| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ppha_0392 | Ppha_0394 | Ppha_0392 | Ppha_0394 | Putative PTS IIA-like nitrogen-regulatory protein PtsN; PFAM: phosphoenolpyruvate-dependent sugar phosphotransferase system EIIA 2; KEGG: plt:Plut_1787 putative PTS IIA-like nitrogen-regulatory protein PtsN. | PFAM: glutaredoxin; glutaredoxin 2; KEGG: cte:CT0237 hypothetical protein. | 0.687 |
| Ppha_0392 | hisS | Ppha_0392 | Ppha_0393 | Putative PTS IIA-like nitrogen-regulatory protein PtsN; PFAM: phosphoenolpyruvate-dependent sugar phosphotransferase system EIIA 2; KEGG: plt:Plut_1787 putative PTS IIA-like nitrogen-regulatory protein PtsN. | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | 0.693 |
| Ppha_0394 | Ppha_0392 | Ppha_0394 | Ppha_0392 | PFAM: glutaredoxin; glutaredoxin 2; KEGG: cte:CT0237 hypothetical protein. | Putative PTS IIA-like nitrogen-regulatory protein PtsN; PFAM: phosphoenolpyruvate-dependent sugar phosphotransferase system EIIA 2; KEGG: plt:Plut_1787 putative PTS IIA-like nitrogen-regulatory protein PtsN. | 0.687 |
| Ppha_0394 | hisS | Ppha_0394 | Ppha_0393 | PFAM: glutaredoxin; glutaredoxin 2; KEGG: cte:CT0237 hypothetical protein. | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | 0.792 |
| aspS | hisS | Ppha_1620 | Ppha_0393 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | 0.844 |
| aspS | metG | Ppha_1620 | Ppha_1197 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.650 |
| aspS | pheT | Ppha_1620 | Ppha_2091 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | KEGG: cph:Cpha266_0925 phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.732 |
| aspS | thrS | Ppha_1620 | Ppha_0176 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | 0.586 |
| aspS | tyrS | Ppha_1620 | Ppha_0861 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. | 0.527 |
| aspS | valS | Ppha_1620 | Ppha_2381 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.819 |
| hisG | hisS | Ppha_0371 | Ppha_0393 | ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Long subfamily. | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | 0.800 |
| hisS | Ppha_0392 | Ppha_0393 | Ppha_0392 | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | Putative PTS IIA-like nitrogen-regulatory protein PtsN; PFAM: phosphoenolpyruvate-dependent sugar phosphotransferase system EIIA 2; KEGG: plt:Plut_1787 putative PTS IIA-like nitrogen-regulatory protein PtsN. | 0.693 |
| hisS | Ppha_0394 | Ppha_0393 | Ppha_0394 | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | PFAM: glutaredoxin; glutaredoxin 2; KEGG: cte:CT0237 hypothetical protein. | 0.792 |
| hisS | aspS | Ppha_0393 | Ppha_1620 | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.844 |
| hisS | hisG | Ppha_0393 | Ppha_0371 | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Long subfamily. | 0.800 |
| hisS | htpG | Ppha_0393 | Ppha_1573 | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.649 |
| hisS | metG | Ppha_0393 | Ppha_1197 | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.664 |
| hisS | pheT | Ppha_0393 | Ppha_2091 | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | KEGG: cph:Cpha266_0925 phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.704 |
| hisS | thrS | Ppha_0393 | Ppha_0176 | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | 0.661 |
| hisS | tyrS | Ppha_0393 | Ppha_0861 | KEGG: cte:CT0236 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. | 0.649 |