ID   CMT_YEASX               Reviewed;         130 AA.
AC   I6WHP7;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 3.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Cysteine methyltransferase {ECO:0000303|PubMed:24412193};
DE            Short=CMT {ECO:0000303|PubMed:24412193};
DE            EC=2.1.1.318 {ECO:0000269|PubMed:24412193};
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=8534-10A x 6460-8D;
RX   PubMed=24412193; DOI=10.1016/j.bbagen.2014.01.005;
RA   Sengupta S., Banerjee S., Lahiri S., Dutta T., Dhar T.K., Ghosh A.K.;
RT   "Purification, characterization, sequencing and molecular cloning of a
RT   novel cysteine methyltransferase that regulates trehalose-6-phosphate
RT   synthase from Saccharomyces cerevisiae.";
RL   Biochim. Biophys. Acta 1840:1861-1871(2014).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-cysteine S-
CC       methyltransferase with broad substrate specificity. Methylates
CC       trehalose-6-phosphate synthase (TPS), enhancing its enzymatic activity
CC       and promoting trehalose synthesis upon entry of cells into stationary
CC       phase. {ECO:0000269|PubMed:24412193}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[trehalose-6-phosphate synthase]-L-cysteine + S-adenosyl-L-
CC         methionine = [trehalose-6-phosphate synthase]-S-methyl-L-cysteine +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46808, Rhea:RHEA-
CC         COMP:11665, Rhea:RHEA-COMP:11666, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:82612; EC=2.1.1.318;
CC         Evidence={ECO:0000269|PubMed:24412193};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.95 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:24412193};
CC         Vmax=3.2 umol/min/mg enzyme {ECO:0000269|PubMed:24412193};
CC       pH dependence:
CC         Optimum pH is 7. {ECO:0000269|PubMed:24412193};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:24412193};
CC   -!- MASS SPECTROMETRY: Mass=13680; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:24412193};
CC   -!- DISRUPTION PHENOTYPE: Exhibits almost 50% reduction in intracellular
CC       trehalose concentration. {ECO:0000269|PubMed:24412193}.
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DR   EMBL; JX072966; AFN42196.3; -; mRNA.
DR   AlphaFoldDB; I6WHP7; -.
DR   PRIDE; I6WHP7; -.
DR   KEGG; ag:AFN42196; -.
DR   BioCyc; MetaCyc:MON-19208; -.
DR   BRENDA; 2.1.1.318; 984.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..130
FT                   /note="Cysteine methyltransferase"
FT                   /id="PRO_0000434724"
SQ   SEQUENCE   130 AA;  14631 MW;  E1096A8128BDBB41 CRC64;
     MIHCKVQQWS PQYLRLPATG YEELTLTLNT SMLARMPEEE DQLFLVVGDS PSSTYVDWGE
     DCNSTRYPSY DHCTHKILYL GASAGTTRSK RLSATIGIRL SKGTGSNNVL GTPMYLLYNE
     MKTRIIESSK