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
metXAHomoserine acetyltransferase (met2); Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the acetyl group of acetyl-CoA is initially transferred to the enzyme to form an acetyl- enzyme intermediate before subsequent transfer to homoserine to form the final product, O-acetylhomoserine. (358 aa)    
Predicted Functional Partners:
thrA
Aspartokinase I / homoserine dehydrogenase I (thrA); Similar to SP:P00561 GB:M10644 GB:V00360 GB:V00361 PID:147979 percent identity: 62.21; identified by sequence similarity; putative; In the C-terminal section; belongs to the homoserine dehydrogenase family.
 
 
 0.983
metE
5-methyltetrahydropteroyltriglutamate- homocysteine methyltransferase (metE); Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family.
    
 0.712
trpC
Indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase (trpC); Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain (By similarity).
   
 
  0.707
cysK
Cysteine synthetase (cysK); Similar to GB:M21451 SP:P11096 GB:X12615 PID:145686 PID:41201 percent identity: 70.65; identified by sequence similarity; putative; Belongs to the cysteine synthase/cystathionine beta- synthase family.
 
  
 0.704
metB
Cystathionine gamma-synthase (metB); Catalyzes the formation of L-cystathionine from O-succinyl-L- homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2- oxobutanoate, succinate and ammonia (By similarity).
 
  
 0.675
cysE
Serine acetyltransferase (cysE); Similar to SP:P05796 GB:M15745 GB:M34333 PID:145676 PID:145694 percent identity: 73.05; identified by sequence similarity; putative.
    
 0.636
srmB
ATP-dependent RNA helicase (srmB); DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity; Belongs to the DEAD box helicase family. SrmB subfamily.
   
  
 0.613
glyA
Serine hydroxymethyltransferase (serine methylase) (glyA); 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.
     
 0.603
thrB
Homoserine kinase (thrB); Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
     
 0.597
ilvA
Threonine deaminase (ilvA); 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 (By similarity).
  
 
 0.593
Your Current Organism:
Haemophilus influenzae
NCBI taxonomy Id: 71421
Other names: H. influenzae Rd KW20, Haemophilus influenzae KW20, Haemophilus influenzae Rd, Haemophilus influenzae Rd KW20
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.