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
ACA71735.1KEGG: psp:PSPPH_1578 tartrate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. (352 aa)    
Predicted Functional Partners:
ACA71260.1
TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: pen:PSEEN4710 acetolactate synthase isozyme III, small subunit.
 
 0.971
ACA71259.1
TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein TPP binding domain protein; KEGG: pen:PSEEN4711 acetolactate synthase III, large subunit.
 
 0.958
ACA71540.1
PFAM: thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein TPP binding domain protein; KEGG: pen:PSEEN4350 acetolactate synthase, large subunit; Belongs to the TPP enzyme family.
 
 0.952
ACA71679.1
PFAM: thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein TPP binding domain protein; KEGG: pen:PSEEN1319 acetolactate synthase, catabolic; Belongs to the TPP enzyme family.
 
 0.950
ACA74629.1
PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; KEGG: pen:PSEEN4252 homoserine dehydrogenase.
  
 
 0.939
ACA73331.1
KEGG: mag:amb3178 tartrate dehydratase beta subunit/fumarate hydratase class I, C-terminal domain; TIGRFAM: hydro-lyase, Fe-S type, tartrate/fumarate subfamily, beta subunit; PFAM: Fe-S type hydro-lyase tartrate/fumarate beta region.
 
 
 0.925
ACA73332.1
KEGG: reu:Reut_B5651 tartrate dehydratase subunit alpha; TIGRFAM: hydro-lyase, Fe-S type, tartrate/fumarate subfamily, alpha subunit; PFAM: Fe-S type hydro-lyase tartrate/fumarate alpha region.
 
  
 0.920
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
 0.908
leuD
3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
  
 0.868
ilvC
Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
 
  
 0.837
Your Current Organism:
Pseudomonas putida W619
NCBI taxonomy Id: 390235
Other names: P. putida W619, Pseudomonas putida str. W619, Pseudomonas putida strain W619
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.