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
Afer_1824Cytochrome c oxidase subunit 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). (257 aa)    
Predicted Functional Partners:
Afer_1707
PFAM: cytochrome c oxidase subunit I; KEGG: syp:SYNPCC7002_A0726 cytochrome oxidase II large subunit; Belongs to the heme-copper respiratory oxidase family.
 0.999
Afer_1822
Hypothetical protein; KEGG: fal:FRAAL5121 putative integral membrane protein.
 
 0.999
Afer_1823
Cytochrome c oxidase, subunit 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.
 0.999
Afer_1825
PFAM: Cytochrome b/b6 domain; KEGG: fre:Franean1_1812 cytochrome b/b6 domain- containing protein.
 
 
 0.999
Afer_1826
PFAM: Rieske [2Fe-2S] domain protein; KEGG: fal:FRAAL5110 ubiquinol-cytochrome c reductase iron-sulfur subunit (Rieske iron-sulfur protein).
 
 0.999
Afer_1828
PFAM: cytochrome c oxidase subunit III; KEGG: mjl:Mjls_3302 cytochrome c oxidase, subunit III.
 
 0.999
ctaB
Protoheme IX farnesyltransferase; 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.
 
 
 0.996
Afer_0375
KEGG: fre:Franean1_6082 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
  
 
 0.949
nuoH
NADH dehydrogenase (quinone); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
  
 
 0.942
Afer_1827
PFAM: cytochrome c class I; KEGG: fre:Franean1_1810 cytochrome c class I.
 
 
 
 0.934
Your Current Organism:
Acidimicrobium ferrooxidans
NCBI taxonomy Id: 525909
Other names: A. ferrooxidans DSM 10331, Acidimicrobium ferrooxidans DSM 10331, Acidimicrobium ferrooxidans ICP, Acidimicrobium ferrooxidans str. DSM 10331, Acidimicrobium ferrooxidans strain DSM 10331
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