node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MAP_0581c | aspS | MAP_0581c | MAP_1063 | Hypothetical protein; Belongs to the amidase family. | AspS; 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. | 0.643 |
MAP_0581c | atpH | MAP_0581c | MAP_2454c | Hypothetical protein; Belongs to the amidase family. | AtpH; 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 (By similarity). | 0.540 |
MAP_0581c | gatB | MAP_0581c | MAP_3042c | Hypothetical protein; Belongs to the amidase family. | GatB; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.968 |
MAP_0581c | gatC | MAP_0581c | MAP_3046c | Hypothetical protein; Belongs to the amidase family. | GatC; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.902 |
MAP_0581c | gltS | MAP_0581c | MAP_3029c | Hypothetical protein; Belongs to the amidase family. | GltS; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.702 |
amiA2 | amiB2 | MAP_2143 | MAP_2509c | AmiA2; Belongs to the amidase family. | AmiB2; Belongs to the amidase family. | 0.911 |
amiA2 | amiC | MAP_2143 | MAP_2954c | AmiA2; Belongs to the amidase family. | AmiC; Belongs to the amidase family. | 0.925 |
amiA2 | aspS | MAP_2143 | MAP_1063 | AmiA2; Belongs to the amidase family. | AspS; 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. | 0.643 |
amiA2 | atpH | MAP_2143 | MAP_2454c | AmiA2; Belongs to the amidase family. | AtpH; 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 (By similarity). | 0.540 |
amiA2 | gatB | MAP_2143 | MAP_3042c | AmiA2; Belongs to the amidase family. | GatB; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.973 |
amiA2 | gatC | MAP_2143 | MAP_3046c | AmiA2; Belongs to the amidase family. | GatC; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.929 |
amiA2 | gltS | MAP_2143 | MAP_3029c | AmiA2; Belongs to the amidase family. | GltS; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.702 |
amiB2 | amiA2 | MAP_2509c | MAP_2143 | AmiB2; Belongs to the amidase family. | AmiA2; Belongs to the amidase family. | 0.911 |
amiB2 | amiC | MAP_2509c | MAP_2954c | AmiB2; Belongs to the amidase family. | AmiC; Belongs to the amidase family. | 0.929 |
amiB2 | aspS | MAP_2509c | MAP_1063 | AmiB2; Belongs to the amidase family. | AspS; 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. | 0.643 |
amiB2 | atpH | MAP_2509c | MAP_2454c | AmiB2; Belongs to the amidase family. | AtpH; 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 (By similarity). | 0.540 |
amiB2 | gatB | MAP_2509c | MAP_3042c | AmiB2; Belongs to the amidase family. | GatB; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.973 |
amiB2 | gatC | MAP_2509c | MAP_3046c | AmiB2; Belongs to the amidase family. | GatC; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.916 |
amiB2 | gltS | MAP_2509c | MAP_3029c | AmiB2; Belongs to the amidase family. | GltS; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.702 |
amiC | amiA2 | MAP_2954c | MAP_2143 | AmiC; Belongs to the amidase family. | AmiA2; Belongs to the amidase family. | 0.925 |