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Protein

Trans-aconitate 3-methyltransferase

Gene

TMT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation.3 Publications

Miscellaneous

Present with 937 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate.

Kineticsi

  1. KM=660 µM for trans-aconitate2 Publications
  2. KM=74000 µM for cis-aconitate2 Publications
  3. KM=44000 µM for itaconate2 Publications
  4. KM=323 µM for isopropylmaleate2 Publications
  5. KM=1670 µM for isopropylfumarate2 Publications
  6. KM=127 µM for (2R,3S)-3-isopropylmalate2 Publications
  7. KM=341 µM for (2S,3R)-3-isopropylmalate2 Publications
  8. KM=428 µM for (2R,3R)/(2S,3S)-3-isopropylmalate2 Publications
  9. KM=19 µM for 2-(1-methylethylidine)succinate2 Publications
  10. KM=45 µM for 3-butylmalate2 Publications
  1. Vmax=44.8 nmol/min/mg enzyme with trans-aconitate as substrate2 Publications
  2. Vmax=12.1 nmol/min/mg enzyme with cis-aconitate as substrate2 Publications
  3. Vmax=26.9 nmol/min/mg enzyme with itaconate as substrate2 Publications
  4. Vmax=39.7 nmol/min/mg enzyme with isopropylmaleate as substrate2 Publications
  5. Vmax=2.4 nmol/min/mg enzyme with isopropylfumarate as substrate2 Publications
  6. Vmax=59.2 nmol/min/mg enzyme with (2R,3S)-3-isopropylmalate as substrate2 Publications
  7. Vmax=77.8 nmol/min/mg enzyme with (2S,3R)-3-isopropylmalate as substrate2 Publications
  8. Vmax=4.4 nmol/min/mg enzyme with (2R,3R)/(2S,3S)-3-isopropylmalate as substrate2 Publications
  9. Vmax=36.2 nmol/min/mg enzyme with 2-(1-methylethylidine)succinate as substrate2 Publications
  10. Vmax=40.4 nmol/min/mg enzyme with 3-butylmalate as substrate2 Publications

GO - Molecular functioni

  • trans-aconitate 3-methyltransferase activity Source: SGD

Keywordsi

Molecular functionMethyltransferase, Transferase
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:YER175C-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Trans-aconitate 3-methyltransferase (EC:2.1.1.145)
Gene namesi
Name:TMT1
Synonyms:TAM1
Ordered Locus Names:YER175C
ORF Names:SYGP-ORF63
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

SGDiS000000977 TMT1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002026582 – 299Trans-aconitate 3-methyltransferaseAdd BLAST298

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32643
PaxDbiP32643
PRIDEiP32643

PTM databases

iPTMnetiP32643

Expressioni

Inductioni

During amino acid starvation.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi36928, 50 interactors
DIPiDIP-4807N
STRINGi4932.YER175C

Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP32643
SMRiP32643
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32643

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00510000049434
HOGENOMiHOG000246573
InParanoidiP32643
KOiK22438
OMAiMITAVEC
OrthoDBiEOG092C3HWF

Family and domain databases

InterProiView protein in InterPro
IPR025714 Methyltranfer_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF13847 Methyltransf_31, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32643-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTFSASDFN SERYSSSRPS YPSDFYKMID EYHDGERKLL VDVGCGPGTA
60 70 80 90 100
TLQMAQELKP FEQIIGSDLS ATMIKTAEVI KEGSPDTYKN VSFKISSSDD
110 120 130 140 150
FKFLGADSVD KQKIDMITAV ECAHWFDFEK FQRSAYANLR KDGTIAIWGY
160 170 180 190 200
ADPIFPDYPE FDDLMIEVPY GKQGLGPYWE QPGRSRLRNM LKDSHLDPEL
210 220 230 240 250
FHDIQVSYFC AEDVRDKVKL HQHTKKPLLI RKQVTLVEFA DYVRTWSAYH
260 270 280 290
QWKQDPKNKD KEDVADWFIK ESLRRRPELS TNTKIEVVWN TFYKLGKRV
Length:299
Mass (Da):34,768
Last modified:October 1, 1993 - v1
Checksum:i50647D67F9A61629
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18922 Genomic DNA Translation: AAB64702.1
BK006939 Genomic DNA Translation: DAA07837.1
PIRiS30861
RefSeqiNP_011102.3, NM_001179065.3

Genome annotation databases

EnsemblFungiiYER175C; YER175C; YER175C
GeneIDi856922
KEGGisce:YER175C

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18922 Genomic DNA Translation: AAB64702.1
BK006939 Genomic DNA Translation: DAA07837.1
PIRiS30861
RefSeqiNP_011102.3, NM_001179065.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3G5TX-ray1.12A2-299[»]
ProteinModelPortaliP32643
SMRiP32643
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36928, 50 interactors
DIPiDIP-4807N
STRINGi4932.YER175C

PTM databases

iPTMnetiP32643

Proteomic databases

MaxQBiP32643
PaxDbiP32643
PRIDEiP32643

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER175C; YER175C; YER175C
GeneIDi856922
KEGGisce:YER175C

Organism-specific databases

SGDiS000000977 TMT1

Phylogenomic databases

GeneTreeiENSGT00510000049434
HOGENOMiHOG000246573
InParanoidiP32643
KOiK22438
OMAiMITAVEC
OrthoDBiEOG092C3HWF

Enzyme and pathway databases

BioCyciYEAST:YER175C-MONOMER

Miscellaneous databases

EvolutionaryTraceiP32643
PROiPR:P32643

Family and domain databases

InterProiView protein in InterPro
IPR025714 Methyltranfer_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF13847 Methyltransf_31, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTMT1_YEAST
AccessioniPrimary (citable) accession number: P32643
Secondary accession number(s): D3DM83
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 7, 2018
This is version 136 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
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Main funding by: National Institutes of Health

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