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; 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. (411 aa)    
Predicted Functional Partners:
Psed_1821
KEGG: svi:Svir_08880 acetolactate synthase 3 regulatory subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT.
  
 
 0.967
Psed_1665
Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.
 
 
0.947
Psed_1820
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: ami:Amir_6021 acetolactate synthase 1 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
 
 0.947
Psed_2011
TIGRFAM: Threonine synthase; KEGG: ami:Amir_1205 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit.
  
 
0.941
Psed_2549
L-serine dehydratase 1; TIGRFAM: Iron-sulphur-dependent L-serine dehydratase single chain form; KEGG: rop:ROP_15050 L-serine dehydratase; PFAM: Serine dehydratase-like, alpha subunit; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
  
 
 0.941
Psed_4150
KEGG: bra:BRADO2458 putative 3-isopropylmalate dehydrogenase (LeuB); PFAM: Isocitrate/isopropylmalate dehydrogenase.
 
 
 0.939
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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily.
 
 
 0.936
Psed_0688
KEGG: mil:ML5_3221 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase.
 
 
 0.935
trpB
Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
0.933
Psed_3157
Benzoylformate decarboxylase; KEGG: tcu:Tcur_0107 thiamine pyrophosphate protein domain-containing protein TPP-binding protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain.
  
 0.931
Your Current Organism:
Pseudonocardia dioxanivorans
NCBI taxonomy Id: 675635
Other names: P. dioxanivorans CB1190, Pseudonocardia dioxanivorans CB1190, Pseudonocardia dioxanivorans DSM 44775, Pseudonocardia dioxanivorans str. CB1190, Pseudonocardia dioxanivorans strain CB1190
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.