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
metEPutative 5-methyltetrahydropteroyltriglutamate--homocysteine S-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. (757 aa)    
Predicted Functional Partners:
CUS_7787
Putative methionine synthase; Identified by match to protein family HMM PF00809; match to protein family HMM PF02310; match to protein family HMM PF02574; match to protein family HMM PF02607.
  
 
 0.983
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.
  
 0.983
metF
Methylenetetrahydrofolate reductase (NAD(P)H); Identified by match to protein family HMM PF02219; match to protein family HMM TIGR00676; Belongs to the methylenetetrahydrofolate reductase family.
 
 0.970
CUS_5219
O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase; Identified by match to protein family HMM PF01041; match to protein family HMM PF01053; match to protein family HMM TIGR01326.
  
 
 0.945
CUS_7999
O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase; Identified by match to protein family HMM PF01053; match to protein family HMM TIGR01326.
  
 
 0.945
ilvA
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.
  
 
 0.914
metC
Cystathionine beta-lyase; Identified by match to protein family HMM PF00266; match to protein family HMM PF01053; match to protein family HMM PF01212.
 
 
 0.901
luxS
S-ribosylhomocysteinase LuxS; 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.
    
 0.900
CUS_7341
Cys/Met metabolism PLP-dependent enzyme; Identified by match to protein family HMM PF01053.
  
 
 0.894
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.
     
 0.890
Your Current Organism:
Ruminococcus albus 8
NCBI taxonomy Id: 246199
Other names: R. albus 8, Ruminococcus albus str. 8
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