| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| fosB | pbpE | BSU17840 | BSU34440 | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis. | 0.556 |
| fosB | pksJ | BSU17840 | BSU17180 | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.408 |
| fosB | ydjP | BSU17840 | BSU06280 | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | Putative peroxydase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.740 |
| fosB | yeaA | BSU17840 | BSU06290 | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.631 |
| fosB | yfhM | BSU17840 | BSU08590 | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | Epoxide hydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the AB hydrolase superfamily. Epoxide hydrolase family. | 0.645 |
| fosB | yqeZ | BSU17840 | BSU25390 | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | Putative membrane bound hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.575 |
| fosB | ythP | BSU17840 | BSU30010 | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | Putative ABC transporter (ATP-binding protein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter; Belongs to the ABC transporter superfamily. | 0.625 |
| fosB | yuaG | BSU17840 | BSU31010 | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | Putative flotillin-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor. | 0.598 |
| pbpE | fosB | BSU34440 | BSU17840 | Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis. | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | 0.556 |
| pbpE | pksJ | BSU34440 | BSU17180 | Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.461 |
| pbpE | ydjP | BSU34440 | BSU06280 | Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis. | Putative peroxydase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.820 |
| pbpE | yfhM | BSU34440 | BSU08590 | Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis. | Epoxide hydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the AB hydrolase superfamily. Epoxide hydrolase family. | 0.693 |
| pbpE | yqeZ | BSU34440 | BSU25390 | Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis. | Putative membrane bound hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.774 |
| pbpE | ythP | BSU34440 | BSU30010 | Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis. | Putative ABC transporter (ATP-binding protein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter; Belongs to the ABC transporter superfamily. | 0.672 |
| pbpE | yuaG | BSU34440 | BSU31010 | Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis. | Putative flotillin-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor. | 0.598 |
| pksJ | fosB | BSU17180 | BSU17840 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. | 0.408 |
| pksJ | pbpE | BSU17180 | BSU34440 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis. | 0.461 |
| pksJ | ydjP | BSU17180 | BSU06280 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Putative peroxydase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.799 |
| pksJ | yfhM | BSU17180 | BSU08590 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Epoxide hydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the AB hydrolase superfamily. Epoxide hydrolase family. | 0.799 |
| pksJ | ythP | BSU17180 | BSU30010 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Putative ABC transporter (ATP-binding protein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter; Belongs to the ABC transporter superfamily. | 0.468 |