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
luxSS-ribosylhomocysteine lyase (Autoinducer-2 production protein luxS) (AI-2 synthesis protein); Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. (154 aa)    
Predicted Functional Partners:
metH
Methionine synthase (5-methyltetrahydrofolate:L-homocysteine S-methyltransferase); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
    
 0.964
metB
Cystathionine gamma-synthase (O-succinylhomoserine (thiol)-lyase).
 
 
 0.950
malY
Cysteine-S-conjugate beta-lyase; L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate.
  
  
  0.911
cys1
Cysteine synthase 1; Belongs to the cysteine synthase/cystathionine beta- synthase family.
  
 
 0.850
cysK
Cysteine synthase (O-acetylserine sulfhydrylase); O3-acetyl-L-serine + H2S = L-cysteine + acetate. COFACTOR: Pyridoxal phosphate Belongs to the cysteine synthase/cystathionine beta-synthase family.
  
 
 0.850
cys2
Cysteine synthase 2; Formation of cysteine from O-acetyl-serine and hydrogen sulfide. O3-acetyl-L-serine + H2S = L-cysteine + acetate; Belongs to the cysteine synthase/cystathionine beta- synthase family.
  
 
 0.850
thrA/hom
L-Homoserine + NAD+ <=> L-Aspartate 4-semialdehyde + NADH + H+ and L-Homoserine + NADP+ <=> L-Aspartate 4-semialdehyde + NADPH + H+.
     
 0.812
ilvA
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
     
 0.811
serB/thrH
Phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; O-Phospho-L-serine + H2O <=> L-Serine + Orthophosphate and D-O-Phosphoserine + H2O <=> D-Serine + Orthophosphate.
    
  0.800
metE
Methionine synthase, vitamin-B12 independent; 5-Methyltetrahydropteroyltri-L-glutamate + L-Homocysteine <=> Tetrahydropteroyltri-L-glutamate + L-Methionine.
    
 0.645
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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