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
ALG70726.1FAD-dependent oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (380 aa)    
Predicted Functional Partners:
ALG73148.1
Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.628
ALG72468.1
4-aminobutyrate aminotransferase; Catalyzes the formation of succinate semialdehyde and glutamate from 4-aminobutanoate and 2-oxoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
  
  
 0.620
ALG70149.1
Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.574
glpK
Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family.
 
  
 0.560
ALG72147.1
Catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate; also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.523
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.
  
  
 0.523
ALG72990.1
Citrate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.523
ALG73700.1
Citrate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.523
ALG73704.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.523
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.
  
  
 0.523
Your Current Organism:
Azospirillum thiophilum
NCBI taxonomy Id: 528244
Other names: A. thiophilum, Azospirillum sp. BV-s, Azospirillum thiophilum Lavrinenko et al. 2010, DSM 21654, VKM B-2513, strain BV-S
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