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
KXU57576.1Hypothetical protein; KEGG: stj:SALIVA_2020 2.2e-110 putative methylcobalamin:homocysteine methyltransferase (Methionine synthase); Psort location: Cytoplasmic, score: 8.96. (204 aa)    
Predicted Functional Partners:
KXU58148.1
Hypothetical protein; KEGG: stj:SALIVA_2020 1.7e-85 putative methylcobalamin:homocysteine methyltransferase (Methionine synthase); Psort location: Cytoplasmic, score: 8.96.
 
     0.976
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.
  
 0.956
MetB1
KEGG: stj:SALIVA_0327 8.3e-189 metB; cystathionine gamma-synthase (CGS) (O-succinylhomoserine (thiol)-lyase); Psort location: Cytoplasmic, score: 9.97.
  
 
 0.947
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.
  
 
  0.928
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.
 
  
 0.923
CysD
O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase; KEGG: stn:STND_0945 3.3e-224 O-acetylhomoserine sulfhydrylase, putative; K01740 O-acetylhomoserine (thiol)-lyase; Psort location: Cytoplasmic, score: 9.97.
  
 
 0.914
KXU59492.1
KEGG: ssr:SALIVB_0350 1.4e-207 patB; putative aminotransferase B K14155; Psort location: Cytoplasmic, score: 9.97.
    
  0.901
KXU56311.1
GAF domain protein; KEGG: pfc:PflA506_1782 1.1e-28 yebR; free methionine-(R)-sulfoxide reductase YebR K07170.
     
  0.900
Hom
KEGG: ssr:SALIVB_0491 7.6e-218 hom; homoserine dehydrogenase K00003; Psort location: Cytoplasmic, score: 9.97.
  
 
 0.845
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.
  
 
 0.821
Your Current Organism:
Streptococcus salivarius
NCBI taxonomy Id: 1304
Other names: ATCC 7073, CCUG 11878, CCUG 17825, CCUG 50207, CIP 102503, DSM 20560, JCM 5707, LMG 11489, LMG:11489, NCIMB 701779, NCTC 8618, S. salivarius, Streptococcus salivarius subsp. salivarius, Streptococcus sp. FStet12, Streptococcus sp. HSISS4
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