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
EHM00427.1Thiamine pyrophosphate enzyme, central domain protein; KEGG: ooe:OEOE_0936 2.2e-197 pyruvate oxidase K00158; Psort location: CytoplasmicMembrane, score: 9.82; Belongs to the TPP enzyme family. (471 aa)    
Predicted Functional Partners:
EHM00426.1
Thiamine pyrophosphate enzyme, TPP binding domain protein; KEGG: ooe:OEOE_0936 1.2e-47 pyruvate oxidase K00158; Psort location: CytoplasmicMembrane, score: 9.82.
     0.994
EHL95934.1
Pyruvate kinase; KEGG: lbr:LVIS_0765 7.0e-263 pyruvate kinase; K00873 pyruvate kinase; Psort location: Cytoplasmic, score: 9.97.
  
 0.894
phnX-2
2-aminoethylphosphonate--pyruvate transaminase; Involved in phosphonate degradation; Belongs to the HAD-like hydrolase superfamily. PhnX family.
  
 
 0.872
EHL98028.1
KEGG: lbr:LVIS_0492 3.1e-79 alpha-acetolactate decarboxylase; K01575 acetolactate decarboxylase; Psort location: Cytoplasmic, score: 8.96.
  
 
 0.850
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.
  
 
 0.784
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.
 
 0.758
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
  
 
 0.757
EHM01617.1
KEGG: ooe:OEOE_1723 1.3e-151 2-isopropylmalate synthase K01649; Psort location: Cytoplasmic, score: 9.97; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
 
 0.754
ilvA
Threonine ammonia-lyase; 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.
  
 0.754
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.
  
 
 0.724
Your Current Organism:
Lactobacillus parafarraginis
NCBI taxonomy Id: 797515
Other names: L. parafarraginis F0439, Lactobacillus parafarraginis F0439, Lactobacillus parafarraginis str. F0439, Lactobacillus parafarraginis strain F0439, Lactobacillus sp. oral taxon 418 str. F0439
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