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
menEO-succinylbenzoate-CoA ligase. (466 aa)    
Predicted Functional Partners:
menC
O-succinylbenzoate-CoA synthase; Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1- carboxylate (SHCHC) to 2-succinylbenzoate (OSB).
 
 
 0.992
menB
Naphthoate synthase; Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2- naphthoyl-CoA (DHNA-CoA).
 
  
 0.991
menH
acyl-CoA thioester hydrolase; Catalyzes a proton abstraction reaction that results in 2,5- elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6- hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
 
 0.915
menD
Menaquinone biosynthesis protein MenD; 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.
 
   
 0.911
menF
Menaquinone-specific isochorismate synthase; Catalyzes the conversion of chorismate to isochorismate.
 
   
 0.842
fadB
Fatty oxidation complex alpha subunit, enoyl-CoA hydratase; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
 
 
 0.830
fadJ
Fatty acid oxidation complex alpha subunit [includes: enoyl-co hydratase; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. Belongs to the enoyl-CoA hydratase/isomerase family. In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
 
 
 0.830
rplF
50E 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.
    
 0.784
rplB
50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
   
 
 0.749
rplC
50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
   
 
 0.747
Your Current Organism:
Aliivibrio wodanis
NCBI taxonomy Id: 80852
Other names: A. wodanis, ATCC BAA-104, Aliivibrio wodanis (Lunder et al. 2000) Urbanczyk et al. 2007, DSM 22225, LMG 24053, LMG:24053, NCIMB 13582, Vibrio wodanis, Vibrio wodanis Lunder et al. 2000, strain NVI 88/441
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