node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
adhE | fucO | b1241 | b2799 | 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. | L-1,2-propanediol oxidoreductase; Protein involved in carbohydrate catabolic process and glycolate metabolic process; Belongs to the iron-containing alcohol dehydrogenase family. | 0.426 |
adhE | gldA | b1241 | b3945 | 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. | Glycerol dehydrogenase, NAD+ dependent; Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lac [...] | 0.900 |
adhE | glpK | b1241 | b3926 | 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. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP; Belongs to the FGGY kinase family. | 0.562 |
adhE | mgsA | b1241 | b0963 | 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. | Methylglyoxal synthase; Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. | 0.654 |
adhE | yahK | b1241 | b0325 | 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 into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use a ketone as substrate. Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of YahK has yet to be determined. Belongs to the zinc-containing alcohol dehydrogenase family. | 0.980 |
adhE | yqhD | b1241 | b3011 | 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 reductase, NADPH-dependent; NADP-dependent ADH activity; Belongs to the iron-containing alcohol dehydrogenase family. | 0.508 |
dhaK | dhaL | b1200 | b1199 | Dihydroxyacetone kinase, PTS-dependent, dihydroxyacetone-binding subunit; Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)- dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP. Binds covalently dihydroxyacetone in hemiaminal linkage. DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL- ADP is [...] | Dihydroxyacetone kinase, C-terminal domain; ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL- ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK. DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PT [...] | 0.999 |
dhaK | dhaM | b1200 | b1198 | Dihydroxyacetone kinase, PTS-dependent, dihydroxyacetone-binding subunit; Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)- dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP. Binds covalently dihydroxyacetone in hemiaminal linkage. DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL- ADP is [...] | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | 0.999 |
dhaK | gldA | b1200 | b3945 | Dihydroxyacetone kinase, PTS-dependent, dihydroxyacetone-binding subunit; Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)- dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP. Binds covalently dihydroxyacetone in hemiaminal linkage. DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL- ADP is [...] | Glycerol dehydrogenase, NAD+ dependent; Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lac [...] | 0.935 |
dhaL | dhaK | b1199 | b1200 | Dihydroxyacetone kinase, C-terminal domain; ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL- ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK. DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PT [...] | Dihydroxyacetone kinase, PTS-dependent, dihydroxyacetone-binding subunit; Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)- dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP. Binds covalently dihydroxyacetone in hemiaminal linkage. DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL- ADP is [...] | 0.999 |
dhaL | dhaM | b1199 | b1198 | Dihydroxyacetone kinase, C-terminal domain; ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL- ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK. DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PT [...] | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | 0.999 |
dhaL | gldA | b1199 | b3945 | Dihydroxyacetone kinase, C-terminal domain; ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL- ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK. DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PT [...] | Glycerol dehydrogenase, NAD+ dependent; Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lac [...] | 0.944 |
dhaM | dhaK | b1198 | b1200 | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | Dihydroxyacetone kinase, PTS-dependent, dihydroxyacetone-binding subunit; Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)- dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP. Binds covalently dihydroxyacetone in hemiaminal linkage. DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL- ADP is [...] | 0.999 |
dhaM | dhaL | b1198 | b1199 | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | Dihydroxyacetone kinase, C-terminal domain; ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL- ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK. DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PT [...] | 0.999 |
dhaM | gldA | b1198 | b3945 | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | Glycerol dehydrogenase, NAD+ dependent; Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lac [...] | 0.957 |
dhaM | glpK | b1198 | b3926 | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP; Belongs to the FGGY kinase family. | 0.500 |
fucO | adhE | b2799 | b1241 | L-1,2-propanediol oxidoreductase; Protein involved in carbohydrate catabolic process and glycolate metabolic process; Belongs to the iron-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. | 0.426 |
fucO | gldA | b2799 | b3945 | L-1,2-propanediol oxidoreductase; Protein involved in carbohydrate catabolic process and glycolate metabolic process; Belongs to the iron-containing alcohol dehydrogenase family. | Glycerol dehydrogenase, NAD+ dependent; Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lac [...] | 0.986 |
fucO | mgsA | b2799 | b0963 | L-1,2-propanediol oxidoreductase; Protein involved in carbohydrate catabolic process and glycolate metabolic process; Belongs to the iron-containing alcohol dehydrogenase family. | Methylglyoxal synthase; Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. | 0.732 |
fucO | yahK | b2799 | b0325 | L-1,2-propanediol oxidoreductase; Protein involved in carbohydrate catabolic process and glycolate metabolic process; Belongs to the iron-containing alcohol dehydrogenase family. | Broad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use a ketone as substrate. Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of YahK has yet to be determined. Belongs to the zinc-containing alcohol dehydrogenase family. | 0.695 |