node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABR65235.1 | ABR66654.1 | MmarC7_0165 | MmarC7_1596 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmq:MmarC5_0725 asparagine synthase (glutamine-hydrolyzing). | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 0.736 |
ABR65235.1 | aspS | MmarC7_0165 | MmarC7_0864 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmq:MmarC5_0725 asparagine synthase (glutamine-hydrolyzing). | 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). | 0.726 |
ABR65235.1 | carB | MmarC7_0165 | MmarC7_0255 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmq:MmarC5_0725 asparagine synthase (glutamine-hydrolyzing). | TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: ATP-dependent carboxylate-amine ligase domain protein ATP-grasp; Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein; MGS domain protein; RimK domain protein ATP-grasp; KEGG: mmp:MMP1013 carbamoyl-phosphate synthase large chain; Belongs to the CarB family. | 0.506 |
ABR65235.1 | gatA | MmarC7_0165 | MmarC7_0756 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmq:MmarC5_0725 asparagine synthase (glutamine-hydrolyzing). | 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). | 0.875 |
ABR65235.1 | gatB | MmarC7_0165 | MmarC7_0193 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmq:MmarC5_0725 asparagine synthase (glutamine-hydrolyzing). | 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. | 0.883 |
ABR65235.1 | gatD | MmarC7_0165 | MmarC7_0513 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmq:MmarC5_0725 asparagine synthase (glutamine-hydrolyzing). | 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. | 0.845 |
ABR65235.1 | gatE | MmarC7_0165 | MmarC7_0512 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmq:MmarC5_0725 asparagine synthase (glutamine-hydrolyzing). | Putative aspartyl-tRNA(Asn) amidotransferase, B 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.810 |
ABR65824.1 | gatA | MmarC7_0757 | MmarC7_0756 | TIGRFAM: amino acid carrier protein; PFAM: sodium:alanine symporter; KEGG: mmp:MMP1511 sodium:alanine symporter. | 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). | 0.587 |
ABR65824.1 | gatD | MmarC7_0757 | MmarC7_0513 | TIGRFAM: amino acid carrier protein; PFAM: sodium:alanine symporter; KEGG: mmp:MMP1511 sodium:alanine symporter. | 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. | 0.591 |
ABR66654.1 | ABR65235.1 | MmarC7_1596 | MmarC7_0165 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmq:MmarC5_0725 asparagine synthase (glutamine-hydrolyzing). | 0.736 |
ABR66654.1 | aspS | MmarC7_1596 | MmarC7_0864 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 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). | 0.988 |
ABR66654.1 | carB | MmarC7_1596 | MmarC7_0255 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: ATP-dependent carboxylate-amine ligase domain protein ATP-grasp; Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein; MGS domain protein; RimK domain protein ATP-grasp; KEGG: mmp:MMP1013 carbamoyl-phosphate synthase large chain; Belongs to the CarB family. | 0.547 |
ABR66654.1 | gatA | MmarC7_1596 | MmarC7_0756 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 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). | 0.999 |
ABR66654.1 | gatB | MmarC7_1596 | MmarC7_0193 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 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. | 0.999 |
ABR66654.1 | gatD | MmarC7_1596 | MmarC7_0513 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 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. | 0.911 |
ABR66654.1 | gatE | MmarC7_1596 | MmarC7_0512 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | Putative aspartyl-tRNA(Asn) amidotransferase, B 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.912 |
ABR66654.1 | guaAA | MmarC7_1596 | MmarC7_0690 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | GMP synthase, small subunit; Catalyzes the synthesis of GMP from XMP. | 0.678 |
ABR66654.1 | guaAB | MmarC7_1596 | MmarC7_0142 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.577 |
aspS | ABR65235.1 | MmarC7_0864 | MmarC7_0165 | 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). | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmq:MmarC5_0725 asparagine synthase (glutamine-hydrolyzing). | 0.726 |
aspS | ABR66654.1 | MmarC7_0864 | MmarC7_1596 | 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). | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 0.988 |