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
leuB3-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. (336 aa)    
Predicted Functional Partners:
leuD
Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
 
 0.998
leuC
Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 0.998
KIU15673.1
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.994
KIU15671.1
3-phosphoglycerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
 
  
 0.981
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.
 
  
 0.979
KIU16773.1
Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.977
KIU15674.1
Acetolactate synthase large subunit; catalyzes the formation of 2-acetolactate from pyruvate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.975
ilvD
Dihydroxy-acid dehydratase; Catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.
 
  
 0.971
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.
 
 
 0.964
KIU18450.1
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family.
 
 0.961
Your Current Organism:
Mycolicibacterium llatzerense
NCBI taxonomy Id: 280871
Other names: CCUG 54744, CECT 7273, DSM 45343, JCM 16229, M. llatzerense, Mycobacterium llatzerense, Mycobacterium llatzerense Gomila et al. 2008, Mycobacterium sp. 13-009-09768, Mycobacterium sp. MG12, Mycobacterium sp. MG13, Mycobacterium sp. MG14, Mycobacterium sp. MG15, Mycobacterium sp. MG16, Mycobacterium sp. MG18, Mycolicibacterium llatzerense (Gomila et al. 2008) Gupta et al. 2018, strain MG13
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