| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ampS | pepA | BSU14450 | BSU32050 | Aminopeptidase; Metal-dependent exopeptidase; Belongs to the peptidase M29 family. | Leucyl aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). | 0.742 |
| ampS | pepT | BSU14450 | BSU38920 | Aminopeptidase; Metal-dependent exopeptidase; Belongs to the peptidase M29 family. | Peptidase T (tripeptidase); Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.672 |
| ampS | ykvY | BSU14450 | BSU13860 | Aminopeptidase; Metal-dependent exopeptidase; Belongs to the peptidase M29 family. | Putative Xaa-Pro dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.781 |
| ampS | ywaD | BSU14450 | BSU38470 | Aminopeptidase; Metal-dependent exopeptidase; Belongs to the peptidase M29 family. | Double-zinc aminopeptidase; Catalyzes the hydrolysis of a range of N-terminal amino acids. | 0.534 |
| ccpA | guaB | BSU29740 | BSU00090 | Transcriptional regulator (Lacl family); Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P- Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. | Inosine-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. | 0.647 |
| ccpA | ykvY | BSU29740 | BSU13860 | Transcriptional regulator (Lacl family); Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P- Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. | Putative Xaa-Pro dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.597 |
| dtpT | pepT | BSU03670 | BSU38920 | Di-tripeptide-proton ABC symporter; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type t: transporter. | Peptidase T (tripeptidase); Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.748 |
| dtpT | ykvY | BSU03670 | BSU13860 | Di-tripeptide-proton ABC symporter; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type t: transporter. | Putative Xaa-Pro dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.623 |
| guaB | ccpA | BSU00090 | BSU29740 | Inosine-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. | Transcriptional regulator (Lacl family); Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P- Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. | 0.647 |
| guaB | ykvY | BSU00090 | BSU13860 | Inosine-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. | Putative Xaa-Pro dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.631 |
| pepA | ampS | BSU32050 | BSU14450 | Leucyl aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). | Aminopeptidase; Metal-dependent exopeptidase; Belongs to the peptidase M29 family. | 0.742 |
| pepA | ykvY | BSU32050 | BSU13860 | Leucyl aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). | Putative Xaa-Pro dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.686 |
| pepA | ywaD | BSU32050 | BSU38470 | Leucyl aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). | Double-zinc aminopeptidase; Catalyzes the hydrolysis of a range of N-terminal amino acids. | 0.870 |
| pepT | ampS | BSU38920 | BSU14450 | Peptidase T (tripeptidase); Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | Aminopeptidase; Metal-dependent exopeptidase; Belongs to the peptidase M29 family. | 0.672 |
| pepT | dtpT | BSU38920 | BSU03670 | Peptidase T (tripeptidase); Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | Di-tripeptide-proton ABC symporter; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type t: transporter. | 0.748 |
| pepT | ykvY | BSU38920 | BSU13860 | Peptidase T (tripeptidase); Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | Putative Xaa-Pro dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.685 |
| tsaB | tsaD | BSU05920 | BSU05940 | tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. | tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB; this reaction does not require ATP in vitro. TsaD likely plays a direct catalytic role in this reaction. Belongs to the KAE1 / TsaD family. | 0.999 |
| tsaB | ykvY | BSU05920 | BSU13860 | tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. | Putative Xaa-Pro dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.569 |
| tsaD | tsaB | BSU05940 | BSU05920 | tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB; this reaction does not require ATP in vitro. TsaD likely plays a direct catalytic role in this reaction. Belongs to the KAE1 / TsaD family. | tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. | 0.999 |
| tsaD | ykvY | BSU05940 | BSU13860 | tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB; this reaction does not require ATP in vitro. TsaD likely plays a direct catalytic role in this reaction. Belongs to the KAE1 / TsaD family. | Putative Xaa-Pro dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.521 |