| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPD_0170 | queA | RPD_0170 | RPD_2602 | 4Fe-4S ferredoxin, iron-sulfur binding. | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.847 |
| RPD_0170 | queF | RPD_0170 | RPD_2817 | 4Fe-4S ferredoxin, iron-sulfur binding. | GTP cyclohydrolase I; Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily. | 0.630 |
| RPD_0170 | tgt | RPD_0170 | RPD_2603 | 4Fe-4S ferredoxin, iron-sulfur binding. | Queuine 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 ribose to form t [...] | 0.539 |
| RPD_2599 | RPD_2600 | RPD_2599 | RPD_2600 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Conserved hypothetical protein. | 0.862 |
| RPD_2599 | RPD_2601 | RPD_2599 | RPD_2601 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | 0.869 |
| RPD_2599 | coaD | RPD_2599 | RPD_2598 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | 0.719 |
| RPD_2599 | polA | RPD_2599 | RPD_0956 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.466 |
| RPD_2599 | queA | RPD_2599 | RPD_2602 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.563 |
| RPD_2599 | tgt | RPD_2599 | RPD_2603 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Queuine 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 ribose to form t [...] | 0.538 |
| RPD_2600 | RPD_2599 | RPD_2600 | RPD_2599 | Conserved hypothetical protein. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | 0.862 |
| RPD_2600 | RPD_2601 | RPD_2600 | RPD_2601 | Conserved hypothetical protein. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | 0.868 |
| RPD_2600 | coaD | RPD_2600 | RPD_2598 | Conserved hypothetical protein. | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | 0.754 |
| RPD_2600 | queA | RPD_2600 | RPD_2602 | Conserved hypothetical protein. | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.579 |
| RPD_2600 | tgt | RPD_2600 | RPD_2603 | Conserved hypothetical protein. | Queuine 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 ribose to form t [...] | 0.530 |
| RPD_2601 | RPD_2599 | RPD_2601 | RPD_2599 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | 0.869 |
| RPD_2601 | RPD_2600 | RPD_2601 | RPD_2600 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Conserved hypothetical protein. | 0.868 |
| RPD_2601 | coaD | RPD_2601 | RPD_2598 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | 0.711 |
| RPD_2601 | polA | RPD_2601 | RPD_0956 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.466 |
| RPD_2601 | queA | RPD_2601 | RPD_2602 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | 0.568 |
| RPD_2601 | tgt | RPD_2601 | RPD_2603 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. | Queuine 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 ribose to form t [...] | 0.544 |