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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.
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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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[Homology]
Score
KDS88459.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (314 aa)    
Predicted Functional Partners:
KDS88461.1
NADH-quinone oxidoreductase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
KDS88454.1
NADH-quinone oxidoreductase subunit N; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.998
KDS88455.1
Oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.997
KDS88456.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.996
KDS88457.1
NADH-ubiquinone oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.996
KDS88458.1
NADH:ubiquinone oxidoreductase subunit J; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.996
nuoA
NADH dehydrogenase; 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 a menaquinone. 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.
 
 0.993
nuoB
NADH-quinone oxidoreductase subunit B; 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 a menaquinone. 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.
 
 0.990
nuoB-2
NADH dehydrogenase; 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 a menaquinone. 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.
 
 0.990
nuoD
NADH-quinone oxidoreductase subunit D; 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 a menaquinone. 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 49 kDa subunit family.
 
 0.989
Your Current Organism:
Streptomyces fradiae
NCBI taxonomy Id: 1906
Other names: ATCC 10745, ATCC 19760, Actinomyces fradii, BCRC 12196, CBS 498.68, CCM 3174, CCRC 12196, CCRC:12196, CECT 3197, DSM 40063, HAMBI 965, HUT 6095, IFO 12773, IFO 3718, IMET 42051, IMI 061202, ISP 5063, JCM 4133, JCM 4579, JCM 4824 [[Streptomyces roseoflavus]], KCTC 9760, NBRC 12773, NBRC 13439 [[Streptomyces roseoflavus]], NBRC 3718, NCIMB 11005, NCIMB 8233, NRRL B-2789 [[Streptomyces roseoflavus]], NRRL-ISP 5063, PCM 2330, RIA 97, S. fradiae, Streptomyces fradiae subsp. fradiae, Streptomyces fradii, Streptomyces roseiflavus, Streptomyces roseoflavus, Streptomyces sp. NEAE-82, UNIQEM 146, VKM Ac-150, VKM Ac-151, VKM Ac-152, VKM Ac-764
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