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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colored nodes:
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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co-expression
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[Homology]
Score
fumCClass II fumarate hydratase; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (464 aa)    
Predicted Functional Partners:
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family.
  
 0.991
SdhA
Part of four member fumarate reductase enzyme complex FrdABCD which catalyzes the reduction of fumarate to succinate during anaerobic respiration; FrdAB are the catalytic subcomplex consisting of a flavoprotein subunit and an iron-sulfur subunit, respectively; FrdCD are the membrane components which interact with quinone and are involved in electron transfer; the catalytic subunits are similar to succinate dehydrogenase SdhAB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 
 0.989
fumA
Fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
 
 0.986
maeB_1
Malic enzyme; NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the malic enzymes family.
  
 
 0.975
sdhB
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.970
maeB_2
Malate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.964
AOI84686.1
Malate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.964
sdhC
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.961
acnA
Aconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate.
 
 0.952
gltA
Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
  
 0.947
Your Current Organism:
Burkholderia cepacia
NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia genomovar I, Burkholderia sp. Bp7081, Burkholderia sp. Bp7091, Burkholderia sp. Bp7098, Burkholderia sp. Bp7108, Burkholderia sp. Bp7432, Burkholderia sp. LK29, Burkholderia sp. NCIM 5465, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717
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