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
ilvEBranched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (308 aa)    
Predicted Functional Partners:
leuA
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
  
 0.967
ilvA
L-threonine dehydratase; 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.
  
 
 0.950
lpdA
Dihydrolipoyl dehydrogenase.
     
 0.938
F897_00836
Homoserine dehydrogenase.
  
 
 0.927
panB
3-methyl-2-oxobutanoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family.
     
 0.910
ilvD
Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
  
 0.907
ilvD-2
Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
  
 0.907
F897_02557
Aminotran_1_2 domain-containing protein.
     
 0.902
thrB
Homoserine kinase; Belongs to the pseudomonas-type ThrB family.
     
 0.900
F897_01397
Phosphoserine phosphatase/homoserine phosphotransferase.
     
 0.899
Your Current Organism:
Acinetobacter variabilis
NCBI taxonomy Id: 70346
Other names: A. variabilis, Acinetobacter genomosp. 15, Acinetobacter genomospecies 15, Acinetobacter sp. 15, Acinetobacter sp. NIPH 2171, Acinetobacter variabilis Krizova et al. 2015, CCM 8555, CCUG 26390, CIP 110486, strain NIPH 2171
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.