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
Swoo_1806L-serine dehydratase 1; KEGG: sse:Ssed_2838 L-serine ammonia-lyase; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. (458 aa)    
Predicted Functional Partners:
glyA
Glycine 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.
  
 
 0.951
ilvA
Threonine dehydratase, biosynthetic; 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.
  
 
 0.920
Swoo_3544
KEGG: sse:Ssed_3373 phosphoserine phosphatase; TIGRFAM: phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB (PSPase-like); PFAM: Haloacid dehalogenase domain protein hydrolase.
   
 
 0.915
Swoo_0447
Serine--pyruvate transaminase; PFAM: aminotransferase class V; KEGG: sse:Ssed_4160 serine--pyruvate transaminase.
    
 0.908
Swoo_0438
KEGG: sse:Ssed_4170 serine O-acetyltransferase; TIGRFAM: serine O-acetyltransferase; PFAM: transferase hexapeptide repeat containing protein; serine acetyltransferase domain protein.
     
 0.904
Swoo_1774
TIGRFAM: serine O-acetyltransferase; KEGG: sse:Ssed_2873 serine O-acetyltransferase.
     
 0.904
Swoo_0864
L-serine dehydratase 1; KEGG: sse:Ssed_0859 L-serine ammonia-lyase; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
  
  
 
0.903
trpA
Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
   
 
 0.902
Swoo_2012
Pyridoxal-5'-phosphate-dependent protein beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
     
  0.900
Swoo_2327
CDP-diacylglycerol--serine O-phosphatidyltransferase; PFAM: phospholipase D/Transphosphatidylase; KEGG: sse:Ssed_2288 phospholipase D/transphosphatidylase.
     
  0.900
Your Current Organism:
Shewanella woodyi
NCBI taxonomy Id: 392500
Other names: S. woodyi ATCC 51908, Shewanella woodyi ATCC 51908, Shewanella woodyi str. ATCC 51908, Shewanella woodyi strain ATCC 51908
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.