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    HOM3 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856778, updated on 11-Sep-2024

    Summary

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    Official Symbol
    HOM3
    Primary source
    SGD:S000000854
    Locus tag
    YER052C
    See related
    AllianceGenome:SGD:S000000854; FungiDB:YER052C; VEuPathDB:YER052C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    BOR1; SIL4; THR3
    Summary
    Enables aspartate kinase activity. Involved in homoserine biosynthetic process; methionine biosynthetic process; and threonine biosynthetic process. Located in cytoplasm. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    Location:
    chromosome: V
    Exon count:
    1
    Sequence:
    Chromosome: V; NC_001137.3 (256375..257958, complement)

    Chromosome V - NC_001137.3Genomic Context describing neighboring genes Neighboring gene mitochondrial 37S ribosomal protein RSM18 Neighboring gene [Histone H3]-lysine-36 demethylase Neighboring gene Cu/Pi carrier Neighboring gene uncharacterized protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001137.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Production of (S)-2-aminobutyric acid and (S)-2-aminobutanol in Saccharomyces cerevisiae. Weber N, et al. Microb Cell Fact, 2017 Mar 23. PMID 28335772, Free PMC Article
    2. A new mutation in the yeast aspartate kinase induces threonine accumulation in a temperature-regulated way. Velasco I, et al. Yeast, 2005 Jan 30. PMID 15645479
    3. Characterization of the aspartate kinase from Saccharomyces cerevisiae and of its interaction with threonine. Marina P, et al. Biochem Biophys Res Commun, 2004 Aug 27. PMID 15358146
    4. Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase. Bareich DC, et al. Biochem Biophys Res Commun, 2003 Nov 21. PMID 14623312
    5. Mutations that cause threonine sensitivity identify catalytic and regulatory regions of the aspartate kinase of Saccharomyces cerevisiae. Arévalo-Rodríguez M, et al. Yeast, 1999 Sep 30. PMID 10509015

    See all (76) 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 aspartate kinase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables aspartate kinase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables aspartate kinase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables aspartate kinase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables kinase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in alpha-amino acid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in amino acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in carboxylic acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in homoserine biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in homoserine biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in lysine biosynthetic process via diaminopimelate IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in lysine biosynthetic process via diaminopimelate IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in methionine biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in threonine biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in threonine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in threonine biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    aspartate kinase
    NP_010972.1
    • Aspartate kinase (L-aspartate 4-P-transferase); cytoplasmic enzyme that catalyzes the first step in the common pathway for methionine and threonine biosynthesis; subject to allosteric feedback inhibition by threonine; expression regulated by Gcn4p and the general control of amino acid synthesis

    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_001137.3 Reference assembly

      Range
      256375..257958 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178943.1 → NP_010972.1  TPA: aspartate kinase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010972.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DLV4, P10869
      UniProtKB/TrEMBL
      A6ZR03, B3LS65, C7GSK1, C8Z756, G2WCT7, N1P4U6
      Conserved Domains (3) summary
      cd04919
      Location:437 → 502
      ACT_AK-Hom3_2; ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3
      cd04934
      Location:362 → 435
      ACT_AK-Hom3_1; CT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains
      cd04247
      Location:13 → 324
      AAK_AK-Hom3; Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal catalytic domain of the aspartokinase HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae and other related AK domains. Aspartokinase, the first enzyme in the ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P10869.2

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