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; 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. (513 aa)    
Predicted Functional Partners:
ilvH
Acetolactate synthase 3 regulatory subunit; With IlvI catalyzes the formation of 2-acetolactate from pyruvate, the small subunit is required for full activity and valine sensitivity; E.coli produces 3 isoenzymes of acetolactate synthase which differ in specificity to substrates, valine sensitivity and affinity for cofactors; also known as acetolactate synthase 3 small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.966
AKO51834.1
Threonine synthase; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.942
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.
 
 
 0.941
AKO51672.1
Acetolactate synthase 3 catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.933
AKO53050.1
Acetolactate synthase catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate; also known as acetolactate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.933
trpB
Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
 0.927
AKO53051.1
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.923
AKO54140.1
Acetolactate synthase; Catalyzes the condensation of two pyruvates to form acetolactate, implicated in pH homeostasis via the acetoin-2,3-butanediol pathway or in valine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family.
  
 0.922
AKO51303.1
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family.
  
 0.922
AKO53760.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family.
  
 0.922
Your Current Organism:
Marinobacter psychrophilus
NCBI taxonomy Id: 330734
Other names: CGMCC 1.6499, JCM 14643, M. psychrophilus, Marinobacter psychrophilus Zhang et al. 2008, Marinobacter sp. BSi20041, strain 20041
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