node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
JU82_09320 | JU82_10405 | JU82_09320 | JU82_10405 | Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.973 |
JU82_09320 | gatA | JU82_09320 | JU82_04805 | Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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). | 0.966 |
JU82_09320 | gatB | JU82_09320 | JU82_11480 | Glutamate synthase; 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. | 0.937 |
JU82_09320 | gatC | JU82_09320 | JU82_02800 | Glutamate synthase; 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. | 0.954 |
JU82_09320 | gltX-2 | JU82_09320 | JU82_08240 | Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | glutamylglutaminyl-tRNA ligase; 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. | 0.917 |
JU82_09320 | hisF | JU82_09320 | JU82_00480 | Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Imidazole glycerol phosphate synthase; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | 0.962 |
JU82_09320 | hisH | JU82_09320 | JU82_07065 | Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glutamine amidotransferase; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. | 0.948 |
JU82_09320 | hisI | JU82_09320 | JU82_06585 | Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | phosphoribosyl-ATP diphosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the PRA-CH family. | 0.944 |
JU82_09320 | pyrG | JU82_09320 | JU82_08270 | Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.971 |
JU82_10405 | JU82_09320 | JU82_10405 | JU82_09320 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.973 |
JU82_10405 | aspS | JU82_10405 | JU82_01045 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 |
JU82_10405 | gatA | JU82_10405 | JU82_04805 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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). | 0.999 |
JU82_10405 | gatB | JU82_10405 | JU82_11480 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; 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. | 0.938 |
JU82_10405 | gatC | JU82_10405 | JU82_02800 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; 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. | 0.997 |
JU82_10405 | gltX-2 | JU82_10405 | JU82_08240 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | glutamylglutaminyl-tRNA ligase; 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. | 0.842 |
JU82_10405 | hisF | JU82_10405 | JU82_00480 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | Imidazole glycerol phosphate synthase; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | 0.664 |
JU82_10405 | hisH | JU82_10405 | JU82_07065 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glutamine amidotransferase; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. | 0.625 |
JU82_10405 | hisI | JU82_10405 | JU82_06585 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | phosphoribosyl-ATP diphosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the PRA-CH family. | 0.798 |
JU82_10405 | pyrG | JU82_10405 | JU82_08270 | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.913 |
aspS | JU82_10405 | JU82_01045 | JU82_10405 | 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. | glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Deinococcus the extra C-terminal extension of YqeY domain enhances affinity for tRNA-Gln; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |