| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKH37697.1 | aspS | AAW31_07565 | AAW31_02380 | Amidase; Catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family. | 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. | 0.631 |
| AKH37697.1 | gatB | AAW31_07565 | AAW31_03035 | Amidase; Catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family. | glutamyl-tRNA amidotransferase; 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. | 0.989 |
| AKH37697.1 | gatC | AAW31_07565 | AAW31_03045 | Amidase; Catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family. | glutamyl-tRNA amidotransferase; 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. | 0.969 |
| AKH37697.1 | glnS | AAW31_07565 | AAW31_15960 | Amidase; Catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family. | glutaminyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.436 |
| AKH38197.1 | aspS | AAW31_10975 | AAW31_02380 | Catalyzes the hydrolysis of allophanate; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.565 |
| AKH38197.1 | gatB | AAW31_10975 | AAW31_03035 | Catalyzes the hydrolysis of allophanate; Derived by automated computational analysis using gene prediction method: Protein Homology. | glutamyl-tRNA amidotransferase; 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. | 0.964 |
| AKH38197.1 | gatC | AAW31_10975 | AAW31_03045 | Catalyzes the hydrolysis of allophanate; Derived by automated computational analysis using gene prediction method: Protein Homology. | glutamyl-tRNA amidotransferase; 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. | 0.956 |
| AKH38197.1 | glnS | AAW31_10975 | AAW31_15960 | Catalyzes the hydrolysis of allophanate; Derived by automated computational analysis using gene prediction method: Protein Homology. | glutaminyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.436 |
| aspS | AKH37697.1 | AAW31_02380 | AAW31_07565 | 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. | Amidase; Catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family. | 0.631 |
| aspS | AKH38197.1 | AAW31_02380 | AAW31_10975 | 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. | Catalyzes the hydrolysis of allophanate; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.565 |
| aspS | gatA | AAW31_02380 | AAW31_03040 | 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 amidotransferase; 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). | 0.625 |
| aspS | gatB | AAW31_02380 | AAW31_03035 | 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 amidotransferase; 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. | 0.995 |
| aspS | gatC | AAW31_02380 | AAW31_03045 | 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 amidotransferase; 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. | 0.872 |
| aspS | glnS | AAW31_02380 | AAW31_15960 | 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. | glutaminyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.740 |
| atpH | gatB | AAW31_01630 | AAW31_03035 | ATP synthase F0F1 subunit delta; 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. | glutamyl-tRNA amidotransferase; 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. | 0.748 |
| atpH | gatC | AAW31_01630 | AAW31_03045 | ATP synthase F0F1 subunit delta; 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. | glutamyl-tRNA amidotransferase; 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. | 0.784 |
| atpH | rplJ | AAW31_01630 | AAW31_01305 | ATP synthase F0F1 subunit delta; 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. | 50S ribosomal protein L10; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family. | 0.895 |
| atpH | rpsN | AAW31_01630 | AAW31_16635 | ATP synthase F0F1 subunit delta; 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. | 30S ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family. | 0.806 |
| dapA | gatC | AAW31_10005 | AAW31_03045 | Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | glutamyl-tRNA amidotransferase; 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. | 0.796 |
| dapA | rplJ | AAW31_10005 | AAW31_01305 | Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | 50S ribosomal protein L10; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family. | 0.585 |