STRINGSTRING
glpD glpD gldA gldA fdhF fdhF frdA frdA hchA hchA dld dld ackA ackA pta pta hycB hycB lldD lldD glpK glpK lpd lpd gloB gloB pflB pflB mgsA mgsA adhE adhE ldhA ldhA aldA aldA gloA gloA pykF pykF
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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gene neighborhood
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Your Input:
glpDSn-glycerol-3-phosphate dehydrogenase, aerobic, FAD/NAD(P)-binding; Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor. (501 aa)
gldAGlycerol 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 [...] (367 aa)
fdhFFormate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. (715 aa)
frdAAnaerobic fumarate reductase catalytic and NAD/flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (602 aa)
hchAProtein/nucleic acid deglycase 1; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, aspartate aminotransferase, [...] (283 aa)
dldD-lactate dehydrogenase, FAD-binding, NADH independent; Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane. (571 aa)
ackAAcetate kinase A and propionate kinase 2; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. During anaerobic growth of the organism, this enzyme is also involved in the synthesis of most of the ATP formed catabolically; Belongs to the acetokinase family. (400 aa)
ptaPhosphate 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. (714 aa)
hycBHydrogenase 3, Fe-S subunit; Probable electron transfer protein for hydrogenase 3. (203 aa)
lldDL-lactate dehydrogenase, FMN-linked; Catalyzes the conversion of L-lactate to pyruvate. Seems to be a primary dehydrogenase in the respiratory chain. To a lesser extent, can also oxidize DL-alpha-hydroxybutyrate, but not D-lactate. (396 aa)
glpKGlycerol 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. (502 aa)
lpdDihydrolipoyl dehydrogenase; Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. (474 aa)
gloBHydroxyacylglutathione hydrolase; Type II glyoxalase that catalyzes the hydrolysis of (R)-S- lactoylglutathione to (R)-lactate and glutathione. Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli. The two isoenzymes have additive effects and ensure maximal MG degradation. (251 aa)
pflBFormate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. (760 aa)
mgsAMethylglyoxal synthase; Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. (152 aa)
adhEAcetaldehyde 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. (891 aa)
ldhAFermentative D-lactate dehydrogenase, NAD-dependent; Fermentative lactate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (329 aa)
aldAAldehyde dehydrogenase A, NAD-linked; Acts on lactaldehyde as well as other aldehydes. (479 aa)
gloAGlyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response. (135 aa)
pykFPyruvate kinase I (formerly F), fructose stimulated; Protein involved in glycolysis, fermentation and anaerobic respiration. (470 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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