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; Derived by automated computational analysis using gene prediction method: Protein Homology. (365 aa)    
Predicted Functional Partners:
thrC_1
Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.922
serC_2
Phosphoserine transaminase; 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.
  
 
 0.916
serC_1
Phosphoserine transaminase; 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.
  
 
 0.916
ltaE
Aspartate aminotransferase family protein; Catalyzes the formation of pyruvate and beta-alanine from L-alanine and 3-oxopropanoate; frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.911
artP-3
Arginine transporter ATP-binding subunit; With ArtMQJI transports arginine across the inner membrane; frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.911
ilvA_1
Threonine ammonia-lyase, 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.
  
 
 0.910
tdcB_1
Threonine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.910
psdht
Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.910
ilvA_2
PLP-dependent 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.
  
 
 0.910
thrB
Homoserine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the pseudomonas-type ThrB family.
    
  0.902
Your Current Organism:
Achromobacter insolitus
NCBI taxonomy Id: 217204
Other names: A. insolitus, API 201-3-84, Achromobacter insolitus Coenye et al. 2003, Achromobacter sp. AR476-2, Achromobacter sp. KCJK1724, Achromobacter sp. KCJK1731, Achromobacter sp. LMG 6003, Achromobacter sp. UBA1170, Achromobacter sp. UBA1582, CCM 7182, CCUG 47057, LMG 6003, LMG:6003, NCTC 13520, strain Gilardi 3038
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