close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
ilvAThreonine dehydratase, biosynthetic; 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. (529 aa)    
Predicted Functional Partners:
ACS18482.1
KEGG: pna:Pnap_2230 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit.
 
 
 0.949
ACS20848.1
PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: cti:RALTA_B1800 putative pyridoxal-5'-phosphate-dependent enzyme, beta family; putative threonine synthase.
  
 
 0.941
trpB
Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
 0.933
leuB
3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
 
 
 0.932
ACS19526.1
PFAM: aminotransferase class V; KEGG: dac:Daci_3052 serine--glyoxylate transaminase.
  
 0.924
trpA
Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
  
 
 0.922
ACS22842.1
PFAM: isocitrate/isopropylmalate dehydrogenase; KEGG: bra:BRADO2458 putative 3-isopropylmalate dehydrogenase (LeuB).
  
 
 0.916
ACS17239.1
Threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; aminotransferase class I and II; KEGG: pna:Pnap_3651 threonine aldolase.
  
 
 0.910
ACS22049.1
PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: azc:AZC_1923 threonine aldolase.
  
 
 0.910
ACS17580.1
PFAM: glycine hydroxymethyltransferase; aminotransferase class I and II; aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: sil:SPO3529 serine hydroxymethyltransferase.
    
 0.908
Your Current Organism:
Variovorax paradoxus S110
NCBI taxonomy Id: 543728
Other names: V. paradoxus S110, Variovorax paradoxus str. S110, Variovorax paradoxus strain S110
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.