node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MMP0575 | asnB | MMP0575 | MMP0918 | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | 0.497 |
MMP0575 | aspS | MMP0575 | MMP1616 | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 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). | 0.992 |
MMP0575 | gatA | MMP0575 | MMP1510 | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | Asp-tRNAAsn/Glu-tRNAGln 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). | 0.999 |
MMP0575 | gatB | MMP0575 | MMP0946 | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | Asp-tRNAAsn/Glu-tRNAGln 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. | 0.999 |
MMP0575 | gatD | MMP0575 | MMP1266 | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | Glutamyl-tRNA(Gln) amidotransferase subunit D; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.917 |
MMP0575 | gatE | MMP0575 | MMP1265 | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | Glutamyl-tRNA(Gln) amidotransferase subunit E; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.918 |
MMP0575 | glnA | MMP0575 | MMP1206 | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | Glutamine synthetase; Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. | 0.511 |
MMP0575 | gltX | MMP0575 | MMP1011 | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 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). | 0.401 |
asnB | MMP0575 | MMP0918 | MMP0575 | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 0.497 |
asnB | aspS | MMP0918 | MMP1616 | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | 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). | 0.826 |
asnB | cysS | MMP0918 | MMP1060 | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | Cysteinyl-tRNA synthetase. | 0.623 |
asnB | gatA | MMP0918 | MMP1510 | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | Asp-tRNAAsn/Glu-tRNAGln 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). | 0.772 |
asnB | gatB | MMP0918 | MMP0946 | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | Asp-tRNAAsn/Glu-tRNAGln 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. | 0.777 |
asnB | gatD | MMP0918 | MMP1266 | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | Glutamyl-tRNA(Gln) amidotransferase subunit D; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.759 |
asnB | gatE | MMP0918 | MMP1265 | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | Glutamyl-tRNA(Gln) amidotransferase subunit E; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.689 |
asnB | gltX | MMP0918 | MMP1011 | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | 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). | 0.680 |
asnB | sepS | MMP0918 | MMP0688 | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | Phenylalanyl-tRNA synthetase alpha subunit; Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys). | 0.563 |
aspS | MMP0575 | MMP1616 | MMP0575 | 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). | Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 0.992 |
aspS | asnB | MMP1616 | MMP0918 | 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). | Asparagine synthetase (glutamine-hydrolyzing); Citation: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I. (1999) Biochemistry 38:16146-57. | 0.826 |
aspS | cysS | MMP1616 | MMP1060 | 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). | Cysteinyl-tRNA synthetase. | 0.905 |