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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene co-occurrence
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[Homology]
Score
ADZ08346.1KEGG: mfv:Mfer_0053 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. (166 aa)    
Predicted Functional Partners:
ADZ08345.1
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: mth:MTH1444 acetolactate synthase catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
 
 0.999
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.
 
 
 0.998
ADZ08817.1
KEGG: mfv:Mfer_0624 acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain.
 
 0.997
ADZ08423.1
KEGG: mru:mru_0103 3-isopropylmalate dehydrogenase LeuB; PFAM: Isocitrate/isopropylmalate dehydrogenase.
  
 0.984
cimA
Isopropylmalate/citramalate/homocitrate synthase; Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
 
 0.964
ADZ10255.1
Acetolactate synthase; KEGG: mth:MTH476 pyruvate dehydrogenase / acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Rubredoxin-type Fe(Cys)4 protein; Thiamine pyrophosphate enzyme, central domain.
 
 
 0.963
ilvD
PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; TIGRFAM: Dihydroxy-acid dehydratase; HAMAP: Dihydroxy-acid dehydratase; KEGG: mmg:MTBMA_c00370 dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.960
ADZ08319.1
SMART: 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; TIGRFAM: Isopropylmalate/citramalate/homocitrate synthase; KEGG: mth:MTH1481 2-isopropylmalate synthase; PFAM: Pyruvate carboxyltransferase; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
 
 0.929
ADZ10621.1
KEGG: mmg:MTBMA_c14150 2-oxoglutarate synthase, subunit alpha; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Transketolase, C-terminal.
  
 
 0.927
ADZ08740.1
KEGG: mmg:MTBMA_c03140 pyruvate synthase, subunit A; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal.
  
 
 0.918
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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