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fabA fabA fadE fadE fadM fadM clsB clsB dhaM dhaM adhP adhP osmC osmC sodC sodC cfa cfa katE katE fadD fadD glpQ glpQ yfcF yfcF yfcG yfcG fadJ fadJ eutB eutB rpoS rpoS yghU yghU glpD glpD yiaY yiaY fadA fadA fadB fadB gldA gldA
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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fabABeta-hydroxydecanoyl thioester dehydrase; Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E- (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP. (172 aa)
fadEAcyl coenzyme A dehydrogenase; Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for E.coli to utilize dodecanoate or oleate as the sole carbon and energy source for growth. (814 aa)
fadMLong-chain acyl-CoA thioesterase III; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids; Belongs to the 4-hydroxybenzoyl-CoA thioesterase family. (132 aa)
clsBCardiolipin synthase 2; Catalyzes the phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Can also catalyze phosphatidyl group transfer to water to form phosphatidate. Belongs to the phospholipase D family. Cardiolipin synthase subfamily. ClsB sub-subfamily. (413 aa)
dhaMPutative 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. (472 aa)
adhPEthanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. (336 aa)
osmCLipoyl-dependent Cys-based peroxidase, hydroperoxide resistance; Preferentially metabolizes organic hydroperoxides over inorganic hydrogen peroxide; Belongs to the OsmC/Ohr family. (143 aa)
sodCSuperoxide dismutase, Cu, Zn, periplasmic; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. (173 aa)
cfaCyclopropane fatty acyl phospholipid synthase, SAM-dependent; Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. (382 aa)
katECatalase HPII, heme d-containing; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. (753 aa)
fadDacyl-CoA synthetase (long-chain-fatty-acid--CoA ligase); Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Activity is the highest with fatty acid substrates of > 10 carbon atoms. Is involved in the aerobic beta- oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source. (561 aa)
glpQGlycerophosphodiester phosphodiesterase, periplasmic; Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols. (358 aa)
yfcFGlutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. (214 aa)
yfcGGSH-dependent disulfide bond oxidoreductase; Exhibits a very robust glutathione (GSH)-dependent disulfide- bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the n [...] (215 aa)
fadJenoyl-CoA hydratase/epimerase and isomerase/3-hydroxyacyl-CoA dehydrogenase; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (714 aa)
eutBEthanolamine ammonia-lyase, heavy chain; Protein involved in amine catabolic process. (453 aa)
rpoSRNA polymerase, sigma S (sigma 38) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response. Controls, positively or negatively, the expression of several hundred genes, which are mainly involved in metabolism, transport, regulation and stress management. (330 aa)
yghUPutative S-transferase; Exhibits a robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also displays a modest GSH-dependent peroxidase activity toward several organic hydroperoxides, such as cumene hydroperoxide and linoleic acid 13(S)-hydroperoxide, but does not reduce H(2)O(2) or tert-butyl hydroperoxide at appreciable rates. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity toward [...] (288 aa)
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)
yiaYL-threonine dehydrogenase; Putative oxidoreductase. (383 aa)
fadA3-ketoacyl-CoA thiolase (thiolase I); Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. (387 aa)
fadBEnoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (729 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)
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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