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
metE5-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. (772 aa)    
Predicted Functional Partners:
yitJ
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.
 0.998
metH
Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
  
 
 0.983
ahcY
S-adenosyl-L-homocysteine hydrolase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
 
 
 0.974
metK
S-adenosylmethionine synthetase; 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.
  
 0.972
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.
    
 0.956
metC1
Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.946
metC3
Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.946
yxjG
5-methyltetrahydropteroyltriglutamate-- homocysteine methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
  0.938
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.
  
 
 0.926
mmuM
Converts homocysteine and S-adenosyl-methionine to methionine and S-adenosyl-homocysteine or S-methyl-methionine and homocysteine to two methionines; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.920
Your Current Organism:
Paenibacillus polymyxa
NCBI taxonomy Id: 1406
Other names: ATCC 842, Aerobacillus polymyxa, Bacillus polymyxa, Bacillus sp. NCIM 2538, Bacillus sp. NCIM 2540, Bacillus sp. NCIM 2726, Bacillus sp. RP 2.2, CCUG 7426, CFBP 4258, CIP 66.22, Clostridium polymyxa, DSM 36, Granulobacter polymyxa, HAMBI 635, IAM 13419, IFO 15309, JCM 2507, LMG 13294, LMG:13294, NBRC 15309, NCCB 24016, NCIB 8158, NCIB:8158, NCTC 10343, NRRL B-4317, P. polymyxa, Paenibacillus sp. JCM 8035, Paenibacillus sp. JCM 8036, Paenibacillus sp. JCM 8037, Paenibacillus sp. JCM 8038, Paenibacillus sp. JCM 8039, Paenibacillus sp. WLY78, VKM B-514
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