STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
yeaEAldo-keto reductase, methylglyoxal to acetol, NADPH-dependent; Putative an aldehyde reductase. (284 aa)    
Predicted Functional Partners:
mipA
Scaffolding protein for murein synthesizing machinery; May serve as a scaffold protein required for the formation of a complex with MrcB/PonB and MltA, this complex could play a role in enlargement and septation of the murein sacculus.
     
 0.683
gldA
Glycerol 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 [...]
     
 0.679
yahK
Broad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use a ketone as substrate. Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of YahK has yet to be determined. Belongs to the zinc-containing alcohol dehydrogenase family.
     
 0.629
yqhD
Aldehyde reductase, NADPH-dependent; NADP-dependent ADH activity; Belongs to the iron-containing alcohol dehydrogenase family.
  
  
 0.624
ycgY
Uncharacterized protein.
      
 0.622
yncH
IPR020099 family protein.
      
 0.622
yqhC
Transcriptional activator of yqhD; Putative ARAC-type regulatory protein; Protein involved in transcription activator activity and transcription.
  
   
 0.606
ydjG
Methylglyoxal reductase, NADH-dependent; Catalyzes the NADH-dependent reduction of methylglyoxal (2- oxopropanal) in vitro. It is not known if this activity has physiological significance. Cannot use NADPH as a cosubstrate. Seems to play some role in intestinal colonization.
 
 
0.574
yajO
2-carboxybenzaldehyde reductase; Catalyzes the conversion of ribulose 5-phosphate (Ru5P) to 1- deoxy-D-xylulose 5-phosphate (DXP), providing a direct route from pentoses to terpenes. May play a role in biosynthesis of DXP under conditions of thiamine starvation; Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily.
 
 
0.562
fucO
L-1,2-propanediol oxidoreductase; Protein involved in carbohydrate catabolic process and glycolate metabolic process; Belongs to the iron-containing alcohol dehydrogenase family.
   
 
 0.546
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 (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.