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
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Experiments
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Textmining
[Homology]
Score
Noca_3306PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: afu:AF2100 acetolactate synthase large subunit. (588 aa)    
Predicted Functional Partners:
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.
 
 
 0.986
ilvC-2
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.
 
 
 0.986
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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily.
 
 0.976
Noca_3391
TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: fal:FRAAL5850 acetolactate synthase III, valine-sensitive, small subunit.
 
 
 0.973
Noca_0979
L-threonine ammonia-lyase; TIGRFAM: threonine dehydratase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; amino acid-binding ACT domain protein; KEGG: sco:SCO4962 threonine dehydratase.
 
 0.963
Noca_0537
PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: tfu:Tfu_2674 2-oxoglutarate ferredoxin oxidoreductase, alpha subunit.
  
 
 0.926
leuA
2-isopropylmalate synthase; 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); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
  
 
 0.921
ilvD
KEGG: rha:RHA1_ro05087 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
  
 0.912
Noca_0536
PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; KEGG: sma:SAV4876 2-oxoglutarate ferredoxin oxidoreductase, beta subunit.
  
 
 0.910
Noca_2359
Pyruvate ferredoxin oxidoreductase, beta subunit; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; KEGG: rfr:Rfer_2185 thiamine pyrophosphate enzyme-like TPP-binding.
  
 
 0.910
Your Current Organism:
Nocardioides sp. JS614
NCBI taxonomy Id: 196162
Other names: N. sp. JS614
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