node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
adhE | adhP | b1241 | b1478 | 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. | Ethanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.989 |
adhE | ahr | b1241 | b4269 | 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. | Broad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined. | 0.987 |
adhE | aldB | b1241 | b3588 | 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 dehydrogenase B; Catalyzes the NADP-dependent oxidation of diverse aldehydes such as chloroacetaldehyde, acetaldehyde, propionaldehyde, benzaldehyde, mafosfamide, 4-hydroperoxycyclophosphamide. Its preferred substrates are acetaldehyde and chloroacetaldehyde. | 0.991 |
adhE | atoB | b1241 | b2224 | 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. | acetyl-CoA acetyltransferase; Protein involved in fatty acid oxidation. | 0.982 |
adhE | eutD | b1241 | b2458 | 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. | Phosphate acetyltransferase; Ethanolamine utilization; homolog of Salmonella acetyl/butyryl P transferase; Protein involved in amine catabolic process. | 0.983 |
adhE | frmA | b1241 | b0356 | 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. | Alcohol dehydrogenase class III; Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. | 0.985 |
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 | pta | b1241 | b2297 | 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. | Phosphate acetyltransferase; Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP. In the N-terminal section; belongs to the CobB/CobQ family. | 0.992 |
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 |
adhP | adhE | b1478 | b1241 | Ethanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase 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. | 0.989 |
adhP | ahr | b1478 | b4269 | Ethanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. | Broad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined. | 0.952 |
adhP | aldB | b1478 | b3588 | Ethanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. | Aldehyde dehydrogenase B; Catalyzes the NADP-dependent oxidation of diverse aldehydes such as chloroacetaldehyde, acetaldehyde, propionaldehyde, benzaldehyde, mafosfamide, 4-hydroperoxycyclophosphamide. Its preferred substrates are acetaldehyde and chloroacetaldehyde. | 0.947 |
adhP | frmA | b1478 | b0356 | Ethanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. | Alcohol dehydrogenase class III; Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. | 0.943 |
adhP | mhpF | b1478 | b0351 | Ethanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol 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. | 0.757 |
adhP | pta | b1478 | b2297 | Ethanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. | Phosphate acetyltransferase; Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP. In the N-terminal section; belongs to the CobB/CobQ family. | 0.439 |
ahr | adhE | b4269 | b1241 | Broad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined. | 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. | 0.987 |
ahr | adhP | b4269 | b1478 | Broad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined. | Ethanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.952 |
ahr | aldB | b4269 | b3588 | Broad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined. | Aldehyde dehydrogenase B; Catalyzes the NADP-dependent oxidation of diverse aldehydes such as chloroacetaldehyde, acetaldehyde, propionaldehyde, benzaldehyde, mafosfamide, 4-hydroperoxycyclophosphamide. Its preferred substrates are acetaldehyde and chloroacetaldehyde. | 0.956 |
ahr | frmA | b4269 | b0356 | Broad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined. | Alcohol dehydrogenase class III; Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. | 0.942 |