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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
metHMethionine synthase (5-methyltetrahydrofolate:L-homocysteine S-methyltransferase); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. (1163 aa)    
Predicted Functional Partners:
metF
5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H; Belongs to the methylenetetrahydrofolate reductase family.
 
 
 0.999
metB
Cystathionine gamma-synthase (O-succinylhomoserine (thiol)-lyase).
  
 
 0.988
metK
S-adenosylmethionine synthetase (Methionine adenosyltransferase) (AdoMet synthetase) (MAT); Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
  
 
 0.971
gcvT1
Glycine cleavage system T protein, aminomethyltransferase; S-Aminomethyldihydrolipoylprotein + Tetrahydrofolate <=> Dihydrolipoylprotein + 5,10-Methylenetetrahydrofolate + NH3.
  
 
 0.966
luxS
S-ribosylhomocysteine lyase (Autoinducer-2 production protein luxS) (AI-2 synthesis protein); Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family.
    
 0.964
fhs
Formate--tetrahydrofolate ligase; ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate; Belongs to the formate--tetrahydrofolate ligase family.
  
 
 0.962
thrA/hom
L-Homoserine + NAD+ <=> L-Aspartate 4-semialdehyde + NADH + H+ and L-Homoserine + NADP+ <=> L-Aspartate 4-semialdehyde + NADPH + H+.
  
 
 0.961
glyA
Glycine hydroxymethyltransferase precursor; 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.
     
 0.954
folA
Dihydrofolate reductase; 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. tetrahydrofolate biosynthesis; tetrahydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 3/3.
    
 0.927
aspC
Aminotransferase, class I and II (Aspartate/tyrosine/aromatic aminotransferase, transaminase A); Annotation inferred by similarity with protein ybdl E coli (swiss prot P77806).
   
 
 0.927
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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