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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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luxSPutative S-ribosylhomocysteine lyase; 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. (160 aa)    
Predicted Functional Partners:
EHI73511.1
5'-methylthioadenosine/S-adenosylhomocysteine 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. Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.
 
 
 0.994
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.
    
 0.990
EHI75284.1
Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein.
    
 0.954
EHI75068.1
Putative cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family.
  
 
 0.942
EHI73931.1
Cystathionine gamma-synthase.
  
 
 0.932
mmuM
Homocysteine S-methyltransferase.
     
 0.913
EHI73936.1
Homoserine dehydrogenase family protein.
     
 0.913
EHI73515.1
Putative O-acetylhomoserine aminocarboxypropyltransferase.
     
 0.913
EHI73315.1
Aminotransferase, class II.
     
 0.912
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.
     
  0.911
Your Current Organism:
Streptococcus criceti
NCBI taxonomy Id: 873449
Other names: S. criceti HS-6, Streptococcus criceti HS-6, Streptococcus criceti str. HS-6, Streptococcus criceti strain HS-6
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