| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Tter_0057 | gatA | Tter_0057 | Tter_0058 | PFAM: Septum formation initiator; KEGG: afr:AFE_0850 septum formation initiator family protein. | 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). | 0.617 |
| Tter_0057 | gatC | Tter_0057 | Tter_0059 | PFAM: Septum formation initiator; KEGG: afr:AFE_0850 septum formation initiator family protein. | 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. | 0.644 |
| Tter_0057 | rodA | Tter_0057 | Tter_0060 | PFAM: Septum formation initiator; KEGG: afr:AFE_0850 septum formation initiator family protein. | Rod shape-determining protein RodA; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily. | 0.797 |
| Tter_0458 | Tter_0474 | Tter_0458 | Tter_0474 | PFAM: Amidase; KEGG: rpb:RPB_0220 amidase; Belongs to the amidase family. | PFAM: ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein; glutamate synthase; glutamine amidotransferase class-II; KEGG: afw:Anae109_0854 glutamate synthase (ferredoxin). | 0.464 |
| Tter_0458 | aspS | Tter_0458 | Tter_0950 | PFAM: Amidase; KEGG: rpb:RPB_0220 amidase; 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. | 0.670 |
| Tter_0458 | gatA | Tter_0458 | Tter_0058 | PFAM: Amidase; KEGG: rpb:RPB_0220 amidase; Belongs to the amidase family. | 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). | 0.918 |
| Tter_0458 | gatB | Tter_0458 | Tter_0804 | PFAM: Amidase; KEGG: rpb:RPB_0220 amidase; Belongs to the amidase 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. | 0.998 |
| Tter_0458 | gatC | Tter_0458 | Tter_0059 | PFAM: Amidase; KEGG: rpb:RPB_0220 amidase; Belongs to the amidase 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. | 0.997 |
| Tter_0474 | Tter_0458 | Tter_0474 | Tter_0458 | PFAM: ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein; glutamate synthase; glutamine amidotransferase class-II; KEGG: afw:Anae109_0854 glutamate synthase (ferredoxin). | PFAM: Amidase; KEGG: rpb:RPB_0220 amidase; Belongs to the amidase family. | 0.464 |
| Tter_0474 | atpH | Tter_0474 | Tter_0066 | PFAM: ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein; glutamate synthase; glutamine amidotransferase class-II; KEGG: afw:Anae109_0854 glutamate synthase (ferredoxin). | 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. | 0.429 |
| Tter_0474 | gatA | Tter_0474 | Tter_0058 | PFAM: ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein; glutamate synthase; glutamine amidotransferase class-II; KEGG: afw:Anae109_0854 glutamate synthase (ferredoxin). | 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). | 0.720 |
| Tter_0474 | gatB | Tter_0474 | Tter_0804 | PFAM: ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein; glutamate synthase; glutamine amidotransferase class-II; KEGG: afw:Anae109_0854 glutamate synthase (ferredoxin). | 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. | 0.705 |
| Tter_0474 | gatC | Tter_0474 | Tter_0059 | PFAM: ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein; glutamate synthase; glutamine amidotransferase class-II; KEGG: afw:Anae109_0854 glutamate synthase (ferredoxin). | 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. | 0.707 |
| Tter_1106 | gatC | Tter_1106 | Tter_0059 | PFAM: protein of unknown function DUF993; KEGG: atc:AGR_L_3385 hypothetical protein. | 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. | 0.707 |
| aspS | Tter_0458 | Tter_0950 | Tter_0458 | 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. | PFAM: Amidase; KEGG: rpb:RPB_0220 amidase; Belongs to the amidase family. | 0.670 |
| aspS | gatA | Tter_0950 | Tter_0058 | 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). | 0.611 |
| aspS | gatB | Tter_0950 | Tter_0804 | 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. | 0.993 |
| aspS | gatC | Tter_0950 | Tter_0059 | 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. | 0.871 |
| atpH | Tter_0474 | Tter_0066 | Tter_0474 | 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. | PFAM: ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein; glutamate synthase; glutamine amidotransferase class-II; KEGG: afw:Anae109_0854 glutamate synthase (ferredoxin). | 0.429 |
| atpH | gatA | Tter_0066 | Tter_0058 | 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, 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). | 0.420 |