node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
adhE | eutE | b1241 | b2455 | Acetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. | Aldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. | 0.948 |
adhE | fadI | b1241 | b2342 | Acetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. | beta-ketoacyl-CoA thiolase, anaerobic, subunit; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. Belongs to the thiolase-like superfamily. Thiolase family. | 0.416 |
adhE | mhpF | b1241 | b0351 | Acetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. | acetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. | 0.990 |
adhE | pflB | b1241 | b0903 | Acetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. | Formate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. | 0.997 |
adhE | tdcE | b1241 | b3114 | Acetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. | Pyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate. Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily. | 0.992 |
eutE | adhE | b2455 | b1241 | Aldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. | Acetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. | 0.948 |
eutE | mhpF | b2455 | b0351 | Aldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. | acetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. | 0.989 |
eutE | pflB | b2455 | b0903 | Aldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. | Formate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. | 0.952 |
eutE | tdcE | b2455 | b3114 | Aldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. | Pyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate. Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily. | 0.948 |
fadI | adhE | b2342 | b1241 | beta-ketoacyl-CoA thiolase, anaerobic, subunit; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. Belongs to the thiolase-like superfamily. Thiolase family. | Acetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. | 0.416 |
fadI | mhpF | b2342 | b0351 | beta-ketoacyl-CoA thiolase, anaerobic, subunit; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. Belongs to the thiolase-like superfamily. Thiolase family. | acetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. | 0.927 |
fadI | pflB | b2342 | b0903 | beta-ketoacyl-CoA thiolase, anaerobic, subunit; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. Belongs to the thiolase-like superfamily. Thiolase family. | Formate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. | 0.805 |
fadI | tdcE | b2342 | b3114 | beta-ketoacyl-CoA thiolase, anaerobic, subunit; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. Belongs to the thiolase-like superfamily. Thiolase family. | Pyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate. Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily. | 0.807 |
mhpF | adhE | b0351 | b1241 | acetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. | Acetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. | 0.990 |
mhpF | eutE | b0351 | b2455 | acetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. | Aldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. | 0.989 |
mhpF | fadI | b0351 | b2342 | acetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. | beta-ketoacyl-CoA thiolase, anaerobic, subunit; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. Belongs to the thiolase-like superfamily. Thiolase family. | 0.927 |
mhpF | pflB | b0351 | b0903 | acetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. | Formate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. | 0.979 |
mhpF | tdcE | b0351 | b3114 | acetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. | Pyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate. Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily. | 0.977 |
pflB | adhE | b0903 | b1241 | Formate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. | Acetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. | 0.997 |
pflB | eutE | b0903 | b2455 | Formate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. | Aldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. | 0.952 |