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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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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Score
AOS61803.1Putative Zn-dependent peptidase. (460 aa)    
Predicted Functional Partners:
AOS61802.1
Putative Zn-dependent peptidase.
     0.996
AOS61804.1
Zn-finger containing NTP pyrophosphohydrolase.
  
    0.843
AOS65137.1
Rieske Fe-S protein.
   
 0.842
AOS61364.1
NADH dehydrogenase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 0.822
AOS62674.1
Putative Zn-dependent peptidase; Belongs to the peptidase M16 family.
    
0.822
atpH
ATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
   
 0.760
atpA
ATP synthase F1 subcomplex alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
   
 0.747
AOS65382.1
2-oxoglutarate dehydrogenase E1 component.
   
 0.738
AOS65450.1
Hypothetical protein.
  
     0.707
nuoI
NADH dehydrogenase subunit I; 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.
  
 
 0.696
Your Current Organism:
Actinoalloteichus hymeniacidonis
NCBI taxonomy Id: 340345
Other names: A. hymeniacidonis, Actinoalloteichus hymeniacidonis Zhang et al. 2006 emend. Nouioui et al. 2018, Actinomycetales bacterium HPA177, CGMCC 4.2500, DSM 45092, JCM 13436, strain HPA177
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