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
srpHSerine acetyltransferase. (308 aa)    
Predicted Functional Partners:
BW43_03733
Cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family.
 
 0.971
cysM
Cysteine synthase B; Belongs to the cysteine synthase/cystathionine beta- synthase family.
 
 0.970
BW43_03118
Putative O-acetylserine (thiol)-lyase.
 
 0.965
BW43_01254
Cystathionine beta-lyase.
 
 0.954
BW43_05403
Putative cysteine synthase.
  
 0.920
cysS
cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.909
BW43_04823
Homoserine dehydrogenase.
  
  
 0.817
metH
B12-dependent methionine synthase; 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.
    
 0.813
BW43_04642
Phosphoserine phosphatase.
    
 0.806
BW43_04589
Putative homocysteine synthase.
    
 0.753
Your Current Organism:
Pseudomonas sp. RIT357
NCBI taxonomy Id: 1470593
Other names: P. sp. RIT357
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