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
MTA/SAH 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 phosphorylas [...]
 
 
 0.986
ADO46919.1
KEGG: enc:ECL_02360 cystathionine beta-synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein.
  
 
 0.945
metE
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.
    
 0.942
ADO47017.1
KEGG: cko:CKO_04402 cystathionine beta-lyase; TIGRFAM: cystathionine beta-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein.
 
 
 0.941
ADO48285.1
KEGG: pmr:PMI0626 cystathionine beta-lyase; TIGRFAM: cystathionine beta-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein.
 
 
 0.935
ADO50565.1
O-succinylhomoserine (thiol)-lyase; KEGG: cro:ROD_38041 cystathionine gamma-synthase; TIGRFAM: O-succinylhomoserine (thiol)-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein.
 
 
 0.935
ADO50380.1
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.
    
 0.930
ADO46831.1
PFAM: aminotransferase class I and II; KEGG: cko:CKO_04539 hypothetical protein.
  
  
  0.912
ADO48462.1
PFAM: aminotransferase class I and II; KEGG: kpn:KPN_01511 bifunctional PLP-dependent beta-cystathionase; repressor of maltose regulon through interaction with MalT.
     
  0.900
ADO47605.1
KEGG: enc:ECL_03744 cysteine synthase A; TIGRFAM: cysteine synthase A; cysteine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; Belongs to the cysteine synthase/cystathionine beta- synthase family.
 
 
 0.866
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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