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
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[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. (344 aa)    
Predicted Functional Partners:
Aaci_2228
TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein; KEGG: dps:DP2770 acetolactate synthase, small subunit.
 
 
 0.999
Aaci_2229
TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: glo:Glov_2503 acetolactate synthase, large subunit, biosynthetic type.
 
 
 0.998
ilvD
KEGG: afr:AFE_0662 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.998
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.
 
  
 0.980
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
  
 0.979
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.
 
  
 0.976
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.
 
  
 0.749
Aaci_1022
Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.
 
  
 0.744
Aaci_1557
KEGG: hypothetical protein; K00031 isocitrate dehydrogenase; TIGRFAM: isocitrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase.
  
  
 0.743
Aaci_0849
TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; PFAM: pyruvate carboxyltransferase; LeuA allosteric (dimerisation) domain; KEGG: gur:Gura_2317 putative alpha- isopropylmalate/homocitrate synthase family transferase; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
  
 0.705
Your Current Organism:
Alicyclobacillus acidocaldarius DSM 446
NCBI taxonomy Id: 521098
Other names: A. acidocaldarius subsp. acidocaldarius DSM 446, Alicyclobacillus acidocaldarius subsp. acidocaldarius ATCC 27009, Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446, Alicyclobacillus acidocaldarius subsp. acidocaldarius IFO 15652, Alicyclobacillus acidocaldarius subsp. acidocaldarius JCM 5260, Alicyclobacillus acidocaldarius subsp. acidocaldarius NBRC 15652, Alicyclobacillus acidocaldarius subsp. acidocaldarius NCIB 11725, Alicyclobacillus acidocaldarius subsp. acidocaldarius str. DSM 446, Alicyclobacillus acidocaldarius subsp. acidocaldarius strain DSM 446
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