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
KOH17429.1Threonine aldolase; Low- specificity; catalyzes the formation of acetaldehyde and glycine from L-threonine; acts on L-threonine, L-allo-threonine, L-threo-phenylserine, and L-erythro-phenylserine; Derived by automated computational analysis using gene prediction method: Protein Homology. (334 aa)    
Predicted Functional Partners:
KOH22402.1
Glycine dehydrogenase; Acts in conjunction with GvcH to form H-protein-S-aminomethyldihydrolipoyllysine from glycine; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.946
glyA
Serine hydroxymethyltransferase; Catalyzes the reaction of glycine with 5,10-methylenetetrahydrofolate to form L-serine and tetrahydrofolate; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.926
KOH19639.1
Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.925
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.
   
 
 0.919
KOH20602.1
Alanine--glyoxylate aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.918
KOH24915.1
2-amino-3-ketobutyrate CoA ligase; Catalyzes the formation of 2-amino-3-oxobutanoate from acetyl-CoA and glycine; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.907
tdh
L-threonine 3-dehydrogenase; Converts threonine and NAD to 1,2-amino-3-oxobutanoate and NADH; functions in threonine catabolism; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
  0.900
ychF
GTP-binding protein; EngD; translation-associated GTPase; the crystal structure of the Haemophilus influenzae YchF protein showed similarity to the yeast structure (PDB: 1NI3); fluorescence spectroscopy revealed nucleic acid binding; the yeast protein YBR025c interacts with the translation elongation factor eEF1; Derived by automated computational analysis using gene prediction method: Protein Homology.
      0.864
KOH17539.1
ADP-ribose pyrophosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.740
KOH17428.1
Cytochrome C554; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.612
Your Current Organism:
Vibrio parahaemolyticus
NCBI taxonomy Id: 670
Other names: ATCC 17802, Beneckea parahaemolytica, CAIM 320, CCUG 14474, CCUG 15657, CCUG 4224, CIP 75.2, DSM 10027, IFO 12711, LMG 2850, LMG:2850, NBRC 12711, NCCB 77010, NCCB 77018, NCTC 10903, NRRL B-4167, Oceanomonas parahaemolytica, Pasteurella parahaemolytica, V. parahaemolyticus
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