node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
alaS | aspS | Dtox_2268 | Dtox_2279 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 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. | 0.863 |
alaS | glyQ | Dtox_2268 | Dtox_3048 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | KEGG: pca:Pcar_0598 glycyl-tRNA synthetase subunit alpha; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: glycyl-tRNA synthetase alpha subunit. | 0.667 |
alaS | glyS | Dtox_2268 | Dtox_3047 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | KEGG: sat:SYN_01537 glycyl-tRNA synthetase beta chain; TIGRFAM: glycyl-tRNA synthetase, beta subunit. | 0.659 |
alaS | guaA | Dtox_2268 | Dtox_0724 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.610 |
alaS | hisS | Dtox_2268 | Dtox_2280 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | KEGG: bar:GBAA4633 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | 0.571 |
alaS | hisZ | Dtox_2268 | Dtox_0749 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | histidyl-tRNA synthetase 2; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. | 0.571 |
alaS | ileS | Dtox_2268 | Dtox_1089 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.799 |
alaS | pheT | Dtox_2268 | Dtox_2395 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: bar:GBAA4803 phenylalanyl-tRNA synthetase subunit beta; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.919 |
aspS | alaS | Dtox_2279 | Dtox_2268 | 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. | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.863 |
aspS | glyQ | Dtox_2279 | Dtox_3048 | 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: pca:Pcar_0598 glycyl-tRNA synthetase subunit alpha; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: glycyl-tRNA synthetase alpha subunit. | 0.561 |
aspS | glyS | Dtox_2279 | Dtox_3047 | 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: sat:SYN_01537 glycyl-tRNA synthetase beta chain; TIGRFAM: glycyl-tRNA synthetase, beta subunit. | 0.661 |
aspS | guaA | Dtox_2279 | Dtox_0724 | 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. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.830 |
aspS | hisS | Dtox_2279 | Dtox_2280 | 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: bar:GBAA4633 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. | 0.967 |
aspS | hisZ | Dtox_2279 | Dtox_0749 | 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. | histidyl-tRNA synthetase 2; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. | 0.819 |
aspS | ileS | Dtox_2279 | Dtox_1089 | 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. | isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.716 |
aspS | pheS | Dtox_2279 | Dtox_2396 | 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: bar:GBAA4804 phenylalanyl-tRNA synthetase subunit alpha; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase class IIc; aminoacyl tRNA synthetase class II domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.528 |
aspS | pheT | Dtox_2279 | Dtox_2395 | 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. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: bar:GBAA4803 phenylalanyl-tRNA synthetase subunit beta; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.857 |
atpH | glyQ | Dtox_4168 | Dtox_3048 | ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | KEGG: pca:Pcar_0598 glycyl-tRNA synthetase subunit alpha; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: glycyl-tRNA synthetase alpha subunit. | 0.612 |
atpH | glyS | Dtox_4168 | Dtox_3047 | ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | KEGG: sat:SYN_01537 glycyl-tRNA synthetase beta chain; TIGRFAM: glycyl-tRNA synthetase, beta subunit. | 0.432 |
atpH | pheT | Dtox_4168 | Dtox_2395 | ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: bar:GBAA4803 phenylalanyl-tRNA synthetase subunit beta; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.535 |