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
thrC-2Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (361 aa)    
Predicted Functional Partners:
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
  
 
 0.997
hom
Homoserine dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
 
 
 0.970
CCH86438.1
L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 
0.944
ilvA
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.
  
 
0.942
CCH90803.1
Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
 
 0.942
ltaA
L-allo-threonine aldolase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 0.941
serC
Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
   
 0.936
thrC
L-threonine synthase; Function of strongly homologous gene; enzyme.
  
  
 
0.922
ask
Aspartokinase; Function of strongly homologous gene; enzyme; Belongs to the aspartokinase family.
  
 
 0.808
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.
  
  
 0.740
Your Current Organism:
Modestobacter marinus
NCBI taxonomy Id: 477641
Other names: CGMCC 4.5581, DSM 45201, M. marinus, Modestobacter marinus Xiao et al. 2011, Modestobacter sp. 42H12-1, strain 42H12-1
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