Putative oxidoreductase.

Putative Zn-binding dehydrogenase; To K.pneumoniae SorE.

NADH:ubiquinone oxidoreductase, fused CD subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.

Putative oxidoreductase.

Glycine decarboxylase, PLP-dependent, subunit P of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.

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 oxidoreductase; To H.influenzae HI_0933.

Putative Zn-dependent NAD(P)-binding oxidoreductase; Catalyzes the NAD(+)-dependent oxidation of the hydroxyl group at C3 of D-gulosides leading to 3-dehydro-D-gulosides. Probably functions in a metabolic pathway that transforms D-gulosides to D- glucosides. Is also able to catalyze the reverse reactions, i.e. the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D- gulosides leading to D-gulosides. In vitro, can oxidize D-gulose and methyl beta-D-guloside, and reduce methyl alpha-3-dehydro-D-guloside and methyl beta-3-dehydro-D-guloside. However, the actual specific physiol [...]

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. Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily.