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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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Score
leuA2-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. (579 aa)    
Predicted Functional Partners:
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.
 
 
 0.993
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
 
 0.993
Achl_2267
TIGRFAM: branched-chain amino acid aminotransferase; PFAM: aminotransferase class IV; KEGG: art:Arth_2529 branched chain amino acid aminotransferase.
  
 0.983
ilvD-2
KEGG: aau:AAur_0356 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.971
Achl_2278
TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; acetolactate synthase small subunit; KEGG: art:Arth_2538 acetolactate synthase 3 regulatory subunit.
 
 
 0.969
ilvD
KEGG: aau:AAur_2510 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
  
 
 0.967
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.
 
  
 0.951
Achl_0174
Carbamoyl-phosphate synthase L chain ATP-binding; PFAM: biotin/lipoyl attachment domain-containing protein; phosphoribosylglycinamide synthetase; ATP-dependent carboxylate-amine ligase domain protein ATP-grasp; Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: art:Arth_0096 carbamoyl-phosphate synthase L chain, ATP-binding.
  
 
 0.947
Achl_1404
PFAM: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: art:Arth_1386 carbamoyl-phosphate synthase L chain, ATP-binding.
  
 
 0.947
Achl_2279
TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein TPP binding domain protein; KEGG: art:Arth_2539 acetolactate synthase 1 catalytic subunit.
 
 
 0.924
Your Current Organism:
Pseudarthrobacter chlorophenolicus
NCBI taxonomy Id: 452863
Other names: Arthrobacter chlorophenolicus A6, P. chlorophenolicus A6, Pseudarthrobacter chlorophenolicus A6
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