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
AFZ46788.1Alpha/beta hydrolase fold protein; COGs: COG2267 Lysophospholipase; InterPro IPR000073; KEGG: ana:alr0851 lysophospholipase; PFAM: alpha/beta hydrolase fold; SPTR: Lysophospholipase. (292 aa)    
Predicted Functional Partners:
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.
   
 
 0.876
ndhJ
NADH dehydrogenase subunit C; 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.
   
 
 0.850
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.
 
 
 0.822
ndhA
NADH dehydrogenase 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.
    
   0.802
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 [...]
 
 
0.801
AFZ46787.1
InterPro IPR002123; KEGG: ava:Ava_2827 phospholipid/glycerol acyltransferase; SMART: phospholipid/glycerol acyltransferase; SPTR: Phospholipid/glycerol acyltransferase.
  
 
 0.789
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.
   
   0.774
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.
    
   0.749
ndhB
NADH dehydrogenase subunit N; 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.
    
   0.672
AFZ47188.1
4Fe-4S ferredoxin iron-sulfur-binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
   
   0.659
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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