node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
APF39804.1 | APF41653.1 | BHE16_00825 | BHE16_02280 | Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Preprotein translocase subunit YajC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.403 |
APF39804.1 | aspS | BHE16_00825 | BHE16_02320 | Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | aspartate--tRNA ligase; 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. | 0.415 |
APF39804.1 | guaA | BHE16_00825 | BHE16_11735 | Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Glutamine-hydrolyzing GMP synthase; Catalyzes the synthesis of GMP from XMP. | 0.460 |
APF39804.1 | ribB | BHE16_00825 | BHE16_00850 | Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; Belongs to the GTP cyclohydrolase II family. | 0.923 |
APF39804.1 | tgt | BHE16_00825 | BHE16_06485 | Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | tRNA-guanine(34) transglycosylase; 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 [...] | 0.534 |
APF39804.1 | thyA | BHE16_00825 | BHE16_11270 | Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Thymidylate synthase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. | 0.695 |
APF39804.1 | truB | BHE16_00825 | BHE16_04115 | Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | tRNA pseudouridine(55) synthase TruB; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. | 0.885 |
APF40717.1 | tgt | BHE16_06480 | BHE16_06485 | DUF4916 domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | tRNA-guanine(34) transglycosylase; 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 [...] | 0.566 |
APF40722.1 | gluQ | BHE16_06510 | BHE16_06650 | Hypothetical protein; Involved in the import of queuosine (Q) precursors, required for Q precursor salvage; Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Q precursor transporter subfamily. | tRNA glutamyl-Q(34) synthetase GluQRS; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | 0.768 |
APF40722.1 | tgt | BHE16_06510 | BHE16_06485 | Hypothetical protein; Involved in the import of queuosine (Q) precursors, required for Q precursor salvage; Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Q precursor transporter subfamily. | tRNA-guanine(34) transglycosylase; 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 [...] | 0.766 |
APF41653.1 | APF39804.1 | BHE16_02280 | BHE16_00825 | Preprotein translocase subunit YajC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.403 |
APF41653.1 | tgt | BHE16_02280 | BHE16_06485 | Preprotein translocase subunit YajC; Derived by automated computational analysis using gene prediction method: Protein Homology. | tRNA-guanine(34) transglycosylase; 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 [...] | 0.452 |
aspS | APF39804.1 | BHE16_02320 | BHE16_00825 | aspartate--tRNA ligase; 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. | Methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.415 |
aspS | gluQ | BHE16_02320 | BHE16_06650 | aspartate--tRNA ligase; 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. | tRNA glutamyl-Q(34) synthetase GluQRS; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | 0.589 |
aspS | guaA | BHE16_02320 | BHE16_11735 | aspartate--tRNA ligase; 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. | Glutamine-hydrolyzing GMP synthase; Catalyzes the synthesis of GMP from XMP. | 0.742 |
aspS | tgt | BHE16_02320 | BHE16_06485 | aspartate--tRNA ligase; 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. | tRNA-guanine(34) transglycosylase; 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 [...] | 0.452 |
gluQ | APF40722.1 | BHE16_06650 | BHE16_06510 | tRNA glutamyl-Q(34) synthetase GluQRS; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Hypothetical protein; Involved in the import of queuosine (Q) precursors, required for Q precursor salvage; Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Q precursor transporter subfamily. | 0.768 |
gluQ | aspS | BHE16_06650 | BHE16_02320 | tRNA glutamyl-Q(34) synthetase GluQRS; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | aspartate--tRNA ligase; 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. | 0.589 |
gluQ | guaA | BHE16_06650 | BHE16_11735 | tRNA glutamyl-Q(34) synthetase GluQRS; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Glutamine-hydrolyzing GMP synthase; Catalyzes the synthesis of GMP from XMP. | 0.671 |
gluQ | tgt | BHE16_06650 | BHE16_06485 | tRNA glutamyl-Q(34) synthetase GluQRS; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | tRNA-guanine(34) transglycosylase; 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 [...] | 0.775 |