| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPA1405 | RPA2974 | RPA1405 | RPA2974 | Putative urea amidolyase. | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | 0.464 |
| RPA2973 | RPA2974 | RPA2973 | RPA2974 | Hypothetical protein. | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | 0.560 |
| RPA2974 | RPA1405 | RPA2974 | RPA1405 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | Putative urea amidolyase. | 0.464 |
| RPA2974 | RPA2973 | RPA2974 | RPA2973 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | Hypothetical protein. | 0.560 |
| RPA2974 | RPA3200 | RPA2974 | RPA3200 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | Putative dual serine/threonine-protein kinase/phosphatase. | 0.446 |
| RPA2974 | aspS | RPA2974 | RPA3043 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | aspartate-tRNA ligase; 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. | 0.493 |
| RPA2974 | gatB | RPA2974 | RPA3104 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | Glu-tRNA(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. | 0.931 |
| RPA2974 | gatC | RPA2974 | RPA3111 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | Glu-tRNA(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. | 0.838 |
| RPA2974 | nthA | RPA2974 | RPA2805 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | Nitrile hydratase alpha subunit; Citation: Payne et al. (1997) Biochemistry 36:5447-5454. | 0.515 |
| RPA2974 | nthB | RPA2974 | RPA2806 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | Putative nitrile hydratase beta subunit; NHase catalyzes the hydration of various nitrile compounds to the corresponding amides; Belongs to the nitrile hydratase subunit beta family. | 0.519 |
| RPA2974 | pfkB | RPA2974 | RPA0379 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | Putative 6-phosphofructokinase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the carbohydrate kinase PfkB family. | 0.497 |
| RPA2974 | serA1 | RPA2974 | RPA2975 | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | Putative phosphoglycerate dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. | 0.469 |
| RPA3200 | RPA2974 | RPA3200 | RPA2974 | Putative dual serine/threonine-protein kinase/phosphatase. | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | 0.446 |
| RPA3200 | gatB | RPA3200 | RPA3104 | Putative dual serine/threonine-protein kinase/phosphatase. | Glu-tRNA(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. | 0.627 |
| aspS | RPA2974 | RPA3043 | RPA2974 | aspartate-tRNA ligase; 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. | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | 0.493 |
| aspS | gatB | RPA3043 | RPA3104 | aspartate-tRNA ligase; 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. | Glu-tRNA(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. | 0.996 |
| aspS | gatC | RPA3043 | RPA3111 | aspartate-tRNA ligase; 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. | Glu-tRNA(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. | 0.942 |
| gatB | RPA2974 | RPA3104 | RPA2974 | Glu-tRNA(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. | Putative 6-aminohexanoate-cyclic-dimer hydrolase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the amidase family. | 0.931 |
| gatB | RPA3200 | RPA3104 | RPA3200 | Glu-tRNA(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. | Putative dual serine/threonine-protein kinase/phosphatase. | 0.627 |
| gatB | aspS | RPA3104 | RPA3043 | Glu-tRNA(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. | aspartate-tRNA ligase; 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. | 0.996 |