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.
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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.
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from curated databases
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
SB4_01075ATP synthase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. (360 aa)    
Predicted Functional Partners:
SB4_01065
Polyphenol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the multicopper oxidase YfiH/RL5 family.
      0.912
SB4_01070
Acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.872
lgt
Diacylglyceryl transferase; Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins; Belongs to the Lgt family.
 
     0.837
nuoI
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 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.
 
  
 0.831
adk
Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.
     
  0.813
nuoC
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 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 30 kDa subunit family.
 
 
 0.781
SB4_02800
NADH dehydrogenase; 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.
 
 
  0.763
SB4_16090
Methyltransferase type 11; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.749
SB4_17080
3-beta hydroxysteroid dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
  0.744
nuoD
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 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 49 kDa subunit family.
 
 
 0.741
Your Current Organism:
Sphingomonas sanguinis
NCBI taxonomy Id: 33051
Other names: 13937T, ATCC 51382, CIP 104197, DSM 13885, GIFU 2397, GIFU:2397, HAMBI 2010, IFO 13937, JCM 7514, LMG 17325, LMG:17325, NBRC 13937, S. sanguinis, Sphingomonas sanguis, strain 13937
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