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
AGA70859.1Serine-pyruvate aminotransferase/archaeal aspartate aminotransferase; PFAM: Aminotransferase class-V. (390 aa)    
Predicted Functional Partners:
glyA
Glycine/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.
  
 0.934
gcvT
Glycine cleavage system T protein; The glycine cleavage system catalyzes the degradation of glycine.
  
 
 0.924
AGA70137.1
L-serine dehydratase, iron-sulfur-dependent, beta subunit; PFAM: ACT domain; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
 
  
 0.919
AGA68328.1
Lactate dehydrogenase-like oxidoreductase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain.
  
 
 0.915
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.
  
 
 0.915
AGA68379.1
Threonine dehydratase, medium form; PFAM: Pyridoxal-phosphate dependent enzyme.
  
 
 0.915
AGA69389.1
Lactate dehydrogenase-like oxidoreductase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain.
  
 
 0.915
AGA69508.1
Fructose-2,6-bisphosphatase; PFAM: Phosphoglycerate mutase family.
  
 
 0.915
AGA69718.1
Transcriptional regulator with HTH domain and aminotransferase domain; PFAM: Aminotransferase class I and II.
  
 
 0.915
AGA68380.1
Threonine aldolase; PFAM: Beta-eliminating lyase.
    
 0.913
Your Current Organism:
Desulfitobacterium dichloroeliminans
NCBI taxonomy Id: 871963
Other names: D. dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans DCA1, Desulfitobacterium dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans LMG P21439, Desulfitobacterium dichloroeliminans str. LMG P-21439, Desulfitobacterium dichloroeliminans strain LMG P-21439
Server load: low (18%) [HD]