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
EHA60397.1KEGG: pmb:A9601_16511 ferredoxin; TIGRFAM: Ferredoxin [2Fe-2S], plant; PFAM: Ferredoxin. (122 aa)    
Predicted Functional Partners:
EHA62471.1
PFAM: Beta-ketoacyl synthase, N-terminal; 2-nitropropane dioxygenase, NPD; Beta-ketoacyl synthase, C-terminal; Acyl transferase; Phosphopantetheine-binding; KEGG: gvi:gll4226 modular polyketide synthase; SMART: Polyketide synthase, beta-ketoacyl synthase domain; Polyketide synthase, acyl transferase domain.
   
 0.970
EHA62472.1
KR domain protein; KEGG: gvi:gll4226 modular polyketide synthase; PFAM: Polyketide synthase, KR; SMART: Polyketide synthase/Fatty acid synthase, KR.
   
 0.970
EHA59278.1
KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal.
     
 0.881
ndhH
NAD(P)H-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
   
 
 0.811
EHA64351.1
PFAM: Photosystem I PsaF, reaction centre subunit III; KEGG: syf:Synpcc7942_1250 photosystem I reaction center subunit III precursor.
    
 
 0.808
psaE
Photosystem I reaction centre subunit IV/PsaE; Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase; Belongs to the PsaE family.
    
 
 0.808
ndhC
NAD(P)H-quinone oxidoreductase subunit 3; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
    
 
 0.807
ndhB
NAD(P)H-quinone oxidoreductase subunit 2; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
    
 
 0.804
ndhA
NADH dehydrogenase (quinone); NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
    
 
 0.804
EHA63025.1
TIGRFAM: Thioredoxin reductase; KEGG: pma:Pro1245 thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Thioredoxin domain.
   
 
 0.803
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
Server load: medium (44%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.