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
OOR92182.15-methyltetrahydropteroyltriglutamate-- homocysteine methyltransferase; Catalyzes the formation of tetrahydropteroyl-L-glutamate and methionine from L-homocysteine and 5-methyltetrahydropteroyltri-L-glutamate; Derived by automated computational analysis using gene prediction method: Protein Homology. (344 aa)    
Predicted Functional Partners:
OOR92183.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.988
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.
  
 0.974
ahcY
Adenosylhomocysteinase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
  
 
 0.961
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
  
 
 0.961
metG
methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
     
 0.909
OOR91124.1
Catalyzes the formation of L-glutamate and an aromatic oxo acid from an aromatic amino acid and 2-oxoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.903
OOR90159.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
 
 0.885
hom
Homoserine dehydrogenase; Catalyzes the formation of L-aspartate 4-semialdehyde from L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.882
ilvA
Threonine ammonia-lyase, 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.
  
 
 0.823
cysK
Cysteine synthase A; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the cysteine synthase/cystathionine beta- synthase family.
     
 0.817
Your Current Organism:
Moraxella bovis
NCBI taxonomy Id: 476
Other names: ATCC 10900, CCUG 2133, CIP 70.40, DSM 6328, Haemophilus bovis, JCM 20472, LMG 986, LMG:986, M. bovis, Moraxella duplex des bovids, NCTC 11013
Server load: low (14%) [HD]