| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ping_0287 | dtd | Ping_0287 | Ping_3481 | TIGRFAM: chorismate mutase; PFAM: Chorismate mutase; Prephenate dehydrogenase; KEGG: vfi:VF0554 chorismate mutase. | 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. | 0.415 |
| Ping_3480 | Ping_3482 | Ping_3480 | Ping_3482 | Pitrilysin, Metallo peptidase, MEROPS family M16A; PFAM: peptidase M16 domain protein; KEGG: pha:PSHAb0349 putative TonB-dependent receptor protease/peptidase. | tRNA-processing RNAse BN; TIGRFAM: putative ribonuclease BN; PFAM: ribonuclease BN; KEGG: ssn:SSO_4055 tRNA processing exoribonuclease BN. | 0.465 |
| Ping_3480 | dtd | Ping_3480 | Ping_3481 | Pitrilysin, Metallo peptidase, MEROPS family M16A; PFAM: peptidase M16 domain protein; KEGG: pha:PSHAb0349 putative TonB-dependent receptor protease/peptidase. | 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. | 0.465 |
| Ping_3482 | Ping_3480 | Ping_3482 | Ping_3480 | tRNA-processing RNAse BN; TIGRFAM: putative ribonuclease BN; PFAM: ribonuclease BN; KEGG: ssn:SSO_4055 tRNA processing exoribonuclease BN. | Pitrilysin, Metallo peptidase, MEROPS family M16A; PFAM: peptidase M16 domain protein; KEGG: pha:PSHAb0349 putative TonB-dependent receptor protease/peptidase. | 0.465 |
| Ping_3482 | bipA | Ping_3482 | Ping_3483 | tRNA-processing RNAse BN; TIGRFAM: putative ribonuclease BN; PFAM: ribonuclease BN; KEGG: ssn:SSO_4055 tRNA processing exoribonuclease BN. | GTP-binding virulence regulator protein BipA; TIGRFAM: small GTP-binding protein; GTP-binding protein TypA; PFAM: elongation factor G domain protein; protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: pat:Patl_1024 GTP-binding protein TypA. | 0.817 |
| Ping_3482 | dtd | Ping_3482 | Ping_3481 | tRNA-processing RNAse BN; TIGRFAM: putative ribonuclease BN; PFAM: ribonuclease BN; KEGG: ssn:SSO_4055 tRNA processing exoribonuclease BN. | 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. | 0.799 |
| bipA | Ping_3482 | Ping_3483 | Ping_3482 | GTP-binding virulence regulator protein BipA; TIGRFAM: small GTP-binding protein; GTP-binding protein TypA; PFAM: elongation factor G domain protein; protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: pat:Patl_1024 GTP-binding protein TypA. | tRNA-processing RNAse BN; TIGRFAM: putative ribonuclease BN; PFAM: ribonuclease BN; KEGG: ssn:SSO_4055 tRNA processing exoribonuclease BN. | 0.817 |
| bipA | dtd | Ping_3483 | Ping_3481 | GTP-binding virulence regulator protein BipA; TIGRFAM: small GTP-binding protein; GTP-binding protein TypA; PFAM: elongation factor G domain protein; protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: pat:Patl_1024 GTP-binding protein TypA. | 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. | 0.568 |
| dtd | Ping_0287 | Ping_3481 | Ping_0287 | 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. | TIGRFAM: chorismate mutase; PFAM: Chorismate mutase; Prephenate dehydrogenase; KEGG: vfi:VF0554 chorismate mutase. | 0.415 |
| dtd | Ping_3480 | Ping_3481 | Ping_3480 | 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. | Pitrilysin, Metallo peptidase, MEROPS family M16A; PFAM: peptidase M16 domain protein; KEGG: pha:PSHAb0349 putative TonB-dependent receptor protease/peptidase. | 0.465 |
| dtd | Ping_3482 | Ping_3481 | Ping_3482 | 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. | tRNA-processing RNAse BN; TIGRFAM: putative ribonuclease BN; PFAM: ribonuclease BN; KEGG: ssn:SSO_4055 tRNA processing exoribonuclease BN. | 0.799 |
| dtd | bipA | Ping_3481 | Ping_3483 | 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-binding virulence regulator protein BipA; TIGRFAM: small GTP-binding protein; GTP-binding protein TypA; PFAM: elongation factor G domain protein; protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: pat:Patl_1024 GTP-binding protein TypA. | 0.568 |
| dtd | lpxH | Ping_3481 | Ping_2186 | 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. | UDP-2,3-diacylglucosamine hydrolase; Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | 0.402 |
| lpxH | dtd | Ping_2186 | Ping_3481 | UDP-2,3-diacylglucosamine hydrolase; Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | 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. | 0.402 |