| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| abgA | abgB | b1338 | b1337 | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. | P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. | 0.995 |
| abgA | abgR | b1338 | b1339 | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. | Putative DNA-binding transcriptional regulator of abgABT operon; Could be the regulator of the abg operon; Belongs to the LysR transcriptional regulatory family. | 0.925 |
| abgA | abgT | b1338 | b1336 | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. | P-aminobenzoyl-glutamate transporter; Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl- glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p- aminobenzoate and glutamate. It seems also to increase the sensitivity to low levels of aminobenzoyl-glutamate. May actually serve physiologically as a transporter for some other molecule, perhaps a dipeptide, and that it transports p-aminobenzoyl-glutamate as a secondary activity. The physiological ro [...] | 0.996 |
| abgA | fnr | b1338 | b1334 | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. | Oxygen-sensing anaerobic growth regulon transcriptional regulator FNR; Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O(2), is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration. | 0.410 |
| abgA | ogt | b1338 | b1335 | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. | O-6-alkylguanine-DNA:cysteine-protein methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.832 |
| abgB | abgA | b1337 | b1338 | P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. | 0.995 |
| abgB | abgR | b1337 | b1339 | P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. | Putative DNA-binding transcriptional regulator of abgABT operon; Could be the regulator of the abg operon; Belongs to the LysR transcriptional regulatory family. | 0.919 |
| abgB | abgT | b1337 | b1336 | P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. | P-aminobenzoyl-glutamate transporter; Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl- glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p- aminobenzoate and glutamate. It seems also to increase the sensitivity to low levels of aminobenzoyl-glutamate. May actually serve physiologically as a transporter for some other molecule, perhaps a dipeptide, and that it transports p-aminobenzoyl-glutamate as a secondary activity. The physiological ro [...] | 0.989 |
| abgB | ogt | b1337 | b1335 | P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. | O-6-alkylguanine-DNA:cysteine-protein methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.828 |
| abgR | abgA | b1339 | b1338 | Putative DNA-binding transcriptional regulator of abgABT operon; Could be the regulator of the abg operon; Belongs to the LysR transcriptional regulatory family. | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. | 0.925 |
| abgR | abgB | b1339 | b1337 | Putative DNA-binding transcriptional regulator of abgABT operon; Could be the regulator of the abg operon; Belongs to the LysR transcriptional regulatory family. | P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. | 0.919 |
| abgR | abgT | b1339 | b1336 | Putative DNA-binding transcriptional regulator of abgABT operon; Could be the regulator of the abg operon; Belongs to the LysR transcriptional regulatory family. | P-aminobenzoyl-glutamate transporter; Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl- glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p- aminobenzoate and glutamate. It seems also to increase the sensitivity to low levels of aminobenzoyl-glutamate. May actually serve physiologically as a transporter for some other molecule, perhaps a dipeptide, and that it transports p-aminobenzoyl-glutamate as a secondary activity. The physiological ro [...] | 0.907 |
| abgR | ogt | b1339 | b1335 | Putative DNA-binding transcriptional regulator of abgABT operon; Could be the regulator of the abg operon; Belongs to the LysR transcriptional regulatory family. | O-6-alkylguanine-DNA:cysteine-protein methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.710 |
| abgT | abgA | b1336 | b1338 | P-aminobenzoyl-glutamate transporter; Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl- glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p- aminobenzoate and glutamate. It seems also to increase the sensitivity to low levels of aminobenzoyl-glutamate. May actually serve physiologically as a transporter for some other molecule, perhaps a dipeptide, and that it transports p-aminobenzoyl-glutamate as a secondary activity. The physiological ro [...] | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. | 0.996 |
| abgT | abgB | b1336 | b1337 | P-aminobenzoyl-glutamate transporter; Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl- glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p- aminobenzoate and glutamate. It seems also to increase the sensitivity to low levels of aminobenzoyl-glutamate. May actually serve physiologically as a transporter for some other molecule, perhaps a dipeptide, and that it transports p-aminobenzoyl-glutamate as a secondary activity. The physiological ro [...] | P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. | 0.989 |
| abgT | abgR | b1336 | b1339 | P-aminobenzoyl-glutamate transporter; Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl- glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p- aminobenzoate and glutamate. It seems also to increase the sensitivity to low levels of aminobenzoyl-glutamate. May actually serve physiologically as a transporter for some other molecule, perhaps a dipeptide, and that it transports p-aminobenzoyl-glutamate as a secondary activity. The physiological ro [...] | Putative DNA-binding transcriptional regulator of abgABT operon; Could be the regulator of the abg operon; Belongs to the LysR transcriptional regulatory family. | 0.907 |
| abgT | fnr | b1336 | b1334 | P-aminobenzoyl-glutamate transporter; Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl- glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p- aminobenzoate and glutamate. It seems also to increase the sensitivity to low levels of aminobenzoyl-glutamate. May actually serve physiologically as a transporter for some other molecule, perhaps a dipeptide, and that it transports p-aminobenzoyl-glutamate as a secondary activity. The physiological ro [...] | Oxygen-sensing anaerobic growth regulon transcriptional regulator FNR; Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O(2), is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration. | 0.474 |
| abgT | ogt | b1336 | b1335 | P-aminobenzoyl-glutamate transporter; Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl- glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p- aminobenzoate and glutamate. It seems also to increase the sensitivity to low levels of aminobenzoyl-glutamate. May actually serve physiologically as a transporter for some other molecule, perhaps a dipeptide, and that it transports p-aminobenzoyl-glutamate as a secondary activity. The physiological ro [...] | O-6-alkylguanine-DNA:cysteine-protein methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.871 |
| ada | aidB | b2213 | b4187 | Fused DNA-binding transcriptional dual regulator/O6-methylguanine-DNA methyltransferase; Involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs O6-methylguanine (O6-MeG) and O4- methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme (Cys-321). Also specifically repairs the Sp diastereomer of DNA methylphosphotriester lesions by the same mechanism, although the methyl transfer occurs onto a different cysteine residue (Cys-38). Cannot demeth [...] | DNA alkylation damage repair protein; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro. | 0.412 |
| ada | alkA | b2213 | b2068 | Fused DNA-binding transcriptional dual regulator/O6-methylguanine-DNA methyltransferase; Involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs O6-methylguanine (O6-MeG) and O4- methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme (Cys-321). Also specifically repairs the Sp diastereomer of DNA methylphosphotriester lesions by the same mechanism, although the methyl transfer occurs onto a different cysteine residue (Cys-38). Cannot demeth [...] | 3-methyl-adenine DNA glycosylase II; Hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions. | 0.965 |