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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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colored nodes:
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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experimentally determined
co-expression
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gene neighborhood
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[Homology]
Score
AMS40724.1Hypothetical protein. (290 aa)    
Predicted Functional Partners:
AMS43341.1
Pfam:pfam04800 ETC complex I subunit conserved region.
  
     0.762
AMS41353.1
Hypothetical protein; Pfam:pfam02636 Putative S-adenosyl-L-methionine-dependent methyltransferase.
  
     0.750
AMS41858.1
NADH dehydrogenase subunit G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family.
  
   
 0.727
AMS42224.1
Pfam:pfam05071 NADH ubiquinone oxidoreductase subunit NDUFA12.
  
     0.697
AMS39627.1
Pfam:pfam01073 3-beta hydroxysteroid dehydrogenase/isomerase family.
 
     0.654
AMS40589.1
Cytochrome C.
  
  
 0.649
AMS40725.1
Amidophosphoribosyltransferase; Pfam:pfam00156 Phosphoribosyl transferase domain.
       0.645
AMS40726.1
Glutaredoxin; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
  
  
 0.620
AMS43469.1
Pfam:pfam00005 ABC transporter.
  
     0.598
nuoI
NADH-quinone oxidoreductase 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.
  
   
 0.596
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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