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
Afer_1546TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: ace:Acel_0707 acetolactate synthase 3 regulatory subunit. (190 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.
 
 
 0.999
Afer_1547
TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP- binding; KEGG: kra:Krad_1335 acetolactate synthase 1 catalytic subunit.
 0.999
Afer_1601
PFAM: thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein TPP binding domain protein; KEGG: mva:Mvan_5213 hypothetical protein.
 
 0.997
Afer_1536
PFAM: isocitrate/isopropylmalate dehydrogenase; KEGG: nca:Noca_3368 3-isopropylmalate dehydrogenase.
  
 0.982
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 1 subfamily.
  
 
 0.953
Afer_1538
TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; PFAM: pyruvate carboxyltransferase; LeuA allosteric (dimerization) domain; KEGG: tfu:Tfu_0617 alpha- isopropylmalate/homocitrate synthase family transferase; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.931
ilvD
KEGG: nfa:nfa11740 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.930
Afer_0713
2-oxo-acid dehydrogenase E1 subunit, homodimeric type; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
     
 0.863
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.
  
  
 0.857
Afer_0824
PFAM: Transketolase central region; Transketolase domain protein; KEGG: gka:GK3216 pyruvate dehydrogenase E1 (lipoamide) beta subunit.
   
 
  0.841
Your Current Organism:
Acidimicrobium ferrooxidans
NCBI taxonomy Id: 525909
Other names: A. ferrooxidans DSM 10331, Acidimicrobium ferrooxidans DSM 10331, Acidimicrobium ferrooxidans ICP, Acidimicrobium ferrooxidans str. DSM 10331, Acidimicrobium ferrooxidans strain DSM 10331
Server load: low (38%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.