| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Meso_1401 | Meso_1403 | Meso_1401 | Meso_1403 | PFAM: Lysine exporter protein (LYSE/YGGA); KEGG: mlo:mlr3188 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. | 0.590 |
| Meso_1401 | Meso_1404 | Meso_1401 | Meso_1404 | PFAM: Lysine exporter protein (LYSE/YGGA); KEGG: mlo:mlr3188 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. | 0.536 |
| Meso_1401 | coaD | Meso_1401 | Meso_1402 | PFAM: Lysine exporter protein (LYSE/YGGA); KEGG: mlo:mlr3188 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. | 0.645 |
| Meso_1401 | gyrA | Meso_1401 | Meso_1400 | PFAM: Lysine exporter protein (LYSE/YGGA); KEGG: mlo:mlr3188 hypothetical protein. | DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | 0.462 |
| Meso_1401 | queA | Meso_1401 | Meso_1405 | PFAM: Lysine exporter protein (LYSE/YGGA); KEGG: mlo:mlr3188 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). | 0.404 |
| Meso_1401 | tgt | Meso_1401 | Meso_1406 | PFAM: Lysine exporter protein (LYSE/YGGA); KEGG: mlo:mlr3188 hypothetical protein. | tRNA-guanine transglycosylase; 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 the [...] | 0.404 |
| Meso_1403 | Meso_1401 | Meso_1403 | Meso_1401 | 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. | PFAM: Lysine exporter protein (LYSE/YGGA); KEGG: mlo:mlr3188 hypothetical protein. | 0.590 |
| Meso_1403 | Meso_1404 | Meso_1403 | Meso_1404 | 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. | 0.793 |
| Meso_1403 | coaD | Meso_1403 | Meso_1402 | 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. | 0.813 |
| Meso_1403 | queA | Meso_1403 | Meso_1405 | 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). | 0.571 |
| Meso_1403 | tgt | Meso_1403 | Meso_1406 | 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. | tRNA-guanine transglycosylase; 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 the [...] | 0.573 |
| Meso_1404 | Meso_1401 | Meso_1404 | Meso_1401 | 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. | PFAM: Lysine exporter protein (LYSE/YGGA); KEGG: mlo:mlr3188 hypothetical protein. | 0.536 |
| Meso_1404 | Meso_1403 | Meso_1404 | Meso_1403 | 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. | 0.793 |
| Meso_1404 | coaD | Meso_1404 | Meso_1402 | 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. | 0.762 |
| Meso_1404 | queA | Meso_1404 | Meso_1405 | 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). | 0.679 |
| Meso_1404 | tgt | Meso_1404 | Meso_1406 | 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. | tRNA-guanine transglycosylase; 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 the [...] | 0.681 |
| coaD | Meso_1401 | Meso_1402 | Meso_1401 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | PFAM: Lysine exporter protein (LYSE/YGGA); KEGG: mlo:mlr3188 hypothetical protein. | 0.645 |
| coaD | Meso_1403 | Meso_1402 | Meso_1403 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD 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. | 0.813 |
| coaD | Meso_1404 | Meso_1402 | Meso_1404 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD 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. | 0.762 |
| coaD | gyrA | Meso_1402 | Meso_1400 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | 0.518 |
