node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ybdR | ycjS | b0608 | b1315 | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | Putative nadh-binding oxidoreductase; Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of [...] | 0.688 |
ybdR | ydbC | b0608 | b1406 | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | Putative nad(p)-binding oxidoreductase; Catalyzes the NAD(P)H-dependent reduction of pyridoxal to pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize pyridoxine or pyridoxamine . Has Kemp eliminase activity towards the non-physiological substrate 5-nitrobenzisoxazole, producing 4-nitro-2-cyanophenol; this activity is not considered to be physiologically relevant | 0.732 |
ybdR | ydgJ | b0608 | b1624 | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | annotation not available | 0.685 |
ybdR | ydjJ | b0608 | b1774 | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | Putative zn-dependent nad(p)-binding oxidoreductase; Uncharacterized zinc-type alcohol dehydrogenase-like protein YdjJ; Putative oxidoreductase | 0.408 |
ybdR | ygcW | b0608 | b2774 | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | Putative deoxygluconate dehydrogenase; Belongs to the short-chain dehydrogenases/reductases (SDR) family | 0.739 |
ybdR | yggP | b0608 | b4465 | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | Putative zinc-binding dehydrogenase yggp; To K.pneumoniae SorE | 0.773 |
ybdR | ygjR | b0608 | b3087 | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | Putative nad(p)-dependent dehydrogenase; Belongs to the Gfo/Idh/MocA family | 0.712 |
ybdR | yhiN | b0608 | b3492 | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | Uncharacterized protein YhiN; Putative enzyme; Not classified; To H.influenzae HI_0933 | 0.731 |
ybdR | yjhC | b0608 | b4280 | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | Gfo/idh/moca family putative oxidoreductase. nad(p)-dependent; Belongs to the Gfo/Idh/MocA family | 0.692 |
ycjS | ybdR | b1315 | b0608 | Putative nadh-binding oxidoreductase; Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of [...] | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | 0.688 |
ycjS | ydbC | b1315 | b1406 | Putative nadh-binding oxidoreductase; Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of [...] | Putative nad(p)-binding oxidoreductase; Catalyzes the NAD(P)H-dependent reduction of pyridoxal to pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize pyridoxine or pyridoxamine . Has Kemp eliminase activity towards the non-physiological substrate 5-nitrobenzisoxazole, producing 4-nitro-2-cyanophenol; this activity is not considered to be physiologically relevant | 0.732 |
ycjS | ydjJ | b1315 | b1774 | Putative nadh-binding oxidoreductase; Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of [...] | Putative zn-dependent nad(p)-binding oxidoreductase; Uncharacterized zinc-type alcohol dehydrogenase-like protein YdjJ; Putative oxidoreductase | 0.780 |
ycjS | ygcW | b1315 | b2774 | Putative nadh-binding oxidoreductase; Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of [...] | Putative deoxygluconate dehydrogenase; Belongs to the short-chain dehydrogenases/reductases (SDR) family | 0.779 |
ycjS | yggP | b1315 | b4465 | Putative nadh-binding oxidoreductase; Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of [...] | Putative zinc-binding dehydrogenase yggp; To K.pneumoniae SorE | 0.775 |
ycjS | yhiN | b1315 | b3492 | Putative nadh-binding oxidoreductase; Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of [...] | Uncharacterized protein YhiN; Putative enzyme; Not classified; To H.influenzae HI_0933 | 0.733 |
ydbC | ybdR | b1406 | b0608 | Putative nad(p)-binding oxidoreductase; Catalyzes the NAD(P)H-dependent reduction of pyridoxal to pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize pyridoxine or pyridoxamine . Has Kemp eliminase activity towards the non-physiological substrate 5-nitrobenzisoxazole, producing 4-nitro-2-cyanophenol; this activity is not considered to be physiologically relevant | Uncharacterized zinc-type alcohol dehydrogenase-like protein YbdR; Putative oxidoreductase | 0.732 |
ydbC | ycjS | b1406 | b1315 | Putative nad(p)-binding oxidoreductase; Catalyzes the NAD(P)H-dependent reduction of pyridoxal to pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize pyridoxine or pyridoxamine . Has Kemp eliminase activity towards the non-physiological substrate 5-nitrobenzisoxazole, producing 4-nitro-2-cyanophenol; this activity is not considered to be physiologically relevant | Putative nadh-binding oxidoreductase; Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of [...] | 0.732 |
ydbC | ydgJ | b1406 | b1624 | Putative nad(p)-binding oxidoreductase; Catalyzes the NAD(P)H-dependent reduction of pyridoxal to pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize pyridoxine or pyridoxamine . Has Kemp eliminase activity towards the non-physiological substrate 5-nitrobenzisoxazole, producing 4-nitro-2-cyanophenol; this activity is not considered to be physiologically relevant | annotation not available | 0.731 |
ydbC | ydjJ | b1406 | b1774 | Putative nad(p)-binding oxidoreductase; Catalyzes the NAD(P)H-dependent reduction of pyridoxal to pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize pyridoxine or pyridoxamine . Has Kemp eliminase activity towards the non-physiological substrate 5-nitrobenzisoxazole, producing 4-nitro-2-cyanophenol; this activity is not considered to be physiologically relevant | Putative zn-dependent nad(p)-binding oxidoreductase; Uncharacterized zinc-type alcohol dehydrogenase-like protein YdjJ; Putative oxidoreductase | 0.735 |
ydbC | ygcW | b1406 | b2774 | Putative nad(p)-binding oxidoreductase; Catalyzes the NAD(P)H-dependent reduction of pyridoxal to pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize pyridoxine or pyridoxamine . Has Kemp eliminase activity towards the non-physiological substrate 5-nitrobenzisoxazole, producing 4-nitro-2-cyanophenol; this activity is not considered to be physiologically relevant | Putative deoxygluconate dehydrogenase; Belongs to the short-chain dehydrogenases/reductases (SDR) family | 0.757 |