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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
hacB3-isopropylmalate dehydratase small subunit; Hydro-lyase with broad substrate specificity for cis- unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4- tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4- tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1- hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)- aconitate. All these reactions are part of the biosynthesis pathway of coenzyme B; Belongs to the LeuD f [...] (163 aa)    
Predicted Functional Partners:
leuC-2
3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 0.999
leuC
3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 0.997
ADZ08832.1
TIGRFAM: Isopropylmalate/isohomocitrate dehydrogenase; KEGG: mth:MTH184 multifunctional 3-isopropylmalate dehydrogenase/D-malate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase.
 
 0.982
ADZ10290.1
TIGRFAM: Isopropylmalate/citramalate/homocitrate synthase; KEGG: mmg:MTBMA_c02150 2-isopropylmalate synthase; PFAM: Pyruvate carboxyltransferase; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.970
ADZ10165.1
Beta-ribofuranosylaminobenzene 5'-phosphate synthase family; Catalyzes the condensation of 4-aminobenzoate (pABA) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P).
       0.887
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.
  
  
 0.880
ADZ08423.1
KEGG: mru:mru_0103 3-isopropylmalate dehydrogenase LeuB; PFAM: Isocitrate/isopropylmalate dehydrogenase.
  
 0.838
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.
  
 
 0.831
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.
  
 
 0.831
ADZ10166.1
PFAM: Radical SAM; KEGG: mmg:MTBMA_c12290 Fe-S oxidoreductase.
       0.811
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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