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
luxSConserved hypothetical 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. (158 aa)    
Predicted Functional Partners:
DR_1451
5`-methylthioadenosine/S-adenosylhomocysteine nuclosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.
 
 
 0.980
MetH
5-methyltetrahydrofolate--homocysteine 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.
    
 0.944
DR_0873
O-acetylhomoserine (thiol)-lyase; Similar to SP:P50125 PID:633761 percent identity: 73.78; identified by sequence similarity; putative.
     
 0.903
DR_2186
O-acetylhomoserine (thiol)-lyase/O-acetylserine (thiol)-lyase; Similar to PID:1526549 percent identity: 60.45; identified by sequence similarity; putative.
     
 0.903
DR_1452
Aminotransferase, class I; Similar to SP:Q08432 GB:S61781 PID:975351 PID:1934779 PID:1934787 percent identity: 54.03; identified by sequence similarity; putative.
     
  0.900
DR_0789
O-acetylserine (thiol)-lyase; Similar to SP:Q43317 percent identity: 69.87; identified by sequence similarity; putative; Belongs to the cysteine synthase/cystathionine beta- synthase family.
 
 
 0.879
DR_1278
Homoserine dehydrogenase; Similar to SP:P08499 GB:Y00476 PID:297383 PID:40503 percent identity: 56.69; identified by sequence similarity; putative.
    
 0.813
ilvA
Threonine dehydratase, biosynthetic; 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.
     
 0.807
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
     
  0.800
lspA
Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family.
     
 0.655
Your Current Organism:
Deinococcus radiodurans
NCBI taxonomy Id: 243230
Other names: D. radiodurans R1, Deinococcus radiodurans R1, Deinococcus radiodurans str. R1
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