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
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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
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
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
mqnAMenaquinone biosynthesis protein; Catalyzes the dehydration of chorismate into 3-[(1- carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2). (282 aa)    
Predicted Functional Partners:
mqnC
Dehypoxanthine futalosine cyclase; Radical SAM enzyme that catalyzes the cyclization of dehypoxanthine futalosine (DHFL) into cyclic dehypoxanthine futalosine (CDHFL), a step in the biosynthesis of menaquinone (MK, vitamin K2).
 
  
 0.989
mqnE
Aminofutalosine synthase MqnE; Radical SAM enzyme that catalyzes the addition of the adenosyl radical to the double bond of 3-[(1-carboxyvinyl)oxy]benzoate, leading to aminodeoxyfutalosine (AFL), a key intermediate in the formation of menaquinone (MK, vitamin K2) from chorismate.
 
  
 0.982
mqnD
1,4-dihydroxy-6-naphthoate synthase; Catalyzes the conversion of cyclic dehypoxanthine futalosine (cyclic DHFL) into 1,4-dihydroxy-6-naphthoate, a step in the biosynthesis of menaquinone (MK, vitamin K2); Belongs to the MqnA/MqnD family. MqnD subfamily.
 
  
 0.980
mqnB
Futalosine hydrolase; Catalyzes the hydrolysis of futalosine (FL) to dehypoxanthine futalosine (DHFL) and hypoxanthine, a step in the biosynthesis of menaquinone (MK, vitamin K2).
  
  
 0.967
KUN47153.1
Chorismate mutase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
  0.891
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
    
  0.863
KUN47803.1
Chorismate mutase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.862
KUN49037.1
Aminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.850
hisC
Aspartate aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
     
  0.850
trpE
Anthranilate synthase; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
     
  0.850
Your Current Organism:
Streptomyces olivochromogenes
NCBI taxonomy Id: 1963
Other names: ATCC 25479, ATCC 3336, Actinomyces olivochromogenus, CBS 889.69, DSM 40451, IFO 13067, IFO 3178, IMET 40352, ISP 5451, JCM 4163, JCM 4500, KCTC 9064, NBRC 13067, NBRC 3178, NRRL-ISP 5451, S. olivochromogenes, Streptomyces olivichromogenes, Streptomyces olivochromogenus
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