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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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
leuA-22-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. (562 aa)    
Predicted Functional Partners:
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
 0.985
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.
  
 
 0.983
ilvE
Branched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
 
 0.973
ilvD
TIGRFAM: dihydroxy-acid dehydratase; PRIAM: Dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; KEGG: cvi:CV1277 dihydroxy-acid dehydratase; COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase category=G; Belongs to the IlvD/Edd family.
  
 
 0.966
Mfla_2120
TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: tbd:Tbd_1990 acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit category=E.
 
 
 0.945
acsA
Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family.
  
 
 0.928
Mfla_0740
Phosphate acetyltransferase.
   
 
 0.922
Mfla_1511
acetyl-CoA carboxylase, biotin carboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
  
 
 0.915
Mfla_2075
Catalytic domain of components of various dehydrogenase complexes; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
     
 0.905
Mfla_2119
TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: tbd:Tbd_1991 acetolactate synthase, large subunit; COGs: COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase pyruvate dehydrogenase (cytochrome) glyoxylate carboligase phosphonopyruvate decarboxylase] category=H.
 
 
 0.904
Your Current Organism:
Methylobacillus flagellatus
NCBI taxonomy Id: 265072
Other names: M. flagellatus KT, Methylobacillus flagellatus KT, Methylobacillus flagellatus str. KT, Methylobacillus flagellatus strain KT
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