node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
cca | dtd | b3056 | b3887 | Fused tRNA nucleotidyl transferase/2'3'-cyclic phosphodiesterase/2'nucleotidase and phosphatase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent [...] | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | 0.596 |
cca | thrS | b3056 | b1719 | Fused tRNA nucleotidyl transferase/2'3'-cyclic phosphodiesterase/2'nucleotidase and phosphatase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent [...] | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isost [...] | 0.424 |
dtd | cca | b3887 | b3056 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | Fused tRNA nucleotidyl transferase/2'3'-cyclic phosphodiesterase/2'nucleotidase and phosphatase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent [...] | 0.596 |
dtd | thrS | b3887 | b1719 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isost [...] | 0.508 |
dtd | tyrS | b3887 | b1637 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | tyrosyl-tRNA synthetase; Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase. In vitro, can also use the non-natural amino acid azatyrosine. | 0.593 |
dtd | ybgL | b3887 | b0713 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | UPF0271 family protein; Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. Belongs to the LamB/PxpA family. | 0.514 |
dtd | yihI | b3887 | b3866 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | Activator of Der GTPase; A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function, negatively regulating cell growth, probably via ribosome assembly. Stimulates the GTPase activity of Der; a construct missing the first 45 residues is even more stimulatory. Does not stimulate 2 other GTPases (ObgE and Era). Overexpression inhibits cell growth; precursor 16S rRNA accumulates, the 23S rRNA is 6-7 bases longer than usual, and 50S ribosomal subunits are improperly assembled, leading to 45S subunits lacking proteins L9, L18 and L25. Overexpression of Der in the same cells sup [...] | 0.551 |
dtd | yihV | b3887 | b3883 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | 6-deoxy-6-sulphofructose kinase; Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6- sulfo-D-fructose 1-phosphate (SFP); Belongs to the carbohydrate kinase PfkB family. | 0.487 |
dtd | yihW | b3887 | b3884 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | Putative transcriptional regulator for sulphoquinovose utilization; Involved in the regulation of the sulfoquinovose operon. Represses the expression of the yihUTS operon and of the yihV and csqR genes. Binds DNA inside the spacer between the bidirectional transcription units comprising the yihUTS operon and the yihV gene, and upstream the csqR gene itself. | 0.535 |
dtd | yihX | b3887 | b3885 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | alpha-D-glucose-1-phosphate phosphatase, anomer-specific; Catalyzes the dephosphorylation of alpha-D-glucose 1- phosphate (Glc1P) and, to a lesser extent, of other sugar phosphates. Has no activity with the beta form of Glc1P. In addition, YihX has significant phosphatase activity against pyridoxal phosphate (PLP) and low beta-phosphoglucomutase activity. | 0.818 |
dtd | yihY | b3887 | b3886 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | BrkB family putative transporter, inner membrane protein; tRNA processing exoribonuclease BN. | 0.809 |
dtd | yiiD | b3887 | b3888 | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | GNAT family putative N-acetyltransferase; Putative acetyltransferase. | 0.985 |
thrS | cca | b1719 | b3056 | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isost [...] | Fused tRNA nucleotidyl transferase/2'3'-cyclic phosphodiesterase/2'nucleotidase and phosphatase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent [...] | 0.424 |
thrS | dtd | b1719 | b3887 | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isost [...] | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | 0.508 |
thrS | tyrS | b1719 | b1637 | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isost [...] | tyrosyl-tRNA synthetase; Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase. In vitro, can also use the non-natural amino acid azatyrosine. | 0.937 |
tyrS | dtd | b1637 | b3887 | tyrosyl-tRNA synthetase; Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase. In vitro, can also use the non-natural amino acid azatyrosine. | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | 0.593 |
tyrS | thrS | b1637 | b1719 | tyrosyl-tRNA synthetase; Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase. In vitro, can also use the non-natural amino acid azatyrosine. | threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isost [...] | 0.937 |
ybgL | dtd | b0713 | b3887 | UPF0271 family protein; Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. Belongs to the LamB/PxpA family. | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | 0.514 |
yihI | dtd | b3866 | b3887 | Activator of Der GTPase; A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function, negatively regulating cell growth, probably via ribosome assembly. Stimulates the GTPase activity of Der; a construct missing the first 45 residues is even more stimulatory. Does not stimulate 2 other GTPases (ObgE and Era). Overexpression inhibits cell growth; precursor 16S rRNA accumulates, the 23S rRNA is 6-7 bases longer than usual, and 50S ribosomal subunits are improperly assembled, leading to 45S subunits lacking proteins L9, L18 and L25. Overexpression of Der in the same cells sup [...] | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | 0.551 |
yihV | dtd | b3883 | b3887 | 6-deoxy-6-sulphofructose kinase; Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6- sulfo-D-fructose 1-phosphate (SFP); Belongs to the carbohydrate kinase PfkB family. | D-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] | 0.487 |