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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AGA28987.1Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. (483 aa)    
Predicted Functional Partners:
ilvA
Threonine 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.
  
 
 0.934
AGA28538.1
Threonine dehydratase; PFAM: Pyridoxal-phosphate dependent enzyme.
  
 
 0.934
AGA26107.1
Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme.
  
  
 
0.928
AGA30739.1
Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase.
  
  
 
0.927
AGA24491.1
Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.
   
 0.916
AGA25540.1
Threonine aldolase; PFAM: Beta-eliminating lyase.
   
 0.916
AGA30055.1
PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain.
 
 
 0.846
AGA30053.1
PFAM: ACT domain; Amino acid kinase family; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase.
  
 
 0.766
leuD
3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
  
  
 0.752
ilvC
Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
 
  
 0.690
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.