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
Databases
Textmining
[Homology]
Score
metXSHomoserine O-acetyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. (381 aa)    
Predicted Functional Partners:
ACD14759.1
TIGRFAM: methionine biosynthesis protein MetW; PFAM: Methionine biosynthesis MetW protein; Methyltransferase type 11; KEGG: bxe:Bxe_A4389 hypothetical protein.
  
 0.998
ACD17164.1
O-acetylhomoserine/O-acetylserine sulfhydrylase; KEGG: bxe:Bxe_A1357 O-acetylhomoserine aminocarboxypropyltransferase; TIGRFAM: O-acetylhomoserine/O-acetylserine sulfhydrylase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein.
 
 
 0.988
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
 
  
 0.963
ACD16214.1
PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; KEGG: bxe:Bxe_A2381 homoserine dehydrogenase.
 
 0.957
ACD14698.1
Glycine hydroxymethyltransferase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein; glycine hydroxymethyltransferase; aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: mka:MK0122 glycine hydroxymethyltransferase.
    
 0.832
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.
    
 0.832
glyA-2
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.
    
 0.832
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.
  
 
 0.831
ACD16280.1
PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: bxe:Bxe_A2315 putative amino-acid dehydratase.
  
 
 0.831
ilvA-2
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.
  
 
 0.831
Your Current Organism:
Paraburkholderia phytofirmans
NCBI taxonomy Id: 398527
Other names: Burkholderia phytofirmans PsJN, Burkholderia sp. PsJN, P. phytofirmans PsJN, Paraburkholderia phytofirmans PsJN
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.