STRINGSTRING
yqhD yqhD araC araC mhpF mhpF adhE adhE ldhA ldhA adhP adhP grxD grxD astD astD pta pta eutG eutG eutE eutE scpA scpA argK argK scpB scpB scpC scpC aldB aldB yiaY yiaY
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:
yqhDAldehyde reductase, NADPH-dependent; NADP-dependent ADH activity; Belongs to the iron-containing alcohol dehydrogenase family. (387 aa)
araCAra regulon transcriptional activator; Transcription factor that regulates the expression of several genes involved in the transport and metabolism of L-arabinose. Functions both as a positive and a negative regulator. In the presence of arabinose, activates the expression of the araBAD, araE, araFGH and araJ promoters. In the absence of arabinose, negatively regulates the araBAD operon. Represses its own transcription. Acts by binding directly to DNA. (292 aa)
mhpFacetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. (316 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)
adhPEthanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. (336 aa)
grxDGlutaredoxin-4; Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters; Belongs to the glutaredoxin family. Monothiol subfamily. (115 aa)
astDSuccinylglutamic semialdehyde dehydrogenase; Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. Also shows activity with decanal or succinic semialdehyde as the electron donor and NAD as the electron acceptor. No activity is detected with NADP as the electron acceptor. Therefore, is an aldehyde dehydrogenase with broad substrate specificity. (492 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)
eutGEthanol dehydrogenase involved in ethanolamine utilization; May act on the acetaldehyde produced from the degradation of ethanolamine; Belongs to the iron-containing alcohol dehydrogenase family. (395 aa)
eutEAldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. (467 aa)
scpAmethylmalonyl-CoA mutase; Catalyzes the interconversion of succinyl-CoA and methylmalonyl-CoA. Could be part of a pathway that converts succinate to propionate. (714 aa)
argKMembrane ATPase/protein kinase; Binds and hydrolyzes GTP. Likely functions as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) ScpA and reactivation of the enzyme during catalysis; Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB subfamily. (331 aa)
scpBmethylmalonyl-CoA decarboxylase, biotin-independent; Catalyzes the decarboxylation of (R)-methylmalonyl-CoA to propionyl-CoA. Could be part of a pathway that converts succinate to propanoate. (261 aa)
scpCpropionyl-CoA:succinate CoA transferase; Catalyzes the transfer of coenzyme A from propionyl-CoA to succinate. Could be part of a pathway that converts succinate to propionate; Belongs to the acetyl-CoA hydrolase/transferase family. (492 aa)
aldBAldehyde dehydrogenase B; Catalyzes the NADP-dependent oxidation of diverse aldehydes such as chloroacetaldehyde, acetaldehyde, propionaldehyde, benzaldehyde, mafosfamide, 4-hydroperoxycyclophosphamide. Its preferred substrates are acetaldehyde and chloroacetaldehyde. (512 aa)
yiaYL-threonine dehydrogenase; Putative oxidoreductase. (383 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 (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.