close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
mmuMPFAM: Homocysteine S-methyltransferase. (288 aa)    
Predicted Functional Partners:
metE
Methionine synthase (B12-independent); 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.
   
 
 0.920
metB
Cystathionine beta-lyase/cystathionine gamma-synthase; PFAM: Cys/Met metabolism PLP-dependent enzyme.
  
 
 0.918
metK
Methionine adenosyltransferase; 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.
     
 0.914
yhcE
Methionine synthase II (cobalamin-independent); PFAM: Cobalamin-independent synthase, Catalytic domain.
   
 
 0.913
AJI78122.1
O-acetylhomoserine sulfhydrylase; PFAM: Cys/Met metabolism PLP-dependent enzyme; TIGRFAM: OAH/OAS sulfhydrylase.
     
 0.908
AJI77875.1
S-ribosylhomocysteine lyase; 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.
     
 0.906
metC
Cystathionine beta-lyase; PFAM: Aminotransferase class I and II.
     
  0.900
hom
PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain.
   
 
 0.815
cysK
Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthase A; cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family.
     
 0.810
ilvA
L-threonine ammonia-lyase; 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.
     
 0.802
Your Current Organism:
Corynebacterium singulare
NCBI taxonomy Id: 161899
Other names: C. singulare, CCUG 37330, CIP 105491, DSM 44357, IBS B52218, IFO 16162, JCM 10385, NBRC 16162
Server load: low (34%) [HD]