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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
Lcho_1555Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. (364 aa)    
Predicted Functional Partners:
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.
 
  
 0.960
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.
   
 0.942
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.
  
 
 0.935
Lcho_2024
KEGG: mpt:Mpe_A1542 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit.
  
 0.929
Lcho_0161
PFAM: FAD dependent oxidoreductase; KEGG: reh:H16_B2189 D-amino-acid dehydrogenase.
    
 0.904
Lcho_1554
PFAM: phospholipase/Carboxylesterase; KEGG: bpt:Bpet2610 hypothetical protein.
       0.558
Lcho_0651
TIGRFAM: para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding-like; KEGG: mpt:Mpe_A2628 chorismate binding enzyme.
  
  
 0.519
Lcho_3341
Acetaldehyde dehydrogenase (acetylating); Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.
     
  0.499
Lcho_0110
NADH dehydrogenase; PFAM: NAD-dependent epimerase/dehydratase; 3-beta hydroxysteroid dehydrogenase/isomerase; dTDP-4-dehydrorhamnose reductase; NmrA family protein; Male sterility domain; KEGG: mpt:Mpe_A3296 nucleoside-diphosphate-sugar epimerase.
 
    0.462
Lcho_2934
TIGRFAM: riboflavin biosynthesis protein RibD; PFAM: CMP/dCMP deaminase zinc-binding; bifunctional deaminase-reductase domain protein; KEGG: mpt:Mpe_A2945 bifunctional protein diaminohydroxyphosphoribosylaminopyrimidine deaminase, 5-amino-6-(5-phosphoribosylamino)uracil reductase.
      
 0.432
Your Current Organism:
Leptothrix cholodnii
NCBI taxonomy Id: 395495
Other names: L. cholodnii SP-6, Leptothrix cholodnii SP-6, Leptothrix cholodnii str. SP-6, Leptothrix cholodnii strain SP-6
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