ID   TMT1_YEAS7              Reviewed;         299 AA.
AC   A6ZRD1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Trans-aconitate 3-methyltransferase;
DE            EC=2.1.1.145;
GN   Name=TMT1; Synonyms=TAM1; ORFNames=SCY_1678;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification
CC       of trans-aconitate and 3-isopropylmalate at high affinity and of other
CC       molecules like cis-aconitate, isocitrate, and citrate at lower
CC       velocities and affinities. The function of trans-aconitate methylation
CC       appears to be in reducing the toxicity of this spontaneous breakdown
CC       product of cis-aconitate. The role of 3-isopropylmalate methylation is
CC       unclear but may represent a metabolic branch at 3-isopropylmalate,
CC       where some of the material is taken in the pathway leading to leucine
CC       and some is taken in a pathway to the 3-isopropylmalate methyl ester, a
CC       molecule that provides a signal to switch from vegetative to invasive
CC       growth in response to amino acid starvation (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + trans-aconitate = (E)-2-
CC         (methoxycarbonylmethyl)but-2-enedioate + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:22200, ChEBI:CHEBI:15708, ChEBI:CHEBI:57469,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.145;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: During amino acid starvation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam family.
CC       {ECO:0000305}.
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DR   EMBL; AAFW02000048; EDN63151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZRD1; -.
DR   SMR; A6ZRD1; -.
DR   PRIDE; A6ZRD1; -.
DR   EnsemblFungi; EDN63151; EDN63151; SCY_1678.
DR   HOGENOM; CLU_049344_1_2_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046547; F:trans-aconitate 3-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P32643"
FT   CHAIN           2..299
FT                   /note="Trans-aconitate 3-methyltransferase"
FT                   /id="PRO_0000324944"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32643"
SQ   SEQUENCE   299 AA;  34800 MW;  50703937F9A60D32 CRC64;
     MSTFSASDFN SERYSSSRPS YPSDFYKMID EYHDGERKLL VDVGCGPGTA TLQMAQELKP
     FEQIIGSDLS ATMIKTAEVI KEGSPDTYKN VSFKISSSDD FKFLGADSVD KQKIDMITAV
     ECAHWFDFEK FQRSAYANLR KDGTIAIWGY ADPIFPDYPE FDDLMIEVPY GKQGLGPYWE
     QPGRSRLRNM LKDSHLDPEL FHDIQVSYFC AEDVRDKVKL HQHTKKPLLI RKQVTLMEFA
     DYVRTWSAYH QWKQDPKNKD KEDVADWFIK ESLRRRPELS TNTKIEVVWN TFYKLGKRV