| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMA44565.1 | AMA44566.1 | APT63_02425 | APT63_02430 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.981 |
| AMA44565.1 | AMA44567.1 | APT63_02425 | APT63_02435 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family. | 0.942 |
| AMA44565.1 | AMA44568.1 | APT63_02425 | APT63_02440 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family. | 0.917 |
| AMA44565.1 | lipA | APT63_02425 | APT63_02450 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.917 |
| AMA44565.1 | lipB | APT63_02425 | APT63_02445 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.917 |
| AMA44565.1 | mrdB | APT63_02425 | APT63_02420 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Rod shape-determining protein RodA; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily. | 0.967 |
| AMA44565.1 | proA | APT63_02425 | APT63_02395 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Gamma-glutamyl-phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family. | 0.933 |
| AMA44565.1 | rlmH | APT63_02425 | APT63_02410 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 23S rRNA (pseudouridine(1915)-N(3))-methyltransferase RlmH; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family. | 0.945 |
| AMA44566.1 | AMA44565.1 | APT63_02430 | APT63_02425 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.981 |
| AMA44566.1 | AMA44567.1 | APT63_02430 | APT63_02435 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family. | 0.944 |
| AMA44566.1 | AMA44568.1 | APT63_02430 | APT63_02440 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family. | 0.920 |
| AMA44566.1 | lipA | APT63_02430 | APT63_02450 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.918 |
| AMA44566.1 | lipB | APT63_02430 | APT63_02445 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.920 |
| AMA44566.1 | mrdB | APT63_02430 | APT63_02420 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Rod shape-determining protein RodA; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily. | 0.989 |
| AMA44566.1 | proA | APT63_02430 | APT63_02395 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Gamma-glutamyl-phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family. | 0.950 |
| AMA44566.1 | rlmH | APT63_02430 | APT63_02410 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 23S rRNA (pseudouridine(1915)-N(3))-methyltransferase RlmH; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family. | 0.962 |
| AMA44567.1 | AMA44565.1 | APT63_02435 | APT63_02425 | D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family. | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.942 |
| AMA44567.1 | AMA44566.1 | APT63_02435 | APT63_02430 | D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.944 |
| AMA44567.1 | AMA44568.1 | APT63_02435 | APT63_02440 | D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family. | 0.955 |
| AMA44567.1 | lipA | APT63_02435 | APT63_02450 | D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.945 |