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
APZ04015.1Succinate-semialdehyde dehydrogenase; In Escherichia coli this enzyme appears to be an NAD+/NADP+-dependent succinate semialdehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (456 aa)    
Predicted Functional Partners:
APZ06836.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.956
APZ04185.1
Fumarate reductase (quinol) flavoprotein subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.921
APZ05782.1
Succinate dehydrogenase flavoprotein subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
   
 0.921
gabD
Succinate-semialdehyde dehydrogenase (NADP(+)); Catalyzes the formation of succinate from succinate semialdehyde; NADP dependent; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.915
APZ04186.1
Succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
   
 
 0.910
sdhB
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.910
APZ06437.1
Succinate-semialdehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.910
APZ05230.1
4-aminobutyrate--2-oxoglutarate transaminase; Catalyzes the formation of succinate semialdehyde and glutamate from 4-aminobutanoate and 2-oxoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
   
 0.906
APZ05781.1
Succinate dehydrogenase, hydrophobic membrane anchor protein; Membrane-anchoring subunit of succinate dehydrogenase (SDH).
   
 
 0.906
sdhC
Succinate dehydrogenase cytochrome b556 large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.905
Your Current Organism:
Kosakonia cowanii
NCBI taxonomy Id: 208223
Other names: CCUG 45998 A, CCUG 45998 B, CIP 107300, DSM 18146, Enterobacter cowanii, Enterobacter cowanii Inoue et al. 2001, JCM 10956, K. cowanii, Kosakonia cowanii (Inoue et al. 2001) Brady et al. 2013, LMG 23569, LMG:23569, NIH group 42, strain 888-76, strain KSK 246, strain UM-79
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.