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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
AMQ94588.1Converts 2-oxoglutarate to glutamate; in Escherichia coli this enzyme plays a role in glutamate synthesis when the cell is under energy restriction; uses NADPH; forms a homohexamer; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. (449 aa)    
Predicted Functional Partners:
ggt
Gamma-glutamyltranspeptidase; Periplasmic enzyme; post-translationally processed into two subunits which are required for wild-type enzyme activity; cleaves the gammaglutamyl linkages of compounds such as glutathione and transfer the gammaglutamyl group to other amino acids and peptides; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.944
nrfA
Cytochrome C nitrite reductase; Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process; Belongs to the cytochrome c-552 family.
     
 0.943
glnA
Forms a homododecamer; forms glutamine from ammonia and glutamate with the conversion of ATP to ADP and phosphate; also functions in the assimilation of ammonia; highly regulated protein controlled by the addition/removal of adenylyl groups by adenylyltransferase from specific tyrosine residues; addition of adenylyl groups results in inactivation of the enzyme; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.940
AMQ93613.1
Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.918
arcC
Carbamate kinase; Reversible synthesis of carbamate and ATP from carbamoyl phosphate and ADP; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.900
pckA
Phosphoenolpyruvate carboxykinase; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
  
 
 0.894
gshAB
Bifunctional glutamate--cysteine ligase/glutathione synthetase; Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine; In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.
    
 0.874
sucA
2-oxoglutarate dehydrogenase subunit E1; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.868
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate.
   
 
 0.859
lpdA
E3 component of pyruvate and 2-oxoglutarate dehydrogenase complex; catalyzes the oxidation of dihydrolipoamide to lipoamide; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.852
Your Current Organism:
Aggregatibacter actinomycetemcomitans
NCBI taxonomy Id: 714
Other names: A. actinomycetemcomitans, ATCC 33384, Actinobacillus (Haemophilus) actinomycetemcomitans, Actinobacillus actinomycetemcomitans, Bacterium acetinomycetum comitans, Bacterium actinomycetem comitans, Bacterium comitans, CCUG 13227, CIP 52.106, DSM 8324, Haemophilus actinomycetemcomitans, Haemophilus actinomyceticomitans, NCTC 9710
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