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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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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. (521 aa)    
Predicted Functional Partners:
AEB85472.1
KEGG: ctt:CtCNB1_1659 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT.
 
 0.954
AEB83582.1
TIGRFAM: Threonine synthase; KEGG: dia:Dtpsy_2558 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit.
  
 
 0.943
AEB83428.1
Acetolactate synthase; KEGG: ajs:Ajs_3488 hypothetical protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain.
  
 0.941
AEB85394.1
Acetolactate synthase; KEGG: ajs:Ajs_2520 thiamine pyrophosphate protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Belongs to the TPP enzyme family.
  
 0.941
AEB85473.1
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: ajs:Ajs_1769 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central domain.
  
 0.941
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.
 
 0.939
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.
    
 0.938
trpB
Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
 0.934
trpB-2
Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
 0.934
AEB83199.1
KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase.
  
 0.926
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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