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
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
KKB62748.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (469 aa)    
Predicted Functional Partners:
KKB63522.1
Fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
 
 0.950
sucC
succinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
    
  0.875
sucD
succinate--CoA ligase; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
    
  0.875
KKB61186.1
Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.872
KKB65089.1
Citrate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.845
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.
  
 
 0.845
KKB63339.1
Citrate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
  
 
 0.845
KKB63340.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.845
KKB62865.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.845
KKB61436.1
Phosphoenolpyruvate phosphomutase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.834
Your Current Organism:
Robbsia andropogonis
NCBI taxonomy Id: 28092
Other names: ATCC 19311 [[Pseudomonas woodsii]], ATCC 23061, Aplanobacter stizolobii, Bacterium andropogoni, Bacterium woodsii, Burkholderia andropogonis, CCUG 32772, CFBP 2421, CIP 105771, DSM 9511, DSM 9884 [[Pseudomonas woodsii]], IBSBF 199, ICMP 2807, ICMP 3967 [[Pseudomonas woodsii]], JCM 10487, LMG 2129, LMG 2362 [[Pseudomonas woodsii]], LMG:2129, LMG:2362 [[Pseudomonas woodsii]], NCPPB 934, NCPPB 968 [[Pseudomonas woodsii]], NRRL B-14296, Paraburkholderia andropogonis, Pseudomonas andropogonis, Pseudomonas stizolobii, Pseudomonas woodsii, R. andropogonis, strain PW 102 [[Pseudomonas woodsii]]
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