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, 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. (517 aa)    
Predicted Functional Partners:
EHA63015.1
TIGRFAM: Acetolactate synthase, small subunit; KEGG: pmf:P9303_08471 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT.
  
 
 0.969
EHA63389.1
Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
   
 0.947
EHA64196.1
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: pmf:P9303_07681 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
  
 0.935
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.
 
 
 0.928
trpB
Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
   
 0.923
ilvE
Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
  
 
 0.916
glyA
Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
     
 0.897
trpA
Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
   
 
 0.891
EHA60199.1
KEGG: pmt:PMT0226 putative cystathionine gamma-synthase; PFAM: Cys/Met metabolism, pyridoxal phosphate-dependent enzyme.
  
 
 0.887
EHA63643.1
Serine--pyruvate transaminase; KEGG: pmf:P9303_16451 serine:pyruvate/alanine:glyoxylate aminotransferase; PFAM: Aminotransferase, class V/Cysteine desulfurase.
  
 0.882
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
Server load: low (18%) [HD]