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

Gene ID: 856922, updated on 13-Apr-2024

Summary

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Gene symbol
TMT1
Gene description
trans-aconitate 3-methyltransferase
Primary source
SGD:S000000977
Locus tag
YER175C
See related
AllianceGenome:SGD:S000000977
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. Located in cytosol. Orthologous to human METTL27 (methyltransferase like 27). [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 (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. 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
  4. Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferases. Cai H, et al. Biochemistry, 2001 Feb 20. PMID 11329290
  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 (17) 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
    A0A8H8UM38, 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

Gene LinkOut

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