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    TRP3 bifunctional anthranilate synthase/indole-3-glycerol-phosphate synthase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853669, updated on 2-Nov-2024

    Summary

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    Official Symbol
    TRP3
    Official Full Name
    bifunctional anthranilate synthase/indole-3-glycerol-phosphate synthase
    Primary source
    SGD:S000001694
    Locus tag
    YKL211C
    See related
    AllianceGenome:SGD:S000001694; FungiDB:YKL211C; VEuPathDB:YKL211C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables indole-3-glycerol-phosphate synthase activity. Contributes to anthranilate synthase activity. Involved in tryptophan biosynthetic process. Located in cytoplasm. Part of anthranilate synthase complex. [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See TRP3 in Genome Data Viewer
    Location:
    chromosome: XI
    Exon count:
    1
    Sequence:
    Chromosome: XI; NC_001143.9 (36699..38153, complement)

    Chromosome XI - NC_001143.9Genomic Context describing neighboring genes Neighboring gene Doa1p Neighboring gene phosphatidylinositol-3-phosphatase SAC1 Neighboring gene ncRNA Neighboring gene E1 ubiquitin-activating protein UBA1

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001143.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Correlation of fitness landscapes from three orthologous TIM barrels originates from sequence and structure constraints. Chan YH, et al. Nat Commun, 2017 Mar 6. PMID 28262665, Free PMC Article
    2. Isolation of Saccharomyces cerevisiae TRP3. Paluh JL, et al. J Bacteriol, 1983 Jan. PMID 6294052, Free PMC Article
    3. The folding of the bifunctional TRP3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase. Crombie T, et al. Eur J Biochem, 1994 Dec 1. PMID 8001582
    4. An allosteric pathway explains beneficial fitness in yeast for long-range mutations in an essential TIM barrel enzyme. Chan YH, et al. Protein Sci, 2020 Sep. PMID 32643222, Free PMC Article
    5. Structure and function of the TRP3 gene of Saccharomyces cerevisiae: Analysis of 3'- and 5'-deletions in vivo and in vitro. Aebi M, et al. Curr Genet, 1984 Apr. PMID 24177736

    See all (73) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    contributes_to anthranilate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables anthranilate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to anthranilate synthase activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables indole-3-glycerol-phosphate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables indole-3-glycerol-phosphate synthase activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables indole-3-glycerol-phosphate synthase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in amino acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in aromatic amino acid family biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in glutamine metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tryptophan biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in tryptophan biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tryptophan biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tryptophan metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    part_of anthranilate synthase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in cytoplasm HDA PubMed 

    General protein information

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    Preferred Names
    bifunctional anthranilate synthase/indole-3-glycerol-phosphate synthase
    NP_012711.1
    • Indole-3-glycerol-phosphate synthase; forms bifunctional hetero-oligomeric anthranilate synthase:indole-3-glycerol phosphate synthase enzyme complex with Trp2p

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001143.9 Reference assembly

      Range
      36699..38153 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179776.1 → NP_012711.1  TPA: bifunctional anthranilate synthase/indole-3-glycerol-phosphate synthase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012711.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VWZ2, P00937
      UniProtKB/TrEMBL
      A7A078, B3LQP8, B5VLV6, C7GJ02, C8ZBW9, G2WHI3, N1P7S9
      Conserved Domains (2) summary
      COG0512
      Location:11 → 199
      PabA; Anthranilate/para-aminobenzoate synthase component II [Amino acid transport and metabolism, Coenzyme transport and metabolism]
      pfam00218
      Location:217 → 481
      IGPS; Indole-3-glycerol phosphate synthase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P00937.2

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