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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
mqoMalate:quinone oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (544 aa)    
Predicted Functional Partners:
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.
  
 
 0.941
gltA-2
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.
  
 
 0.941
maeB
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.
  
 
 0.938
fumC
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.
    
 0.923
fumA_1
Fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
     
 0.921
AKL36062.1
Fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
     
 0.921
AKL37416.1
Fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
     
 0.921
maeA_2
NAD-dependent malic enzyme; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.918
aceB
Malate synthase; Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.917
ppc
Phosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family.
     
 0.917
Your Current Organism:
Klebsiella oxytoca
NCBI taxonomy Id: 571
Other names: ATCC 13182, Bacillus oxytocus perniciosus, CCUG 15717, CIP 103434, DSM 5175, IAM 14201, K. oxytoca, Klebsiella sp. CECRI-24/07, Klebsiella sp. MN9SED2, LMG 3055, LMG:3055, NBRC 102593, NBRC 105695, NCTC 13727, strain 479-2
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