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    TMT1 trans-aconitate 3-methyltransferase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856922, updated on 9-Dec-2024

    Summary

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    Official Symbol
    TMT1
    Official Full Name
    trans-aconitate 3-methyltransferase
    Primary source
    SGD:S000000977
    Locus tag
    YER175C
    See related
    AllianceGenome:SGD:S000000977; FungiDB:YER175C; VEuPathDB:YER175C
    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
    TAM1
    Summary
    Enables trans-aconitate 3-methyltransferase activity. Involved in cellular response to amino acid starvation. Is active in cytosol. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See TMT1 in Genome Data Viewer
    Location:
    chromosome: V
    Exon count:
    1
    Sequence:
    Chromosome: V; NC_001137.3 (539464..540363, complement)

    Chromosome V - NC_001137.3Genomic Context describing neighboring genes Neighboring gene Rad24p Neighboring gene monothiol glutaredoxin GRX4 Neighboring gene uncharacterized protein Neighboring gene RNA helicase

    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. 3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase. Katz JE, et al. Biochemistry, 2004 May 25. PMID 15147181
    2. Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae. Cai H, et al. Biochemistry, 2001 Nov 13. PMID 11695919
    3. Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferases. Cai H, et al. Biochemistry, 2001 Feb 20. PMID 11329290
    4. Secreted 3-isopropylmalate methyl ester signals invasive growth during amino acid starvation in Saccharomyces cerevisiae. Dumlao DS, et al. Biochemistry, 2008 Jan 15. PMID 18092814
    5. Histone Acetylation, Not Stoichiometry, Regulates Linker Histone Binding in Saccharomyces cerevisiae. Lawrence MBD, et al. Genetics, 2017 Sep. PMID 28739661, Free PMC Article

    See all (19) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 methyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables trans-aconitate 3-methyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables trans-aconitate 3-methyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cellular response to amino acid starvation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in methylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    trans-aconitate 3-methyltransferase
    NP_011102.3
    • Trans-aconitate methyltransferase; cytosolic enzyme that catalyzes the methyl esterification of 3-isopropylmalate, an intermediate of the leucine biosynthetic pathway, and trans-aconitate, which inhibits the citric acid cycle

    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
      539464..540363 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179065.3 → NP_011102.3  TPA: trans-aconitate 3-methyltransferase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011102.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      A6ZRD1, D3DM83, P32643
      UniProtKB/TrEMBL
      B5VHV6, C7GS35, C8Z7J8, G2WD61, N1P798
      Conserved Domains (1) summary
      cl17173
      Location:33 → 147
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P32643.1

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