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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
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Co-occurrence
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[Homology]
Score
ctaDICytochrome c oxidase polypeptide I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (551 aa)    
Predicted Functional Partners:
ctaEII
Cytochrome c oxidase polypeptide III; Sly1025100.
 
 0.999
ctaCI
Cytochrome c oxidase polypeptide II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
 
 0.999
ctaEI
Cytochrome c oxidase polypeptide III; Sly1021950.
 0.999
ctaB
Heme O synthase, protoheme IX farnesyltransferase COX10-CtaB; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
 
 0.998
ctaC
Cytochrome c oxidase polypeptide II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
 
 0.998
petB
Cytochrome b6-f complex subunit, cytochrome b6; 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.
 
 0.993
hoxF
NAD-reducing hydrogenase subunit HoxF; Sly1009910.
   
 
 0.962
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.
   
 0.929
ctaDII
Cytochrome c oxidase polypeptide I; Sly1025110; Belongs to the heme-copper respiratory oxidase family.
  
  
 
0.903
ndhA
NAD(P)H-quinone oxidoreductase chain 1; 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.
   
 
 0.902
Your Current Organism:
Synechocystis sp. PCC6714
NCBI taxonomy Id: 1147
Other names: Aphanocapsa sp. (strain 5.3A), Aphanocapsa sp. 5-3A, Aphanocapsa sp. 5.3A, S. sp. PCC 6714, Synechocystis sp. (ATCC 27178), Synechocystis sp. (PCC 6714), Synechocystis sp. (strain PCC 6714), Synechocystis sp. ATCC 27178, Synechocystis sp. PCC 6714, Synechocystis sp. SAG 92.79, Synechocystis sp. UTCC 98, Synechocystis sp. UTEX 2470
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