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BNA4 protein (Coprinopsis cinerea) - STRING interaction network
"BNA4" - Kynurenine 3-monooxygenase in Coprinopsis cinerea
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Known Interactions
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Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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BNA4Kynurenine 3-monooxygenase; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid (458 aa)    
Predicted Functional Partners:
BNA5
Kynureninase; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively; Belongs to the kynureninase family (444 aa)
 
  0.998
CC1G_00425
Aminotransferase (382 aa)
     
 
  0.985
BNA1
3-hydroxyanthranilate 3,4-dioxygenase; Catalyzes the oxidative ring opening of 3- hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate (191 aa)
   
   
  0.967
CC1G_00160
Nicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA); Belongs to the NadC/ModD family (298 aa)
     
   
  0.811
CC1G_11927
Uncharacterized protein (292 aa)
           
  0.633
CC1G_12439
Oxoglutarate dehydrogenase (1005 aa)
     
   
  0.618
CC1G_09352
Nicotinamide-nucleotide adenylyltransferase; Nicotinamide mononucleotide adenylyl transferase; Belongs to the eukaryotic NMN adenylyltransferase family (305 aa)
           
  0.595
CC1G_13978
Dol-P-Man-Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase; Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol (414 aa)
           
  0.590
CC1G_09831
Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (313 aa)
           
  0.573
CC1G_04273
Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val) (258 aa)
     
        0.545
Your Current Organism:
Coprinopsis cinerea
NCBI taxonomy Id: 5346
Other names: C. cinerea, Coprinopsis cinerea, Coprinus cinereus, Coprinus macrorhizus
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