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
KDS88996.1Threonine aldolase; Derived by automated computational analysis using gene prediction method: Protein Homology. (372 aa)    
Predicted Functional Partners:
KDS88998.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.959
KDS88997.1
Short-chain dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.946
gcvP
Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
    
 0.940
KDS89913.1
L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.
   
 0.930
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
    
 0.915
KDS88376.1
Threonine synthase; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.910
KDS84395.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.902
KDS87321.1
Threonine dehydratase; Catalyzes the formation of 2-oxobutanoate from L-threonine; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.898
KDS84637.1
Threonine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.898
KDS84170.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.861
Your Current Organism:
Streptomyces fradiae
NCBI taxonomy Id: 1906
Other names: ATCC 10745, ATCC 19760, Actinomyces fradii, BCRC 12196, CBS 498.68, CCM 3174, CCRC 12196, CCRC:12196, CECT 3197, DSM 40063, HAMBI 965, HUT 6095, IFO 12773, IFO 3718, IMET 42051, IMI 061202, ISP 5063, JCM 4133, JCM 4579, JCM 4824 [[Streptomyces roseoflavus]], KCTC 9760, NBRC 12773, NBRC 13439 [[Streptomyces roseoflavus]], NBRC 3718, NCIMB 11005, NCIMB 8233, NRRL B-2789 [[Streptomyces roseoflavus]], NRRL-ISP 5063, PCM 2330, RIA 97, S. fradiae, Streptomyces fradiae subsp. fradiae, Streptomyces fradii, Streptomyces roseiflavus, Streptomyces roseoflavus, Streptomyces sp. NEAE-82, UNIQEM 146, VKM Ac-150, VKM Ac-151, VKM Ac-152, VKM Ac-764
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.