STRINGSTRING
thrA thrA ilvH ilvH ilvN ilvN ilvM ilvM lysC lysC glnD glnD purU purU tyrR tyrR gcvR gcvR pheA pheA relA relA serA serA spoT spoT
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
thrABifunctional: aspartokinase I (N-terminal); homoserine dehydrogenase I (C-terminal); Protein involved in threonine biosynthetic process, methionine biosynthetic process and homoserine biosynthetic process. (820 aa)
ilvHAcetolactate synthase III, valine sensitive, small subunit. (163 aa)
ilvNAcetolactate synthase I, valine sensitive, small subunit. (96 aa)
ilvMPseudogene, acetolactate synthase 2 large subunit, valine-insensitive; acetolactate synthase II, large subunit, cryptic, interrupted. (87 aa)
lysCLysine-sensitive aspartokinase 3; Aspartokinase III, lysine sensitive; Protein involved in lysine biosynthetic process via diaminopimelate and homoserine biosynthetic process. (449 aa)
glnDUridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. (890 aa)
purUFormyltetrahydrofolate hydrolase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). Provides the major source of formate for the PurT-dependent synthesis of 5'- phosphoribosyl-N-formylglycinamide (FGAR) during aerobic growth. Has a role in regulating the one-carbon pool. (280 aa)
tyrRAromatic amino acid biosynthesis and transport regulon transcriptional regulator; Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP ge [...] (513 aa)
gcvRTranscriptional repressor, regulatory protein accessory to GcvA; Negative transcriptional regulator of the glycine cleavage system operon (GCV). Does not autoregulate its own expression. It is not yet known how GcvR acts as a repressor. It does not seem to bind DNA. It could interact with GcvA and suppress its activatory activity. (190 aa)
pheAChorismate mutase and prephenate dehydratase, P-protein; Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. (386 aa)
relA(p)ppGpp synthetase I/GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response which coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c-di-GMP induces it. ppGpp activates transcription of CsrA-antagonistic small RNAs CsrB and CsrC, which d [...] (744 aa)
serAD-3-phosphoglycerate dehydrogenase; Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate. (410 aa)
spoTBifunctional (p)ppGpp synthetase II/ guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response which coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the synthesis and degradation of ppGpp. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c-di-GMP induces it. ppGpp activates transcription of CsrA-antagonistic s [...] (702 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
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.