TMT1/YER175C Summary Help

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
ChrV:540363 to 539464 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All TMT1 GO evidence and references
  View Computational GO annotations for TMT1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Resources
Large-scale survey
null
Resources
26 total interaction(s) for 25 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 1
  • Biochemical Activity: 1
  • Reconstituted Complex: 1

Genetic Interactions
  • Negative Genetic: 11
  • Positive Genetic: 9
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 299
Molecular Weight (Da) 34,768
Isoelectric Point (pI) 6.2
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrV:540363 to 539464 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..900 540363..539464 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
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
Primary SGDIDS000000977
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