close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
tdcGPFAM: Serine dehydratase alpha chain; Serine dehydratase beta chain; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, single chain form. (469 aa)    
Predicted Functional Partners:
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.
  
 
 0.982
ilvA
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
  
 
 0.950
serB
Phosphoserine phosphatase; PFAM: ACT domain; haloacid dehalogenase-like hydrolase; TIGRFAM: Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; phosphoserine phosphatase SerB.
   
 
 0.941
cysE
Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (six repeats); TIGRFAM: serine O-acetyltransferase.
     
 0.908
trpA
Tryptophan synthase, alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
   
 
 0.901
trpB
Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
     
  0.900
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
  
 
 0.830
hom
PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain.
   
 
 0.820
metX
Homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
     
  0.800
AJI79058.1
PFAM: NADPH-dependent FMN reductase; TIGRFAM: LLM-partnered FMN reductase, CE1759 family; FMN reductase, MsuE subfamily.
       0.750
Your Current Organism:
Corynebacterium singulare
NCBI taxonomy Id: 161899
Other names: C. singulare, CCUG 37330, CIP 105491, DSM 44357, IBS B52218, IFO 16162, JCM 10385, NBRC 16162
Server load: low (40%) [HD]