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
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Textmining
[Homology]
Score
ilvAThreonine ammonia-lyase, biosynthetic, long form; 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. (526 aa)    
Predicted Functional Partners:
AGA29135.1
PFAM: ACT domain; Small subunit of acetolactate synthase; TIGRFAM: acetolactate synthase, small subunit.
 
 
 0.971
AGA26107.1
Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme.
  
 
 0.934
AGA28987.1
Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase.
  
 
 0.934
AGA30739.1
Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase.
  
 
 0.934
AGA25957.1
Acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type.
 
 0.931
trpB
Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
 0.929
AGA31243.1
Cystathionine beta-synthase; PFAM: CBS domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthase A; cysteine synthases; cystathionine beta-synthase.
    
0.928
AGA28538.1
Threonine dehydratase; PFAM: Pyridoxal-phosphate dependent enzyme.
  
  
 
0.924
AGA26587.1
Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family.
  
 0.922
AGA28159.1
Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family.
  
 0.922
Your Current Organism:
Singulisphaera acidiphila
NCBI taxonomy Id: 886293
Other names: S. acidiphila DSM 18658, Singulisphaera acidiphila DSM 18658, Singulisphaera acidiphila MOB10, Singulisphaera acidiphila str. DSM 18658, Singulisphaera acidiphila strain DSM 18658
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.