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
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[Homology]
Score
frmBS-formylglutathione hydrolase; Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against two pNP-esters (pNP- acetate and pNP-propionate), alpha-naphthyl acetate and lactoylglutathione. (277 aa)    
Predicted Functional Partners:
frmA
Alcohol dehydrogenase class III; Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
 0.999
frmR
Regulator protein that represses frmRAB operon; Repressor of the frmRAB operon.
  
  
 0.991
yeiG
S-formylglutathione hydrolase; Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids.
  
 
0.914
fdoG
Formate dehydrogenase-O, large subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
   
 
 0.906
fdoI
Formate dehydrogenase-O, cytochrome b556 subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase.
     
  0.900
fdoH
Formate dehydrogenase-O, Fe-S subunit; Allows to use formate as major electron donor during aerobic respiration. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit (By similarity).
     
  0.900
rcnR
Transcriptional repressor of rcnA; Repressor of rcnA expression. Acts by binding specifically to the rcnA promoter in the absence of nickel and cobalt. In the presence of one of these metals, it has a weaker affinity for rcnA promoter. Belongs to the FrmR/RcnR family.
     
 0.558
purU
Formyltetrahydrofolate 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.
  
  
 0.492
gloB
Hydroxyacylglutathione 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.
   
  
 0.478
yfcG
GSH-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 [...]
  
    0.400
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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