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
menE1O-succinylbenzoate-CoA ligase; ATP + 2-Succinylbenzoate + CoA <=> AMP + Pyrophosphate + 2-Succinylbenzoyl-CoA. (352 aa)    
Predicted Functional Partners:
mmgA
2 Acetyl-CoA <=> CoA + Acetoacetyl-CoA and Acetyl-CoA + Butanoyl-CoA <=> CoA + 3-Oxohexanoyl-CoA; Belongs to the thiolase-like superfamily. Thiolase family.
 
 
 0.933
menD
Menaquinone biosynthesis protein; Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2- succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Belongs to the TPP enzyme family. MenD subfamily.
 
  
 0.761
rplF
50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
    
  0.678
ispE
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
      
 0.677
ispF
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (MECPS) (MECDP-synthase); Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
   
  
 0.669
ispD
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
     
 0.667
dxr
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family.
      
 0.666
menB
Naphthoate synthase (Dihydroxynaphthoic acid synthetase); Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2- naphthoyl-CoA (DHNA-CoA); Belongs to the enoyl-CoA hydratase/isomerase family. MenB subfamily.
 
 
 0.664
dxs
Deoxyxylulose-5-phosphate synthase; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP); Belongs to the transketolase family. DXPS subfamily.
      
 0.660
ispG
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin); Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family.
      
 0.659
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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