BNA2 protein (Saccharomyces cerevisiae) - STRING interaction network
"BNA2" - Tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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Gene Fusion
BNA2Tryptophan 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)    
Predicted Functional Partners:
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)
Formylkynurenine 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)
Aromatic aminotransferase I, expression is regulated by general control of amino acid biosynthesis; General aromatic amino acid transaminase involved in several otherwise unrelated metabolic pathways. Responsible for phenylalanine and tyrosine biosynthesis. Active with glutamate, phenylalanine, tyrosine and tryptophan as amino donors and with phenylpyruvate, hydroxyphenylpyruvate, 2-oxoglutarate and pyruvate as amino acceptors. Also active with methionine, alpha- aminoadipate and leucine as amino donors when phenylpyruvate is the amino acceptor and in the reverse reactions with the cor [...] (500 aa)
N-formyltyrosine oxidase, sporulation-specific microsomal enzyme involved in the production of N,N-bisformyl dityrosine required for spore wall maturation, homologous to cytochrome P-450s; Involved in spore wall maturation. Thought to catalyze the oxidation of tyrosine residues in the formation of LL- dityrosine a precursor of the spore wall (489 aa)
Tryptophan synthase, catalyzes the last step of tryptophan biosynthesis; regulated by the general control system of amino acid biosynthesis (707 aa)
Nicotinate phosphoribosyltransferase, acts in the salvage pathway of NAD+ biosynthesis; required for silencing at rDNA and telomeres and has a role in silencing at mating-type loci; localized to the nucleus; Essential for growth under anaerobic conditions (429 aa)
3-hydroxyanthranilic acid dioxygenase, required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p; Catalyzes the oxidative ring opening of 3- hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate (177 aa)
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)
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)
Single stranded DNA-binding protein found at TG1-3 telomere G-tails; regulates telomere replication through recruitment of specific sub-complexes, but the essential function is telomere capping; Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomera [...] (924 aa)
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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