close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
ilvDDihydroxy-acid dehydratase (ilvD); Similar to GB:L77117 PID:1591912 percent identity: 54.55; identified by sequence similarity; putative; Belongs to the IlvD/Edd family. (547 aa)    
Predicted Functional Partners:
ilvC
Ketol-acid reductoisomerase (ilvC); 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 or NADH to yield (R)-2,3-dihydroxy-isovalerate. It is able to use both NADPH and NADH, but has a preference for NADH.
 
 
 0.998
ilvE
Branched-chain amino acid aminotransferase (ilvE); Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
  
 0.997
leuA
2-isopropylmalate synthase (leuA-2); Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate).
 
 
 0.987
leuB
3-isopropylmalate dehydrogenase (leuB); 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 (By similarity); Belongs to the isocitrate and isopropylmalate dehydrogenases family.
  
  
 0.959
AF_1720
Acetolactate synthase, large subunit (ilvB-1); Similar to GB:L77117 SP:Q57725 PID:1591003 percent identity: 57.48; identified by sequence similarity; putative.
  
 0.934
ilvH
Acetolactate synthase, small subunit (ilvN); Similar to GB:L77117 SP:Q57625 PID:1590918 percent identity: 60.38; identified by sequence similarity; putative; Belongs to the acetolactate synthase small subunit family.
 
 
 0.898
leuC1
Aconitase (acn); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
  
 0.898
leuC2
3-isopropylmalate dehydratase, large subunit (leuC); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
  
 0.897
trpCD
Anthranilate synthase component II (trpD); Bifunctional enzyme that catalyzes the second and fourth steps of tryptophan biosynthetic pathway. The second step is catalyzed by the anthranilate phosphoribosyltransferase, coded by the TrpD domain and the fourth step is catalyzed by indole-3-glycerol phosphate synthase, coded by the TrpC domain (By similarity).
  
  
 0.888
cimA
2-isopropylmalate synthase (leuA-1); Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
  
 0.872
Your Current Organism:
Archaeoglobus fulgidus
NCBI taxonomy Id: 224325
Other names: A. fulgidus DSM 4304, Archaeoglobus fulgidus DSM 4304, Archaeoglobus fulgidus VC-16, Archaeoglobus fulgidus str. DSM 4304, Archaeoglobus fulgidus strain DSM 4304
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.