|dkgB||Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG) (267 aa)|| |
Predicted Functional Partners:
Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2- keto-D-gluconate (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its physiological function. Inactive towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D- fructose and L-sorbose. Activity with NAD is very low
| || || ||0.980
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, lactaldehyde and 1,2-propanediol, respectively.
| || || || || || ||0.929
Uncharacterized protein YagA; Pseudogene, CP4-6 prophage;Phage or Prophage Related
| || || || || || || ||0.878
Catalyzes the stereospecific, NADPH-dependent reduction of L- glyceraldehyde 3-phosphate (L-GAP). The physiological role of gpr is the detoxification of L-GAP, which may be formed by non-enzymatic racemization of GAP. Also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
| || || || || ||0.857
Displays esterase activity toward pNP-butyrate.
| || || || || ||0.737
May be involved in a fimbrial system chaperoned by YqiH and exported by YqiG
| || || || || || || ||0.673
Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
| || || || || || ||0.657
annotation not available
| || || || || || || ||0.607
Not known; probable catabolic enzyme
| || || || ||0.575
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.
| || || || || || ||0.550