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
AJI79375.1Arabinose efflux permease family protein; PFAM: Major Facilitator Superfamily. (384 aa)    
Predicted Functional Partners:
gcvP
PFAM: Glycine cleavage system P-protein; TIGRFAM: glycine dehydrogenase (decarboxylating); Belongs to the GcvP family.
       0.624
gcvT
Glycine cleavage system T protein; The glycine cleavage system catalyzes the degradation of glycine.
  
    0.618
sucB
2-oxoglutarate dehydrogenase E2 component; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); e3 binding domain; Biotin-requiring enzyme; TIGRFAM: 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase.
  
    0.541
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.
       0.496
AJI79741.1
Tellurite resistance protein-like permease; PFAM: Voltage-dependent anion channel.
  
     0.459
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.
  
    0.437
AJI79373.1
Hypothetical protein.
   
   0.400
Your Current Organism:
Corynebacterium singulare
NCBI taxonomy Id: 161899
Other names: C. singulare, CCUG 37330, CIP 105491, DSM 44357, IBS B52218, IFO 16162, JCM 10385, NBRC 16162
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.