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
luxSQuorum-sensing autoinducer 2 (AI-2), 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. (171 aa)    
Predicted Functional Partners:
mtnN
Methylthioadenosine nucleosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation. Belongs to the PNP/UDP [...]
 
 
 0.985
ABP62078.1
TIGRFAM: cystathionine beta-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent enzymes; KEGG: sbo:SBO_3002 cystathionine beta-lyase.
 
 
 0.944
ABP62690.1
O-succinylhomoserine (thiol)-lyase; KEGG: ssn:SSO_4113 cystathionine gamma-synthase; TIGRFAM: O-succinylhomoserine (thiol)-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent enzymes.
 
 
 0.940
ABP60663.1
PFAM: Methionine synthase, vitamin-B12 independent; KEGG: eca:ECA1113 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase.
 
  
 0.937
ABP58912.1
Methionine synthase (B12-dependent); 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.
    
 0.925
ABP60449.1
Cystathionine beta-synthase; PFAM: CBS domain containing protein; Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: yen:YE1470 cystathionine beta-lyase.
  
 
 0.924
ABP60788.1
PFAM: Methionine synthase, vitamin-B12 independent; Cobalamin-independent synthase MetE, N-terminal domain protein; KEGG: eca:ECA3126 5-methyltetrahydropteroyltriglutamate- homocystein e methyltransferase.
    
 0.918
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.
    
 0.918
ABP59513.1
PFAM: homocysteine S-methyltransferase; KEGG: ecj:JW0253 S-methylmethionine:homocysteine methyltransferase.
     
 0.915
ABP60505.1
PFAM: aminotransferase, class I and II; KEGG: ssn:SSO_1536 enzyme that may degrade or block biosynthesis of endogenous mal inducer, probably aminotrasferase.
  
  
  0.911
Your Current Organism:
Enterobacter sp. 638
NCBI taxonomy Id: 399742
Other names: E. sp. 638
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