node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Sde_0011 | glyQ | Sde_0011 | Sde_0013 | Phospholipid/glycerol acyltransferase. | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | 0.638 |
Sde_0011 | glyS | Sde_0011 | Sde_0012 | Phospholipid/glycerol acyltransferase. | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | 0.638 |
Sde_0812 | atpH | Sde_0812 | Sde_3969 | Biotin carboxyl carrier protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | 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. | 0.551 |
Sde_0812 | glyQ | Sde_0812 | Sde_0013 | Biotin carboxyl carrier protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | 0.599 |
Sde_0812 | guaA | Sde_0812 | Sde_1460 | Biotin carboxyl carrier protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.507 |
alaS | glyQ | Sde_1299 | Sde_0013 | 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. | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | 0.742 |
alaS | glyS | Sde_1299 | Sde_0012 | 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. | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | 0.681 |
alaS | guaA | Sde_1299 | Sde_1460 | 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 (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.668 |
alaS | hisS | Sde_1299 | Sde_1435 | 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. | 0.736 |
alaS | ileS | Sde_1299 | Sde_2566 | 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. | 0.817 |
alaS | metG | Sde_1299 | Sde_2398 | 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. | 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. | 0.872 |
alaS | pheS | Sde_1299 | Sde_1581 | 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. | phenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.455 |
atpH | Sde_0812 | Sde_3969 | Sde_0812 | 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. | Biotin carboxyl carrier protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | 0.551 |
atpH | glyQ | Sde_3969 | Sde_0013 | 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. | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | 0.642 |
glyQ | Sde_0011 | Sde_0013 | Sde_0011 | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | Phospholipid/glycerol acyltransferase. | 0.638 |
glyQ | Sde_0812 | Sde_0013 | Sde_0812 | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | Biotin carboxyl carrier protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | 0.599 |
glyQ | alaS | Sde_0013 | Sde_1299 | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | 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. | 0.742 |
glyQ | atpH | Sde_0013 | Sde_3969 | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | 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. | 0.642 |
glyQ | glyS | Sde_0013 | Sde_0012 | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | 0.999 |
glyQ | guaA | Sde_0013 | Sde_1460 | glycyl-tRNA synthetase is a tetramer of two alpha and two beta chains. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.703 |