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
lipBOctanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. (287 aa)    
Predicted Functional Partners:
lipA
Lipoic acid synthetase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
 
 0.999
gcvH
Glycine cleavage H-protein (lipoate-binding); The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
   
 0.978
lplA
Lipoate-protein ligase A.
   
 0.928
gcvP
Glycine dehydrogenase [decarboxylating] (Glycine decarboxylase) (Glycine cleavage system P-protein); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
     
 0.877
acpP
Acyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis.
   
 0.873
fabF
3-oxoacyl-[acyl-carrier-protein] synthase (Beta-ketoacyl-ACP synthase); Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
    
 0.824
birA
BirA, Biotin-(acetyl-CoA carboxylase) ligase; Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. ATP + Biotin + Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] <=> AMP + Pyrophosphate + [Acetyl-CoA:carbon-dioxide ligase (ADP-forming)].
     
 0.782
pdxS
Pyridoxal biosynthesis lyase pdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family.
      
 0.708
CBL57356.1
Iron-sulfur protein.
      
 0.705
pdhB
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Succinyl-CoA + Enzyme N6-(dihydrolipoyl)lysine <=> CoA + [Dihydrolipoyllysine-residue succinyltransferase]S-succinyldihydrolipoyllysine, Glutaryl-CoA + Dihydrolipoamide <=> CoA + S-Glutaryldihydrolipoamide.
 
 
 0.696
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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