node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ARQ06629.1 | lytC | MCCS_09820 | MCCS_16080 | Hypothetical protein; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern; penicillin-binding protein 2' homolog MecB. | N-acetylmuramoyl-L-alanine amidase LytC precursor; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.566 |
ARQ06629.1 | murAA | MCCS_09820 | MCCS_22680 | Hypothetical protein; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern; penicillin-binding protein 2' homolog MecB. | UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily. | 0.684 |
ARQ06629.1 | murE | MCCS_09820 | MCCS_08580 | Hypothetical protein; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern; penicillin-binding protein 2' homolog MecB. | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L- lysine ligase; Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan; Belongs to the MurCDEF family. MurE subfamily. | 0.819 |
ARQ06629.1 | recJ | MCCS_09820 | MCCS_16120 | Hypothetical protein; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern; penicillin-binding protein 2' homolog MecB. | Single-stranded-DNA-specific exonuclease RecJ; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.460 |
ARQ07037.1 | lytC | MCCS_13960 | MCCS_16080 | Glycyl-glycine endopeptidase ALE-1 precursor; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | N-acetylmuramoyl-L-alanine amidase LytC precursor; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.594 |
apt | dtd | MCCS_16110 | MCCS_16090 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.585 |
apt | hisS | MCCS_16110 | MCCS_16060 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Histidine--tRNA ligase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.402 |
apt | lytC | MCCS_16110 | MCCS_16080 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | N-acetylmuramoyl-L-alanine amidase LytC precursor; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.568 |
apt | recJ | MCCS_16110 | MCCS_16120 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Single-stranded-DNA-specific exonuclease RecJ; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.858 |
apt | relA | MCCS_16110 | MCCS_16100 | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.591 |
dtd | apt | MCCS_16090 | MCCS_16110 | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | 0.585 |
dtd | hisS | MCCS_16090 | MCCS_16060 | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | Histidine--tRNA ligase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.492 |
dtd | lytC | MCCS_16090 | MCCS_16080 | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | N-acetylmuramoyl-L-alanine amidase LytC precursor; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.834 |
dtd | recJ | MCCS_16090 | MCCS_16120 | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | Single-stranded-DNA-specific exonuclease RecJ; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.707 |
dtd | relA | MCCS_16090 | MCCS_16100 | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.902 |
gluP | lytC | MCCS_14770 | MCCS_16080 | Rhomboid protease GluP; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | N-acetylmuramoyl-L-alanine amidase LytC precursor; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.975 |
hisS | apt | MCCS_16060 | MCCS_16110 | Histidine--tRNA ligase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | 0.402 |
hisS | dtd | MCCS_16060 | MCCS_16090 | Histidine--tRNA ligase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.492 |
hisS | lytC | MCCS_16060 | MCCS_16080 | Histidine--tRNA ligase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | N-acetylmuramoyl-L-alanine amidase LytC precursor; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.565 |
hisS | recJ | MCCS_16060 | MCCS_16120 | Histidine--tRNA ligase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | Single-stranded-DNA-specific exonuclease RecJ; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. | 0.627 |