| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABD30813.1 | ABD30815.1 | SAOUHSC_01742 | SAOUHSC_01744 | GTP pyrophosphokinase; 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. | Conserved hypothetical protein. | 0.549 |
| ABD30813.1 | apt | SAOUHSC_01742 | SAOUHSC_01743 | GTP pyrophosphokinase; 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. | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | 0.530 |
| ABD30813.1 | aspS | SAOUHSC_01742 | SAOUHSC_01737 | GTP pyrophosphokinase; 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. | aspartyl-tRNA synthetase; 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. | 0.637 |
| ABD30813.1 | dtd | SAOUHSC_01742 | SAOUHSC_01741 | GTP pyrophosphokinase; 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. | 0.920 |
| ABD30813.1 | hisS | SAOUHSC_01742 | SAOUHSC_01738 | GTP pyrophosphokinase; 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. | histidyl-tRNA synthetase. | 0.595 |
| ABD30813.1 | lytH | SAOUHSC_01742 | SAOUHSC_01739 | GTP pyrophosphokinase; 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. | Conserved hypothetical protein; Probably involved in cell-wall metabolism (By similarity). May have autolysin activity. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | 0.851 |
| ABD30815.1 | ABD30813.1 | SAOUHSC_01744 | SAOUHSC_01742 | Conserved hypothetical protein. | GTP pyrophosphokinase; 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. | 0.549 |
| ABD30815.1 | apt | SAOUHSC_01744 | SAOUHSC_01743 | Conserved hypothetical protein. | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | 0.855 |
| ABD30815.1 | dtd | SAOUHSC_01744 | SAOUHSC_01741 | Conserved hypothetical 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. | 0.525 |
| ABD30815.1 | hisF | SAOUHSC_01744 | SAOUHSC_03008 | Conserved hypothetical protein. | Imidazole glycerol phosphate synthase subunit hisF, putative; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit; In the C-terminal section; belongs to the PRA-PH family. | 0.590 |
| ABD30815.1 | lytH | SAOUHSC_01744 | SAOUHSC_01739 | Conserved hypothetical protein. | Conserved hypothetical protein; Probably involved in cell-wall metabolism (By similarity). May have autolysin activity. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | 0.525 |
| apt | ABD30813.1 | SAOUHSC_01743 | SAOUHSC_01742 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | GTP pyrophosphokinase; 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. | 0.530 |
| apt | ABD30815.1 | SAOUHSC_01743 | SAOUHSC_01744 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Conserved hypothetical protein. | 0.855 |
| apt | dtd | SAOUHSC_01743 | SAOUHSC_01741 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | 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. | 0.533 |
| apt | hisF | SAOUHSC_01743 | SAOUHSC_03008 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Imidazole glycerol phosphate synthase subunit hisF, putative; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit; In the C-terminal section; belongs to the PRA-PH family. | 0.884 |
| apt | lytH | SAOUHSC_01743 | SAOUHSC_01739 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Conserved hypothetical protein; Probably involved in cell-wall metabolism (By similarity). May have autolysin activity. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | 0.525 |
| aspS | ABD30813.1 | SAOUHSC_01737 | SAOUHSC_01742 | aspartyl-tRNA synthetase; 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 pyrophosphokinase; 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. | 0.637 |
| aspS | dtd | SAOUHSC_01737 | SAOUHSC_01741 | aspartyl-tRNA synthetase; 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. | 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. | 0.630 |
| aspS | hisS | SAOUHSC_01737 | SAOUHSC_01738 | aspartyl-tRNA synthetase; 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. | histidyl-tRNA synthetase. | 0.991 |
| aspS | lytH | SAOUHSC_01737 | SAOUHSC_01739 | aspartyl-tRNA synthetase; 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. | Conserved hypothetical protein; Probably involved in cell-wall metabolism (By similarity). May have autolysin activity. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | 0.527 |