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
EKE99892.1KEGG: npu:Npun_F0648 9.9e-97 acyl-CoA dehydrogenase type 2. (395 aa)    
Predicted Functional Partners:
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.
    
 0.913
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.
    
 0.907
EKE97447.1
AMP-binding enzyme; KEGG: ava:Ava_1613 0. non-ribosomal peptide synthase.
  
 
 0.890
EKF02499.1
Hypothetical protein; KEGG: fba:FIC_02097 4.9e-07 catalase.
  
 0.890
EKF00081.1
4Fe-4S binding domain protein; KEGG: mbu:Mbur_0285 7.3e-10 formylmethanofuran dehydrogenase, subunit F K00205; Psort location: Cytoplasmic, score: 8.96.
  
 0.886
ndhI
NADH-plastoquinone oxidoreductase, I subunit; 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; Belongs to the complex I 23 kDa subunit family.
  
 0.886
EKE97400.1
KEGG: ava:Ava_3046 0. ferredoxin (flavodoxin) oxidoreductase K03737.
  
 
 0.869
EKF00361.1
Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin.
  
 
 0.869
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.
     
 0.866
EKE96453.1
KEGG: npu:Npun_F3359 5.4e-233 beta-ketoacyl synthase; Psort location: CytoplasmicMembrane, score: 9.82.
  
 0.863
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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