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
lipALipoic 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. (333 aa)    
Predicted Functional Partners:
lipB
Lipoate-protein ligase B; 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.
 
 0.999
gcvH
Glycine cleavage system H protein; 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.
 
 
 0.930
Rpic_1944
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: biotin/lipoyl attachment domain-containing protein; FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: rso:RSc1603 probable dihydrolipoamide dehydrogenase (E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes) protein.
 
  
 0.730
Rpic_4647
PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: bte:BTH_II0930 probable pyruvate dehydrogenase, E2 component, dihydrolipoamide acetyltransferase.
 
  
 0.662
Rpic_1098
2-oxoglutarate dehydrogenase, E2 subunit, dihydrolipoamide succinyltransferase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
 
  
 0.628
Rpic_3047
Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
 
 
    0.628
Rpic_3742
PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: rso:RSc0014 probable glutathione reductase oxidoreductase protein.
 
  
 0.628
pdhA
Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
   
 0.620
Rpic_4646
Transketolase central region; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
 
  
 0.601
Rpic_1099
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; fumarate reductase/succinate dehydrogenase flavoprotein domain protein; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: rso:RSc1271 dihydrolipoamide dehydrogenase.
 
  
 0.600
Your Current Organism:
Ralstonia pickettii 12J
NCBI taxonomy Id: 402626
Other names: R. pickettii 12J, Ralstonia pickettii str. 12J, Ralstonia pickettii strain 12J
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.