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    FOL3 dihydrofolate synthase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855140, updated on 9-Dec-2024

    Summary

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    Official Symbol
    FOL3
    Official Full Name
    dihydrofolate synthase
    Primary source
    SGD:S000004719
    Locus tag
    YMR113W
    See related
    AllianceGenome:SGD:S000004719; FungiDB:YMR113W; VEuPathDB:YMR113W
    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 dihydrofolate synthase activity. Involved in folic acid-containing compound biosynthetic process. Located in cytoplasm. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See FOL3 in Genome Data Viewer
    Location:
    chromosome: XIII
    Exon count:
    1
    Sequence:
    Chromosome: XIII; NC_001145.3 (494999..496282)

    Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene Euc1p Neighboring gene Med11p Neighboring gene putative peptide hydrolase Neighboring gene Mgr3p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001145.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Isolation of the Pneumocystis carinii dihydrofolate synthase gene and functional complementation in Saccharomyces cerevisiae. Hauser PM, et al. FEMS Microbiol Lett, 2006 Mar. PMID 16499613
    2. Folic acid utilisation related to sulfa drug resistance in Saccharomyces cerevisiae. Bayly AM, et al. FEMS Microbiol Lett, 2001 Nov 13. PMID 11731153
    3. Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae. Cherest H, et al. J Biol Chem, 2000 May 12. PMID 10799479
    4. A bifunctional dihydrofolate synthetase--folylpolyglutamate synthetase in Plasmodium falciparum identified by functional complementation in yeast and bacteria. Salcedo E, et al. Mol Biochem Parasitol, 2001 Feb. PMID 11223131
    5. Nutritional control of epigenetic processes in yeast and human cells. Sadhu MJ, et al. Genetics, 2013 Nov. PMID 23979574, Free PMC Article

    See all (20) 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
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables acid-amino acid ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dihydrofolate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables dihydrofolate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dihydrofolate synthase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tetrahydrofolylpolyglutamate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables tetrahydrofolylpolyglutamate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in dihydrofolate biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in folic acid-containing compound biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in folic acid-containing compound biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in folic acid-containing compound biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in one-carbon metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tetrahydrofolylpolyglutamate biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    dihydrofolate synthase
    NP_013831.1
    • Dihydrofolate synthetase, involved in folic acid biosynthesis; catalyzes conversion of dihydropteroate to dihydrofolate in folate coenzyme biosynthesis; FOL3 has a paralog, RMA1, that arose from the whole genome duplication

    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_001145.3 Reference assembly

      Range
      494999..496282
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182613.1 → NP_013831.1  TPA: dihydrofolate synthase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013831.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VZT6, Q12676
      UniProtKB/TrEMBL
      A6ZMH0, B3LM04, C7GW96, C8ZEW6, G2WKG3, N1NXC5
      Conserved Domains (1) summary
      COG0285
      Location:3 → 427
      FolC; Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q12676.1

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