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BNA7 protein (Saccharomyces cerevisiae) - STRING interaction network
"BNA7" - Formylkynurenine formamidase, involved in the de novo biosynthesis of NAD from tryptophan via kynurenine in Saccharomyces cerevisiae
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Predicted Interactions
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protein homology
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BNA7Formylkynurenine formamidase, involved in the de novo biosynthesis of NAD from tryptophan via kynurenine; Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites (261 aa)    
Predicted Functional Partners:
BNA5
Kynureninase, required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p; 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 (453 aa)
       
  0.987
BNA3
Kynurenine aminotransferase, catalyzes formation of kynurenic acid from kynurenine; potential Cdc28p substrate; Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA) (444 aa)
   
 
  0.971
BNA4
Kynurenine 3-monooxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p; putative therapeutic target for Huntington disease; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid (460 aa)
       
  0.963
BNA2
Tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase; required for de novo biosynthesis of NAD from tryptophan via kynurenine; interacts genetically with telomere capping gene CDC13; regulated by Hst1p and Aftp; Catalyzes the first step in tryptophan catabolism in order to supply de novo nicotinamide adenine dinucleotide (NAD(+)) via the kynurenine pathway. Plays a role in the cellular response to telomere uncapping (453 aa)
         
  0.956
FDH1
NAD(+)-dependent formate dehydrogenase, may protect cells from exogenous formate; Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms (PubMed-9178506, PubMed-12144528, PubMed-11921099). Has a role in the detoxification of exogenous formate in non-methylotrophic organisms (PubMed-11921099) (376 aa)
         
  0.901
MDH2
Cytoplasmic malate dehydrogenase, one of three isozymes that catalyze interconversion of malate and oxaloacetate; involved in the glyoxylate cycle and gluconeogenesis during growth on two-carbon compounds; interacts with Pck1p and Fbp1; The isoenzyme MDH2 may function primarily in the glyoxylate cycle (377 aa)
       
  0.806
MDH1
Mitochondrial malate dehydrogenase, catalyzes interconversion of malate and oxaloacetate; involved in the tricarboxylic acid (TCA) cycle; phosphorylated (334 aa)
       
  0.806
MDH3
Peroxisomal malate dehydrogenase, catalyzes interconversion of malate and oxaloacetate; involved in the glyoxylate cycle (343 aa)
       
  0.806
FUM1
Fumarase, converts fumaric acid to L-malic acid in the TCA cycle; cytosolic and mitochondrial distribution determined by the N-terminal targeting sequence, protein conformation, and status of glyoxylate shunt; phosphorylated in mitochondria (488 aa)
       
    0.802
MLS1
Malate synthase, enzyme of the glyoxylate cycle, involved in utilization of non-fermentable carbon sources; expression is subject to carbon catabolite repression; localizes in peroxisomes during growth in oleic acid medium; This isozyme is necessary for growth on acetate as sole C-source (554 aa)
         
    0.800
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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