| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EKY26218.1 | EKY26220.1 | HMPREF0216_02257 | HMPREF0216_02259 | GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | Metallo-beta-lactamase domain protein. | 0.824 |
| EKY26218.1 | EKY26221.1 | HMPREF0216_02257 | HMPREF0216_02260 | GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | Coproporphyrinogen dehydrogenase HemZ. | 0.707 |
| EKY26218.1 | aspS | HMPREF0216_02257 | HMPREF0216_02262 | GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.689 |
| EKY26218.1 | dtd | HMPREF0216_02257 | HMPREF0216_02258 | GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.882 |
| EKY26218.1 | hisS | HMPREF0216_02257 | HMPREF0216_02261 | GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | histidine--tRNA ligase. | 0.750 |
| EKY26220.1 | EKY26218.1 | HMPREF0216_02259 | HMPREF0216_02257 | Metallo-beta-lactamase domain protein. | GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.824 |
| EKY26220.1 | EKY26221.1 | HMPREF0216_02259 | HMPREF0216_02260 | Metallo-beta-lactamase domain protein. | Coproporphyrinogen dehydrogenase HemZ. | 0.800 |
| EKY26220.1 | aspS | HMPREF0216_02259 | HMPREF0216_02262 | Metallo-beta-lactamase domain protein. | aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.762 |
| EKY26220.1 | dtd | HMPREF0216_02259 | HMPREF0216_02258 | Metallo-beta-lactamase domain protein. | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.739 |
| EKY26220.1 | hisS | HMPREF0216_02259 | HMPREF0216_02261 | Metallo-beta-lactamase domain protein. | histidine--tRNA ligase. | 0.829 |
| EKY26221.1 | EKY26218.1 | HMPREF0216_02260 | HMPREF0216_02257 | Coproporphyrinogen dehydrogenase HemZ. | GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.707 |
| EKY26221.1 | EKY26220.1 | HMPREF0216_02260 | HMPREF0216_02259 | Coproporphyrinogen dehydrogenase HemZ. | Metallo-beta-lactamase domain protein. | 0.800 |
| EKY26221.1 | aspS | HMPREF0216_02260 | HMPREF0216_02262 | Coproporphyrinogen dehydrogenase HemZ. | aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.786 |
| EKY26221.1 | dtd | HMPREF0216_02260 | HMPREF0216_02258 | Coproporphyrinogen dehydrogenase HemZ. | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.717 |
| EKY26221.1 | hisS | HMPREF0216_02260 | HMPREF0216_02261 | Coproporphyrinogen dehydrogenase HemZ. | histidine--tRNA ligase. | 0.827 |
| EKY28331.1 | hisG | HMPREF0216_00853 | HMPREF0216_02564 | Ribose-phosphate diphosphokinase; KEGG: cpr:CPR_1519 2.5e-164 prs; phosphoribosylpyrophosphate synthetase K00948; Psort location: Cytoplasmic, score: 9.97; Belongs to the ribose-phosphate pyrophosphokinase family. | 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. Short subfamily. | 0.852 |
| EKY28331.1 | hisS | HMPREF0216_00853 | HMPREF0216_02261 | Ribose-phosphate diphosphokinase; KEGG: cpr:CPR_1519 2.5e-164 prs; phosphoribosylpyrophosphate synthetase K00948; Psort location: Cytoplasmic, score: 9.97; Belongs to the ribose-phosphate pyrophosphokinase family. | histidine--tRNA ligase. | 0.800 |
| EKY28331.1 | lysS | HMPREF0216_00853 | HMPREF0216_02539 | Ribose-phosphate diphosphokinase; KEGG: cpr:CPR_1519 2.5e-164 prs; phosphoribosylpyrophosphate synthetase K00948; Psort location: Cytoplasmic, score: 9.97; Belongs to the ribose-phosphate pyrophosphokinase family. | lysine--tRNA ligase; KEGG: cbk:CLL_A0178 6.1e-232 lysS; lysyl-tRNA synthetase K04567; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.638 |
| aspS | EKY26218.1 | HMPREF0216_02262 | HMPREF0216_02257 | aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.689 |
| aspS | EKY26220.1 | HMPREF0216_02262 | HMPREF0216_02259 | aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Metallo-beta-lactamase domain protein. | 0.762 |