| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Arch_0418 | Arch_0422 | Arch_0418 | Arch_0422 | Phospholipase D/Transphosphatidylase; COGs: COG1502 Phosphatidylserine/phosphatidylglycerophosphate/ cardiolipin synthase; InterPro IPR001736; KEGG: xce:Xcel_1743 phospholipase D/transphosphatidylase; PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase; SPTR: D0WS38 Cardiolipin synthetase; PFAM: Phospholipase D Active site motif. | Malic protein NAD-binding protein; COGs: COG0281 Malic enzyme; InterPro IPR016040:IPR015884:IPR012301:IPR012302; KEGG: nca:Noca_2034 malate dehydrogenase; PFAM: malic protein NAD-binding; malic protein domain protein; SPTR: D0WL78 NADP-dependent malic enzyme; PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain. | 0.475 |
| Arch_0418 | gatA | Arch_0418 | Arch_0420 | Phospholipase D/Transphosphatidylase; COGs: COG1502 Phosphatidylserine/phosphatidylglycerophosphate/ cardiolipin synthase; InterPro IPR001736; KEGG: xce:Xcel_1743 phospholipase D/transphosphatidylase; PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase; SPTR: D0WS38 Cardiolipin synthetase; PFAM: Phospholipase D Active site motif. | glutamyl-tRNA(Gln) amidotransferase, A subunit; 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 |
| Arch_0418 | gatB | Arch_0418 | Arch_0421 | Phospholipase D/Transphosphatidylase; COGs: COG1502 Phosphatidylserine/phosphatidylglycerophosphate/ cardiolipin synthase; InterPro IPR001736; KEGG: xce:Xcel_1743 phospholipase D/transphosphatidylase; PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase; SPTR: D0WS38 Cardiolipin synthetase; PFAM: Phospholipase D Active site motif. | glutamyl-tRNA(Gln) amidotransferase, B subunit; 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. | 0.623 |
| Arch_0418 | gatC | Arch_0418 | Arch_0419 | Phospholipase D/Transphosphatidylase; COGs: COG1502 Phosphatidylserine/phosphatidylglycerophosphate/ cardiolipin synthase; InterPro IPR001736; KEGG: xce:Xcel_1743 phospholipase D/transphosphatidylase; PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase; SPTR: D0WS38 Cardiolipin synthetase; PFAM: Phospholipase D Active site motif. | glutamyl-tRNA(Gln) amidotransferase, C subunit; 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. | 0.623 |
| Arch_0422 | Arch_0418 | Arch_0422 | Arch_0418 | Malic protein NAD-binding protein; COGs: COG0281 Malic enzyme; InterPro IPR016040:IPR015884:IPR012301:IPR012302; KEGG: nca:Noca_2034 malate dehydrogenase; PFAM: malic protein NAD-binding; malic protein domain protein; SPTR: D0WL78 NADP-dependent malic enzyme; PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain. | Phospholipase D/Transphosphatidylase; COGs: COG1502 Phosphatidylserine/phosphatidylglycerophosphate/ cardiolipin synthase; InterPro IPR001736; KEGG: xce:Xcel_1743 phospholipase D/transphosphatidylase; PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase; SPTR: D0WS38 Cardiolipin synthetase; PFAM: Phospholipase D Active site motif. | 0.475 |
| Arch_0422 | gatA | Arch_0422 | Arch_0420 | Malic protein NAD-binding protein; COGs: COG0281 Malic enzyme; InterPro IPR016040:IPR015884:IPR012301:IPR012302; KEGG: nca:Noca_2034 malate dehydrogenase; PFAM: malic protein NAD-binding; malic protein domain protein; SPTR: D0WL78 NADP-dependent malic enzyme; PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain. | glutamyl-tRNA(Gln) amidotransferase, A subunit; 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). | 0.619 |
| Arch_0422 | gatB | Arch_0422 | Arch_0421 | Malic protein NAD-binding protein; COGs: COG0281 Malic enzyme; InterPro IPR016040:IPR015884:IPR012301:IPR012302; KEGG: nca:Noca_2034 malate dehydrogenase; PFAM: malic protein NAD-binding; malic protein domain protein; SPTR: D0WL78 NADP-dependent malic enzyme; PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain. | glutamyl-tRNA(Gln) amidotransferase, B subunit; 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. | 0.615 |
| Arch_0422 | gatC | Arch_0422 | Arch_0419 | Malic protein NAD-binding protein; COGs: COG0281 Malic enzyme; InterPro IPR016040:IPR015884:IPR012301:IPR012302; KEGG: nca:Noca_2034 malate dehydrogenase; PFAM: malic protein NAD-binding; malic protein domain protein; SPTR: D0WL78 NADP-dependent malic enzyme; PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain. | glutamyl-tRNA(Gln) amidotransferase, C subunit; 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. | 0.607 |
| aspS | gatA | Arch_0837 | Arch_0420 | 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, A subunit; 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). | 0.809 |
| aspS | gatB | Arch_0837 | Arch_0421 | 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, B subunit; 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. | 0.985 |
| aspS | gatC | Arch_0837 | Arch_0419 | 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, C subunit; 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. | 0.941 |
| aspS | gluSR | Arch_0837 | Arch_1100 | 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.846 |
| aspS | guaA | Arch_0837 | Arch_1307 | 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, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.876 |
| atpH | gatB | Arch_0364 | Arch_0421 | ATP synthase F1, delta subunit; 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; Belongs to the ATPase delta chain family. | glutamyl-tRNA(Gln) amidotransferase, B subunit; 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. | 0.482 |
| atpH | gatC | Arch_0364 | Arch_0419 | ATP synthase F1, delta subunit; 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; Belongs to the ATPase delta chain family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; 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. | 0.590 |
| atpH | rpsN | Arch_0364 | Arch_0536 | ATP synthase F1, delta subunit; 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; Belongs to the ATPase delta chain family. | 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. | 0.709 |
| atpH | rpsZ | Arch_0364 | Arch_1375 | ATP synthase F1, delta subunit; 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; Belongs to the ATPase delta chain family. | 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. | 0.709 |
| gatA | Arch_0418 | Arch_0420 | Arch_0418 | glutamyl-tRNA(Gln) amidotransferase, A subunit; 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). | Phospholipase D/Transphosphatidylase; COGs: COG1502 Phosphatidylserine/phosphatidylglycerophosphate/ cardiolipin synthase; InterPro IPR001736; KEGG: xce:Xcel_1743 phospholipase D/transphosphatidylase; PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase; SPTR: D0WS38 Cardiolipin synthetase; PFAM: Phospholipase D Active site motif. | 0.625 |
| gatA | Arch_0422 | Arch_0420 | Arch_0422 | glutamyl-tRNA(Gln) amidotransferase, A subunit; 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). | Malic protein NAD-binding protein; COGs: COG0281 Malic enzyme; InterPro IPR016040:IPR015884:IPR012301:IPR012302; KEGG: nca:Noca_2034 malate dehydrogenase; PFAM: malic protein NAD-binding; malic protein domain protein; SPTR: D0WL78 NADP-dependent malic enzyme; PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain. | 0.619 |
| gatA | aspS | Arch_0420 | Arch_0837 | glutamyl-tRNA(Gln) amidotransferase, A subunit; 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. | 0.809 |