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
AFZ47305.1Ferredoxin; PFAM: 2Fe-2S iron-sulfur cluster binding domain; InterPro IPR001041; KEGG: ava:Ava_3217 ferredoxin; PFAM: ferredoxin; SPTR: Ferredoxin. (111 aa)    
Predicted Functional Partners:
AFZ46264.1
AMP-dependent synthetase and ligase; PFAM: AMP-binding enzyme; COGs: COG0318 Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; InterPro IPR020845:IPR000873; KEGG: cyc:PCC7424_1874 beta-ketoacyl synthase; PFAM: AMP-dependent synthetase and ligase; SPTR: Beta-ketoacyl synthase.
  
 
 0.898
AFZ46265.1
Beta-ketoacyl synthase; PFAM: Acyl transferase domain; Phosphopantetheine attachment site; KR domain; Beta-ketoacyl synthase, N-terminal domain; AMP-binding enzyme; Sulfotransferase domain; Beta-ketoacyl synthase, C-terminal domain; COGs: COG3321 Polyketide synthase modules and related protein; InterProIPR000639:IPR009081:IPR006162:IPR018201:IPR 000873:IPR006163:IPR014030:IPR014031:IPR014043:IPR013968:I PR000863:IPR000073; KEGG: cyc:PCC7424_1874 beta-ketoacyl synthase; PFAM: Beta-ketoacyl synthase; phosphopantetheine-binding; AMP-dependent synthetase and ligase; Acyl transferase; KR do [...]
  
 
 0.898
AFZ47304.1
PFAM: Cellulose synthase; COGs: COG1215 Glycosyltransferase probably involved in cell wall biogenesis; InterPro IPR001173; KEGG: amr:AM1_4863 cellulose synthase catalytic subunit; PFAM: glycosyl transferase family 2; SPTR: Cellulose synthase superfamily.
       0.746
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.
  
 
 
 0.744
AFZ48815.1
Glutamate synthase (NADH) small subunit; PFAM: Pyridine nucleotide-disulphide oxidoreductase; TIGRFAM: glutamate synthases, NADH/NADPH, small subunit; COGs: COG0493 NADPH-dependent glutamate synthase beta chain and related oxidoreductase; InterPro IPR013027:IPR000759:IPR006005; KEGG: cyc:PCC7424_3656 glutamate synthase, NADH/NADPH, small subunit; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; SPTR: Glutamate synthase, NADH/NADPH, small subunit; TIGRFAM: glutamate synthase, NADH/NADPH, small subunit.
    
 0.669
AFZ47643.1
PFAM: Photosystem I reaction centre subunit III; InterPro IPR003666; KEGG: cyh:Cyan8802_2714 photosystem I reaction center protein PsaF subunit III; PFAM: photosystem I reaction center protein PsaF subunit III; SPTR: Photosystem I reaction center protein PsaF subunit III.
  
 
 0.658
ndhH
NADH dehydrogenase subunit D; 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.
   
 
 0.614
ndhC
NADH dehydrogenase subunit A; 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.
   
 
 0.602
AFZ47083.1
PFAM: PsaD; InterPro IPR003685; KEGG: cyh:Cyan8802_0387 photosystem I protein PsaD; PFAM: photosystem I protein PsaD; SPTR: Photosystem I protein PsaD.
    
 
 0.597
ndhK
NADH dehydrogenase subunit B; 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; Belongs to the complex I 20 kDa subunit family.
  
   0.596
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
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