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
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Co-occurrence
Co-expression
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[Homology]
Score
AGA67881.1Putative ring-cleavage extradiol dioxygenase. (121 aa)    
Predicted Functional Partners:
AGA68572.1
Lactoylglutathione lyase-like lyase; PFAM: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.
 
 
 0.924
AGA70870.1
Lactoylglutathione lyase-like lyase.
  
 
 0.912
AGA68328.1
Lactate dehydrogenase-like oxidoreductase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain.
   
 
  0.900
AGA69930.1
Zn-dependent hydrolase, glyoxylase; PFAM: Metallo-beta-lactamase superfamily.
    
  0.900
AGA70593.1
Zn-dependent hydrolase, glyoxylase; PFAM: Metallo-beta-lactamase superfamily.
    
  0.900
trpB
Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
     
  0.800
ilvA
L-threonine ammonia-lyase; 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.
     
  0.800
AGA68379.1
Threonine dehydratase, medium form; PFAM: Pyridoxal-phosphate dependent enzyme.
     
  0.800
AGA70136.1
L-serine dehydratase, iron-sulfur-dependent, alpha subunit; PFAM: Serine dehydratase alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
  0.800
AGA70137.1
L-serine dehydratase, iron-sulfur-dependent, beta subunit; PFAM: ACT domain; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
  0.800
Your Current Organism:
Desulfitobacterium dichloroeliminans
NCBI taxonomy Id: 871963
Other names: D. dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans DCA1, Desulfitobacterium dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans LMG P21439, Desulfitobacterium dichloroeliminans str. LMG P-21439, Desulfitobacterium dichloroeliminans strain LMG P-21439
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