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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
gloBHydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. (253 aa)    
Predicted Functional Partners:
gloA
Lactoylglutathione lyase.
 
 0.975
BVIR_151
Hypothetical protein.
      0.937
BVIR_3140
Putative metallo-hydrolase.
  
  
0.916
ldhA
D-lactate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
  
 
  0.906
BVIR_1583
Putative FAD-linked oxidoreductase.
     
 0.901
BVIR_2729
Putative FAD-linked oxidoreductase.
     
 0.901
grxD
Glutaredoxin-4; Belongs to the glutaredoxin family. Monothiol subfamily.
 
  
 0.656
BVIR_153
Methyltransferase domain protein.
     
 0.619
BVIR_96
Peptidase M15.
  
    0.531
gshB_1
Glutathione synthetase; Belongs to the prokaryotic GSH synthase family.
 
   
 0.501
Your Current Organism:
Blastochloris viridis
NCBI taxonomy Id: 1079
Other names: ATCC 19567, B. viridis, CCUG 30818, CCUG 7830, DSM 133, LMG 4321, LMG:4321, NBRC 102659, Rhodopseudomonas viridis, strain G. Drews F
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