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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[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. (327 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.
 
 0.998
ACB24170.1
PFAM: cyclase/dehydrase; KEGG: mex:Mext_2800 cyclase/dehydrase.
       0.772
ACB22998.1
Transketolase central region; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
 
  
 0.747
ACB27556.1
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: biotin/lipoyl attachment domain-containing protein; FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glucose-inhibited division protein A; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: pnu:Pnuc_0736 dihydrolipoamide dehydrogenase.
 
  
 0.743
ACB23001.1
Pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
  
 0.739
ACB22934.1
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).
 
  
 0.737
ACB23003.1
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glucose-inhibited division protein A; fumarate reductase/succinate dehydrogenase flavoprotein domain protein; pyridine nucleotide-disulphide oxidoreductase dimerisation region; FAD dependent oxidoreductase; KEGG: mex:Mext_2790 dihydrolipoamide dehydrogenase.
 
  
 0.717
ACB27557.1
PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: rso:RSc1601 dihydrolipoamide acetyltransferase.
 
  
 0.665
ACB22936.1
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glucose-inhibited division protein A; pyridine nucleotide-disulphide oxidoreductase dimerisation region; HI0933 family protein; KEGG: mex:Mext_1648 dihydrolipoamide dehydrogenase.
 
  
 0.659
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).
 
   
 0.649
Your Current Organism:
Methylobacterium radiotolerans
NCBI taxonomy Id: 426355
Other names: M. radiotolerans JCM 2831, Methylobacterium radiotolerans ATCC 27329, Methylobacterium radiotolerans IAM 12098, Methylobacterium radiotolerans JCM 2831, Methylobacterium radiotolerans str. JCM 2831, Methylobacterium radiotolerans strain JCM 2831
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