STRINGSTRING
fusA fusA yiaY yiaY idnD idnD aceE aceE gloB gloB eda eda edd edd flhD flhD tktB tktB tktA tktA tdcE tdcE
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
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
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
fusAProtein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...] (704 aa)
yiaYL-threonine dehydrogenase; Putative oxidoreductase. (383 aa)
idnDL-idonate 5-dehydrogenase, NAD-binding; Catalyzes the NADH/NADPH-dependent oxidation of L-idonate to 5-ketogluconate (5KG); Belongs to the zinc-containing alcohol dehydrogenase family. (343 aa)
aceEPyruvate dehydrogenase, decarboxylase component E1, thiamine triphosphate-binding; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (887 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)
edaKHG/KDPG aldolase; Involved in the degradation of glucose via the Entner- Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-Keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D- glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with si-facial selectivity. It accepts some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate, and fluorobutanoate. It has a preference for the S-configuration at C2 of the electrophile. (213 aa)
edd6-phosphogluconate dehydratase; Catalyzes the dehydration of 6-phospho-D-gluconate to 2- dehydro-3-deoxy-6-phospho-D-gluconate. (603 aa)
flhDFlagellar class II regulon transcriptional activator, with FlhC; Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways. (116 aa)
tktBTransketolase 2, thiamine triphosphate-binding; Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate (By similarity). (667 aa)
tktATransketolase 1, thiamine triphosphate-binding; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Thus, catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose- 5-phosphate. (663 aa)
tdcEPyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate. Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily. (764 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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