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
lplALipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. (338 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.
 
 
 0.982
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.
 
 
 0.970
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.
   
 0.940
ABP59348.1
Pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.823
ABP59908.1
2-oxoglutarate dehydrogenase E2 component; 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).
 
 0.809
ABP59907.1
KEGG: sec:SC0740 2-oxoglutarate dehydrogenase (decarboxylase component); TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase, E1 component; Transketolase, central region.
    
  0.797
ABP59349.1
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glucose-inhibited division protein A; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: stm:STM0154 dihydrolipoamide dehydrogenase.
 
 
 0.738
ABP62568.1
TIGRFAM: glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: ecc:c4299 glutathione reductase.
 
 
 0.710
prs
Ribose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
   
 
 0.702
ABP59233.1
KEGG: sec:SC4421 membrane protein, transcribed divergently from SerB.
       0.675
Your Current Organism:
Enterobacter sp. 638
NCBI taxonomy Id: 399742
Other names: E. sp. 638
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