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
EHA60185.1Hypothetical protein; KEGG: xau:Xaut_4571 alpha/beta hydrolase domain-containing protein. (313 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.
 
 0.936
EHA62472.1
KR domain protein; KEGG: gvi:gll4226 modular polyketide synthase; PFAM: Polyketide synthase, KR; SMART: Polyketide synthase/Fatty acid synthase, KR.
 
 0.936
petC
Cytochrome b6-f complex iron-sulfur subunit; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
    
  0.913
EHA63429.1
4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
    
   0.862
ndhI
NAD(P)H-quinone oxidoreductase subunit I; 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.
    
   0.862
EHA63019.1
PFAM: NAD-dependent epimerase/dehydratase; KEGG: pmf:P9303_08511 putative chaperon-like protein for quinone binding in photosystem II.
   
   0.858
EHA63126.1
KEGG: vcn:VOLCADRAFT_76013 hypothetical protein.
   
   0.858
EHA63501.1
KEGG: sun:SUN_0875 long-chain fatty-acid-CoA ligase; PFAM: AMP-dependent synthetase/ligase.
  
 0.817
EHA61825.1
o-succinylbenzoate--CoA ligase; KEGG: pmf:P9303_27321 putative O-succinylbenzoic acid--CoA ligase (OSB-CoA synthetase); PFAM: AMP-dependent synthetase/ligase.
  
 0.817
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
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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