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
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[Homology]
Score
hacB3-isopropylmalate dehydratase (leuD); 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, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are pa [...] (170 aa)    
Predicted Functional Partners:
hacA
3-isopropylmalate dehydratase (leuC); 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, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are pa [...]
 0.999
leuC
3-isopropylmalate dehydratase (leuC); Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate; Belongs to the [...]
 0.998
aksF
3-isopropylmalate dehydrogenase 2 (leuB2); Catalyzes the NAD-dependent oxidation and decarboxylation of (2R,3S)-homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate), (2R,3S)-homo(2)-isocitrate and (2R,3S)-homo(3)-isocitrate, into 2- oxoadipate, 2-oxopimelate, and 2-oxosuberate, respectively. This last compound is a precursor to coenzyme B and biotin in methanoarchaea. Is also able to produce 2-oxoazelate from (2R,3S)-homo(4)-isocitrate. Is not able to use NADP as an oxidant.
 
 
 0.996
aksA
2-isopropylmalate synthase (leuA); Catalyzes the condensation of alpha-ketoglutarate and acetyl- CoA to form trans-homoaconitate. Can also catalyze the condensation of alpha-ketoadipate with acetyl-CoA to form (R)-homo(2)citrate, and the condensation of alpha-ketopimelate with acetyl-CoA to form (R)- homo(3)citrate; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
 
 0.974
leuB
3-isopropylmalate dehydrogenase 1 (leuB1); Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate, which decarboxylates to 4-methyl-2-oxopentanoate (2- oxoisocaproate). Also catalyzes the oxidative decarboxylation of 3- methylmalate to 2-oxobutyrate, and that of D-malate to pyruvate. Cannot use NADP(+) instead of NAD(+). Cannot catalyze the oxidation of L- malate, L-tartrate, D-tartrate, DL-isocitrate, or DL-lactate.
 
 
 0.944
leuD
3-isopropylmalate dehydratase (leuD); Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.
  
  
 
0.904
ilvC
Ketol-acid reductoisomerase (ilvC); 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.
  
  
 0.893
leuA
2-isopropylmalate synthase (leuA); 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).
  
 
 0.870
cimA
2-isopropylmalate synthase (leuA); Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
 
 0.870
ilvH
Acetolactate synthase small subunit (ilvN); Similar to GB:L03181 SP:P37252 PID:143092 PID:1770067 GB:AL009126 percent identity: 49.37; identified by sequence similarity; putative; Belongs to the acetolactate synthase small subunit family.
  
  
 0.865
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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