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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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[Homology]
Score
AMF_834Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. (434 aa)    
Predicted Functional Partners:
coxB
Cytochrome c oxidase subunit II (coxB); 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).
  
 0.974
coxC
Cytochrome C oxidase, subunit III (coxC); Psort: bacterial inner membrane --- Certainty= 0.370(Affirmative); COG1845 CyoC heme/copper-type cytochrome/quinol oxidase, subunit 3.
  
 0.974
petB
Cytochrome B (petB); Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
  
 
 0.959
nuoH
NADH dehydrogenase I chain H (nuoH); 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.
   
 
 0.937
nuoA
NADH dehydrogenase I chain A (nuoA); 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; Belongs to the complex I subunit 3 family.
   
 
 0.935
nuoM
NADH dehydrogenase I chain M (nuoM); Psort: bacterial inner membrane --- Certainty= 0.711(Affirmative); COG1008 NuoM NADH:ubiquinone oxidoreductase subunit 4 (chain M).
   
 
 0.933
nuoN1
NADH dehydrogenase I, N chain (nuoN1); 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; Belongs to the complex I subunit 2 family.
   
 
 0.909
atpB
ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
   
 0.886
petC
Cytochrome c1, heme protein precursor; Psort: bacterial inner membrane --- Certainty= 0.317(Affirmative); COG2857 CYT1 cytochrome c1.
  
 
 0.839
ctaB
Cytochrome c oxidase assembly factor (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.
  
 
 0.827
Your Current Organism:
Anaplasma marginale
NCBI taxonomy Id: 320483
Other names: A. marginale str. Florida, Anaplasma marginale str. Florida, Anaplasma marginale strain Florida
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