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
etfAElectron transfer flavoprotein, alpha subunit; The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various dehydrogenases. In Bacteria, ETFs are produced under specific growth conditions, receiving electrons only from the oxidation of specific substrates. ETFs are heterodimeric proteins composed of an alpha and beta subunit, and contain an FAD cofactor and an AMP molecule. EtfA codes the alpha subunit that participate, with the alpha subunit, to the binding of the FAD molecule; Localized in the cytoplasm; High confidence in function and specificity. (322 aa)    
Predicted Functional Partners:
etfB
Electron transfer flavoprotein, beta subunit; The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various dehydrogenases. In Bacteria, ETFs are produced under specific growth conditions, receiving electrons only from the oxidation of specific substrates. ETFs are heterodimeric proteins composed of an alpha and beta subunit, and contain an FAD cofactor and an AMP molecule. EtfB codes the beta subunit that binds the AMP molecule; Localized in the cytoplasm; High confidence in function and specificity.
 
 0.999
bcdA
Butyryl-CoA dehydrogenase converts the Butanoyl-CoA to 2-butenoyl-CoA. It uses electron transfer flavoprotein (FAD) as its electron acceptor; Localized in the cytoplasm; High confidence in function and specificity.
 
 0.991
gcdH
Glutaryl-CoA dehydrogenase catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO2 in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism; Uses FAD as prosthetic group; Belongs to the acyl-CoA dehydrogenase family; Localized in the cytoplasm; High confidence in function and specificity.
 
 0.985
CAZ94724.1
Acyl-CoA dehydrogenases catalyze the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. Reoxidation of the flavin involves transfer of electrons to ETF (electron transfering flavoprotein). These enzymes are homodimers containing one molecule of FAD; Localized in the cytoplasm; Specificity unclear.
 
 0.980
fadE
Acyl-CoA dehydrogenase is involved in fatty acid degradation. It catalyzes the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3- enoyl CoA-products with concommitant reduction of enzyme- bound FAD. In Bacillus subtilis, this protein, formerly known as yusJ protein, has been renamed FadE by Matsuoka et al (JBC, 2007). Localized in the cytoplasm; Specificity unclear.
 
 0.962
acxA
Acyl-coA oxidase, with FAD cofactor, converts acyl-CoA into trans-2-enoyl-CoA; Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18); Family membership.
 
 
 0.799
fadN
3-Hydroxyl-CoA dehydrogenase / Enoyl-CoA hydratase; Modular protein containing a N-terminal 3-Hydroxyl-CoA dehydrogenase domain and a C-terminal Enoyl-CoA hydratase domain. In Bacillus subtilis, this protein was formerly known as YusL, and has been renamed FadN by Matsuoka et al (JBC, 2007). FadN is involved in fatty acid degradation. 3-Hydroxyl-CoA dehydrogenase catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. It uses NAD as cofactor. Enoyl-CoA hydratase catalyzes the hydratation of 2-trans-enoyl-CoA into 3-hydroxyacyl-CoA. Localized in the cytoplasm; High confidence in [...]
  
 
 0.775
CAZ94933.1
UVR domain Protein; Conserved hypothetical protein belonging to the DUF151 family. Also displays a C-terminal UVR domain (~35 residues). The UVR domain has been first described in UvrB and UvrC, enzymes involved in DNA repair. This domain in UvrB can interact with the homologous domain in UvrC throughout a putative coiled coil structure; Localized in the cytoplasm; Conserved hypothetical protein.
       0.727
pdhB
Pyruvate dehydrogenase, E1 component subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
  
 
 0.711
crtA
3-hydroxybutyryl-CoA dehydratase; Enzyme, also called crotonase, that participates to the fatty acid metabolism in the Butyrate/butanol-producing pathway; High confidence in function and specificity; Belongs to the enoyl-CoA hydratase/isomerase family.
 
 0.688
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.