesis protein. | Thiol:disulfide interchange protein precursor DsbA. | 0.488 |
| ccmG | dsbB | Lfee_0366 | Lfee_2741 | Cytochrome C biogenesis protein. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.586 |
| ccmG | dsbD | Lfee_0366 | Lfee_0045 | Cytochrome C biogenesis protein. | Thiol:disulfide interchange protein DsbD; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.936 |
| ccmG | ppiB | Lfee_0366 | Lfee_2739 | Cytochrome C biogenesis protein. | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.419 |
| dsbA | ccmG | Lfee_1700 | Lfee_0366 | Thiol:disulfide interchange protein precursor DsbA. | Cytochrome C biogenesis protein. | 0.488 |
| dsbA | dsbB | Lfee_1700 | Lfee_2741 | Thiol:disulfide interchange protein precursor DsbA. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.982 |
| dsbA | dsbD | Lfee_1700 | Lfee_0045 | Thiol:disulfide interchange protein precursor DsbA. | Thiol:disulfide interchange protein DsbD; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.813 |
| dsbA | recG | Lfee_1700 | Lfee_2157 | Thiol:disulfide interchange protein precursor DsbA. | ATP-dependent DNA helicase RecG; Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y- DNA); Belongs to the helicase family. RecG subfamily. | 0.462 |
| dsbB | Lfee_2740 | Lfee_2741 | Lfee_2740 | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Queuine/archaeosine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribo [...] | 0.688 |