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
ilvCKetol-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. (491 aa)    
Predicted Functional Partners:
ilvH
Acetolactate synthase is a complex of a large catalytic chain and a smaller regulatory chain associated in an alpha2/beta2 heterotetramer. It catalyzes the first step of the isoleucine and valine biosynthesic pathways. The regulatory subunit, IlvH, features an ACT domain. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.996
ilvB
Acetolactate synthase is a complex of a large catalytic chain and a small regulatory chain associated in an alpha2/beta2 heterotetramer. It catalyzes the first step of the isoleucine and valine biosynthesic pathways. The catalytic subunit, IlvB, is a thiamine pyrophosphate-dependent enzyme. It also binds one magnesium ion and one FAD per subunit, although the role of this cofactor is not clear considering that the reaction does not involve redox chemistry; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.991
ilvD1
Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid; Binds a 4Fe-4S cluster; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the IlvD/Edd family.
 
 
 0.987
ilvD2
Dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid; Binds a 4Fe-4S cluster; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the IlvD/Edd family.
  
 
 0.894
leuC
3-Isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
  
 0.892
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.
  
  
 0.874
ilvA
Threonine 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.
 
  
 0.824
LeuB2
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.
 
  
 0.776
gltA-2
Glutamate synthase [NADPH] large chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit (GltB). GltA binds as cofactors a 3Fe-4S cluster, a FAD and a FMN. Localized i [...]
  
  
 0.772
leuA1
2-Isopropylmalate synthase catalyzes the first step in the L-leucine biosynthesis pathway. LeuA condensates the acetyl group of acetyl-CoA with 3-methyl-2- oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Its features a N-terminal catalytic HMGL-like domain and a C-terminal LeuA-dimerization domain. LeuA forms a homotetramer. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
  
 0.747
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.