| Standard Name | TMT1 1 |
|---|---|
| Systematic Name | YER175C |
| Alias | TAM1 2 |
| Feature Type | ORF, Verified |
| Description | 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 (1, 3) |
| Name Description | Trans-aconitate MethylTransferase 1 |
| Chromosomal Location | |
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| Note: this feature is encoded on the Crick strand. | |
Gene Ontology Annotations All TMT1 GO evidence and references
| View Computational GO annotations for TMT1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated |
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| Cellular Component | |
| Manually curated |
Mutant phenotypes All TMT1 Phenotype evidence and references
| Large-scale survey | |
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| null |
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| Resources |
interactions All TMT1 Interaction evidence and references
| 25 total interaction(s) for 24 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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Expression Summary
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| Resources |
Protein Information All TMT1 Protein evidence and references
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
sequence information
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
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| Retrieve sequences | |||||||||||||
Analyze Sequence
| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
Resources
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000000977 |
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References cited on this page View Complete Literature Guide for TMT1
| 1) | Cai H, et al. (2001) Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae. Biochemistry 40(45):13699-709 |
| 2) | Cai H, et al. (2001) Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferases. Biochemistry 40(7):2210-9 |
| 3) | Katz JE, et al. (2004) 3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase. Biochemistry 43(20):5976-86 |




