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
metCCystathionine gamma-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (391 aa)    
Predicted Functional Partners:
metH
Homocysteine methyltransferase; Catalyzes the formation of 5,10-methylenetetrahydrofolate from 5-methyltetrahydrofolate and S-adenosyl-L-homocysteine and methionine from S-adenosyl-L-methionine and L-homocysteine; expressed in B. subtilis under methionine starvation conditions; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
metE
5-methyltetrahydropteroyltriglutamate-- homocysteine methyltransferase; 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.
 
 
 0.993
metB1
Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 
0.983
mccA
Cysteine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.958
cysK
Cysteine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the cysteine synthase/cystathionine beta- synthase family.
  
 0.949
cysD
O-acetylhomoserine aminocarboxypropyltransferase; Catalyzes the formation of L-methionine and acetate from O-acetyl-L-homoserine and methanethiol; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
0.909
hom
Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.903
luxS
S-ribosylhomocysteinase; 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.
  
 
 0.893
ilvA-2
Threonine dehydratase; 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.
  
 
 0.885
thrB
Serine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
  
 
 0.885
Your Current Organism:
Staphylococcus microti
NCBI taxonomy Id: 569857
Other names: CCM 4903, CCUG 55861, DSM 22147, NCTC 13832, S. microti, Staphylococcus microti Novakova et al. 2010, Staphylococcus sp. CCM 4903, Staphylococcus sp. CCM 4904, strain 4005-LJ(m)
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