node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AEB09465.1 | gatA | Desac_1614 | Desac_0468 | acetyl-CoA carboxylase, biotin carboxylase; 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. | Glutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.924 |
asnS | aspS | Desac_0972 | Desac_0562 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | 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. | 0.400 |
asnS | gatA | Desac_0972 | Desac_0468 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | Glutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.986 |
asnS | gatB | Desac_0972 | Desac_0997 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; 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. | 0.998 |
asnS | gatC | Desac_0972 | Desac_0467 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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. | 0.974 |
asnS | glnS | Desac_0972 | Desac_2578 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; HAMAP: Glutaminyl-tRNA synthetase, bacterial; InterPro IPR022861:IPR020058:IPR020059:IPR004514; KEGG: sfu:Sfum_3516 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; PRIAM: Glutamine--tRNA ligase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; IMG reference gene:2504156139; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-cod [...] | 0.803 |
asnS | gltX | Desac_0972 | Desac_1683 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | glutamyl-tRNA synthetase; 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). | 0.791 |
asnS | guaA | Desac_0972 | Desac_2142 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.582 |
asnS | ileS | Desac_0972 | Desac_2908 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | 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. | 0.866 |
aspS | asnS | Desac_0562 | Desac_0972 | 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. | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | 0.400 |
aspS | gatA | Desac_0562 | Desac_0468 | 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. | Glutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.822 |
aspS | gatB | Desac_0562 | Desac_0997 | 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. | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; 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. | 0.983 |
aspS | gatC | Desac_0562 | Desac_0467 | 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. | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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. | 0.882 |
aspS | glnS | Desac_0562 | Desac_2578 | 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. | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; HAMAP: Glutaminyl-tRNA synthetase, bacterial; InterPro IPR022861:IPR020058:IPR020059:IPR004514; KEGG: sfu:Sfum_3516 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; PRIAM: Glutamine--tRNA ligase; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; IMG reference gene:2504156139; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-cod [...] | 0.652 |
aspS | gltX | Desac_0562 | Desac_1683 | 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. | glutamyl-tRNA synthetase; 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). | 0.569 |
aspS | guaA | Desac_0562 | Desac_2142 | 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 (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.871 |
aspS | ileS | Desac_0562 | Desac_2908 | 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. | 0.705 |
gatA | AEB09465.1 | Desac_0468 | Desac_1614 | Glutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | acetyl-CoA carboxylase, biotin carboxylase; 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. | 0.924 |
gatA | asnS | Desac_0468 | Desac_0972 | Glutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; HAMAP: Asparaginyl-tRNA synthetase, class IIb; InterPro IPR004365:IPR004364:IPR004522; KEGG: drm:Dred_1281 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; IMG reference gene:2504154505; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | 0.986 |
gatA | aspS | Desac_0468 | Desac_0562 | Glutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 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. | 0.822 |