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
ABY93956.1Pyridoxal phosphate-dependent acyltransferase, putative; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. (395 aa)    
Predicted Functional Partners:
tdh
L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family.
 
 
 0.993
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.
  
 
 0.926
gcvPB
Glycine dehydrogenase (decarboxylating); 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. C-terminal subunit subfamily.
  
 
 0.916
gcvPA
Glycine dehydrogenase (decarboxylating); 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.
  
 
 0.915
ABY95633.1
PFAM: aminotransferase, class V; Cys/Met metabolism pyridoxal-phosphate-dependent enzymes; aromatic amino acid beta-eliminating lyase/threonine aldolase.
  
 
 0.914
ABY94309.1
PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB.
  
  
 0.830
birA
biotin--acetyl-CoA-carboxylase ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family.
  
  
 0.718
ABY93958.1
PFAM: 4Fe-4S ferredoxin, iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family.
       0.650
ABY94534.1
PFAM: Alcohol dehydrogenase GroES domain protein.
  
  
 0.505
gcvT
Glycine cleavage system T protein; The glycine cleavage system catalyzes the degradation of glycine.
  
 
 0.503
Your Current Organism:
Thermoanaerobacter pseudethanolicus
NCBI taxonomy Id: 340099
Other names: Clostridium thermohydrosulfuricum 39E, T. pseudethanolicus ATCC 33223, Thermoanaerobacter ethanolicus ATCC 33223, Thermoanaerobacter pseudethanolicus 39E, Thermoanaerobacter pseudethanolicus ATCC 33223, Thermoanaerobacter pseudethanolicus str. ATCC 33223, Thermoanaerobacter pseudethanolicus strain ATCC 33223
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.