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    FAS1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853653, updated on 11-Sep-2024

    Summary

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    Official Symbol
    FAS1
    Primary source
    SGD:S000001665
    Locus tag
    YKL182W
    See related
    AllianceGenome:SGD:S000001665; FungiDB:YKL182W; VEuPathDB:YKL182W
    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 3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; fatty acid synthase activity; and palmitoyltransferase activity. Contributes to fatty acid synthase activity. Involved in long-chain fatty acid biosynthetic process. Located in cytosol and lipid droplet. Part of fatty acid synthase complex. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    Location:
    chromosome: XI
    Exon count:
    1
    Sequence:
    Chromosome: XI; NC_001143.9 (100671..106826)

    Chromosome XI - NC_001143.9Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene Lot5p Neighboring gene ribose phosphate diphosphokinase subunit PRS1 Neighboring gene ribosomal 60S subunit protein L17A

    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. Biphasic modulation of fatty acid synthase by hydrogen peroxide in Saccharomyces cerevisiae. Matias AC, et al. Arch Biochem Biophys, 2011 Nov. PMID 21907179
    2. Down-regulation of fatty acid synthase increases the resistance of Saccharomyces cerevisiae cells to H2O2. Matias AC, et al. Free Radic Biol Med, 2007 Nov 15. PMID 17936191
    3. Genetic analysis of non-complementing fatty acid synthetase mutants in Saccharomyces cerevisiae. Tauro P, et al. Mol Gen Genet, 1974 Mar 14. PMID 4598796
    4. The development and application of a novel chromophoric substrate for investigation of the mechanism of yeast fatty acid synthase. Singh N, et al. Biochem Biophys Res Commun, 1985 Sep 16. PMID 3902014
    5. The pentafunctional FAS1 gene of yeast: its nucleotide sequence and order of the catalytic domains. Schweizer M, et al. Mol Gen Genet, 1986 Jun. PMID 3528750

    See all (154) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS).
      Title: Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS).
    2. This study shows that single mutations at domain-domain interfaces can severely perturb substrate shuttling in FAS1.
      Title: Analysis and engineering of substrate shuttling by the acyl carrier protein (ACP) in fatty acid synthases (FASs).
    3. Overexpression of FAS1, FAS2 and Acc1 leads to accumulation of sterols.
      Title: Overexpression of genes of the fatty acid biosynthetic pathway leads to accumulation of sterols in Saccharomyces cerevisiae.
    4. Results structurally and functionally characterized the FAS type I PPT as part of the multienzyme protein and as an isolated domain.
      Title: Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase.
    5. The crystal structure of the 2.6-MDa Saccharomyces cerevisiae fatty acid synthase (FAS) multienzyme in complex with the antibiotic cerulenin, is presented.
      Title: Inhibition of the fungal fatty acid synthase type I multienzyme complex.
    6. Fatty acid synthase (Fas) plays a key role during the cellular response of Saccharomyces cerevisiae to H2O2.
      Title: Down-regulation of fatty acid synthase increases the resistance of Saccharomyces cerevisiae cells to H2O2.
    7. Sfh2p inhibits fatty acid synthase activity in response to haem depletion
      Title: SFH2 regulates fatty acid synthase activity in the yeast Saccharomyces cerevisiae and is critical to prevent saturated fatty acid accumulation in response to haem and oleic acid depletion.
    8. Study determined crystal structure of fatty acid synthase, which illuminates how this enzyme is initially activated and then carries out multiple steps of synthesis in each of six sterically isolated reaction chambers.
      Title: The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together.
    Submit: New GeneRIF Correction

    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 (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables [acyl-carrier-protein] S-acetyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables [acyl-carrier-protein] S-acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables [acyl-carrier-protein] S-acetyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables [acyl-carrier-protein] S-malonyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables [acyl-carrier-protein] S-malonyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables [acyl-carrier-protein] S-malonyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables enoyl-[acyl-carrier-protein] reductase (NADH) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables enoyl-[acyl-carrier-protein] reductase (NADPH) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables enoyl-[acyl-carrier-protein] reductase (NADPH) activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables fatty acid synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to fatty acid synthase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables fatty acyl-[ACP] hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables fatty-acyl-CoA synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables palmitoyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables palmitoyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in fatty acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in long-chain fatty acid biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in long-chain fatty acid biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of fatty acid synthase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of fatty acid synthase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of fatty acid synthase complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in lipid droplet IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrion HDA PubMed 

    General protein information

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    Preferred Names
    tetrafunctional fatty acid synthase subunit FAS1
    NP_012739.1
    • Beta subunit of fatty acid synthetase; complex catalyzes the synthesis of long-chain saturated fatty acids; contains acetyltransacylase, dehydratase, enoyl reductase, malonyl transacylase, and palmitoyl transacylase activities; specific target of the broad-spectrum antifungal NPD6433

    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
      100671..106826
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179748.1 → NP_012739.1  TPA: tetrafunctional fatty acid synthase subunit FAS1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012739.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VX19, P07149, Q05747
      UniProtKB/TrEMBL
      A6ZZE4, C7GJ28, N1P0M8
      Conserved Domains (5) summary
      COG0331
      Location:159 → 536
      FabD; Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]
      COG4981
      Location:559 → 1350
      COG4981; Enoyl reductase domain of yeast-type FAS1 [Lipid transport and metabolism]
      cd03447
      Location:1536 → 1660
      FAS_MaoC; the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).
      pfam00698
      Location:1663 → 2037
      Acyl_transf_1; Acyl transferase domain
      pfam17828
      Location:5 → 131
      FAS_N; N-terminal domain in fatty acid synthase subunit beta
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P07149.2

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