| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BDP_0057 | BDP_0058 | BDP_0057 | BDP_0058 | Serine protease. | Cation-transporting ATPase. | 0.644 |
| BDP_0057 | tgt | BDP_0057 | BDP_0056 | Serine protease. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.632 |
| BDP_0058 | BDP_0057 | BDP_0058 | BDP_0057 | Cation-transporting ATPase. | Serine protease. | 0.644 |
| BDP_0058 | tgt | BDP_0058 | BDP_0056 | Cation-transporting ATPase. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.470 |
| aspS | der | BDP_0785 | BDP_1165 | aspS 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. | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | 0.471 |
| aspS | gltX | BDP_0785 | BDP_2005 | aspS 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-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.499 |
| aspS | guaA | BDP_0785 | BDP_1005 | aspS 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 glutamine amidotransferase; Catalyzes the synthesis of GMP from XMP. | 0.724 |
| aspS | hisS | BDP_0785 | BDP_0784 | aspS 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. | HisS Histidyl-tRNA synthetase. | 0.940 |
| aspS | pnp | BDP_0785 | BDP_0367 | aspS 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. | Pnp Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. | 0.465 |
| aspS | tgt | BDP_0785 | BDP_0056 | aspS 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. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.476 |
| der | aspS | BDP_1165 | BDP_0785 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | aspS 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. | 0.471 |
| der | guaA | BDP_1165 | BDP_1005 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | GMP synthase glutamine amidotransferase; Catalyzes the synthesis of GMP from XMP. | 0.823 |
| der | pnp | BDP_1165 | BDP_0367 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | Pnp Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. | 0.532 |
| der | tgt | BDP_1165 | BDP_0056 | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.688 |
| gltX | aspS | BDP_2005 | BDP_0785 | Glutamyl-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | aspS 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. | 0.499 |
| gltX | guaA | BDP_2005 | BDP_1005 | Glutamyl-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | GMP synthase glutamine amidotransferase; Catalyzes the synthesis of GMP from XMP. | 0.618 |
| gltX | tgt | BDP_2005 | BDP_0056 | Glutamyl-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] | 0.503 |
| guaA | aspS | BDP_1005 | BDP_0785 | GMP synthase glutamine amidotransferase; Catalyzes the synthesis of GMP from XMP. | aspS 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. | 0.724 |
| guaA | der | BDP_1005 | BDP_1165 | GMP synthase glutamine amidotransferase; Catalyzes the synthesis of GMP from XMP. | Bifunctional cytidylate kinase/GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily. | 0.823 |
| guaA | gltX | BDP_1005 | BDP_2005 | GMP synthase glutamine amidotransferase; Catalyzes the synthesis of GMP from XMP. | Glutamyl-Q tRNA(Asp) synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.618 |