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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: Annotation score: 5 out of 5-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

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
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-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

EuPathDBiFungiDB:YER175C.
SGDiS000000977. TMT1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 299298Trans-aconitate 3-methyltransferasePRO_0000202658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32643.

PTM databases

iPTMnetiP32643.

Expressioni

Inductioni

During amino acid starvation.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi36928. 24 interactions.
DIPiDIP-4807N.
MINTiMINT-509889.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 54Combined sources
Helixi11 – 177Combined sources
Helixi23 – 3210Combined sources
Beta strandi38 – 436Combined sources
Turni46 – 483Combined sources
Helixi49 – 579Combined sources
Beta strandi62 – 698Combined sources
Helixi71 – 8313Combined sources
Turni85 – 906Combined sources
Beta strandi91 – 955Combined sources
Helixi102 – 1043Combined sources
Turni106 – 1105Combined sources
Beta strandi114 – 1218Combined sources
Helixi123 – 1253Combined sources
Helixi128 – 13811Combined sources
Beta strandi139 – 15416Combined sources
Helixi159 – 1613Combined sources
Helixi164 – 1707Combined sources
Turni172 – 1754Combined sources
Helixi176 – 1783Combined sources
Helixi183 – 1886Combined sources
Turni189 – 1935Combined sources
Turni198 – 2003Combined sources
Beta strandi201 – 2099Combined sources
Helixi211 – 2155Combined sources
Helixi217 – 2226Combined sources
Beta strandi231 – 2344Combined sources
Helixi236 – 2438Combined sources
Helixi247 – 2548Combined sources
Helixi256 – 2583Combined sources
Helixi264 – 27512Combined sources
Beta strandi285 – 29814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G5TX-ray1.12A2-299[»]
ProteinModelPortaliP32643.
SMRiP32643. Positions 2-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32643.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00510000049434.
HOGENOMiHOG000246573.
InParanoidiP32643.
OMAiAVPEWKA.
OrthoDBiEOG092C3HWF.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3G5TX-ray1.12A2-299[»]
ProteinModelPortaliP32643.
SMRiP32643. Positions 2-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36928. 24 interactions.
DIPiDIP-4807N.
MINTiMINT-509889.

PTM databases

iPTMnetiP32643.

Proteomic databases

MaxQBiP32643.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER175C; YER175C; YER175C.
GeneIDi856922.
KEGGisce:YER175C.

Organism-specific databases

EuPathDBiFungiDB:YER175C.
SGDiS000000977. TMT1.

Phylogenomic databases

GeneTreeiENSGT00510000049434.
HOGENOMiHOG000246573.
InParanoidiP32643.
OMAiAVPEWKA.
OrthoDBiEOG092C3HWF.

Enzyme and pathway databases

BioCyciYEAST:YER175C-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32643.
PROiP32643.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTMT1_YEAST
AccessioniPrimary (citable) accession number: P32643
Secondary accession number(s): D3DM83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 7, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.