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
thrCThreonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (354 aa)    
Predicted Functional Partners:
thrB
Serine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
 
 
 0.998
dhoM
Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.996
AKS72627.1
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.
  
 
0.949
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.
  
 
0.949
AKS73746.1
Aspartate kinase; Catalyzes the formation of 4-phospho-L-aspartate from L-aspartate and ATP; lysine and threonine sensitive; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartokinase family.
  
 
 0.867
AKS73742.1
HAD family hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.741
serA
D-3-phosphoglycerate dehydrogenase; Catalyzes the formation of 3-phosphonooxypyruvate from 3-phospho-D-glycerate in serine biosynthesis; can also reduce alpha ketoglutarate to form 2-hydroxyglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
 
  
 0.715
leuD
Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
  
  
 0.698
gltB
Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.681
AKS73160.1
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.642
Your Current Organism:
Staphylococcus schleiferi
NCBI taxonomy Id: 1295
Other names: ATCC 43808, CCUG 25351, CIP 103643, DSM 4807, LMG 13347, LMG:13347, NCTC 12218, NRRL B-14775, S. schleiferi, strain N850274
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