ID   TMT2_BRAOL              Reviewed;         226 AA.
AC   Q93XC4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Probable thiocyanate methyltransferase 2;
DE            EC=2.1.1.n4;
GN   Name=TMT2;
OS   Brassica oleracea (Wild cabbage).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3712;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. April Red; TISSUE=Leaf;
RX   PubMed=12369626; DOI=10.1023/a:1019865829534;
RA   Attieh J., Djiana R., Koonjul P., Etienne C., Sparace S.A., Saini H.S.;
RT   "Cloning and functional expression of two plant thiol methyltransferases: a
RT   new class of enzymes involved in the biosynthesis of sulfur volatiles.";
RL   Plant Mol. Biol. 50:511-521(2002).
RN   [2]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=10933880; DOI=10.1006/abbi.2000.1896;
RA   Attieh J., Sparace S.A., Saini H.S.;
RT   "Purification and properties of multiple isoforms of a novel thiol
RT   methyltransferase involved in the production of volatile sulfur compounds
RT   from Brassica oleracea.";
RL   Arch. Biochem. Biophys. 380:257-266(2000).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase. Probably
CC       involved in glucosinolate metabolism and defense against
CC       phytopathogens. Highly reactive to thiocyanate (NCS(-)) derived from
CC       myrosinase-mediated hydrolysis of glucosinolates upon tissue damage (By
CC       similarity). Also accepts halid ions as substrates. {ECO:0000250,
CC       ECO:0000269|PubMed:10933880, ECO:0000269|PubMed:12369626}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + thiocyanate = methyl thiocyanate +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:28014, ChEBI:CHEBI:18022,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61112; EC=2.1.1.n4;
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TPMT family. {ECO:0000255|PROSITE-ProRule:PRU00918}.
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DR   EMBL; AF387792; AAK69761.1; -; mRNA.
DR   AlphaFoldDB; Q93XC4; -.
DR   SMR; Q93XC4; -.
DR   BioCyc; MetaCyc:MON-16292; -.
DR   BRENDA; 2.1.1.9; 947.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0102215; F:thiocyanate methyltransferase activity; IEA:RHEA.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR044995; TMT/HOL.
DR   InterPro; IPR008854; TPMT.
DR   PANTHER; PTHR32183; PTHR32183; 1.
DR   Pfam; PF05724; TPMT; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51585; SAM_MT_TPMT; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Phosphoprotein; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..226
FT                   /note="Probable thiocyanate methyltransferase 2"
FT                   /id="PRO_0000393281"
FT   BINDING         35
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT   BINDING         39
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q0WP12,
FT                   ECO:0000255|PROSITE-ProRule:PRU00918"
FT   BINDING         46
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT   BINDING         73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT   BINDING         94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q0WP12,
FT                   ECO:0000255|PROSITE-ProRule:PRU00918"
FT   BINDING         122..123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT   BINDING         138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0WP12"
SQ   SEQUENCE   226 AA;  25017 MW;  03389A8ED337F018 CRC64;
     MAEVQQNSGN SNGENIIPPE DVAKFLPKTV DEGGWEKCWE DGVTPWDQGR ATPLVVHLVE
     SSSLPLGRGL VPGCGGGHDV VAMASPERYV VGLDISESAL EKAAETYGSS PKAKYFTFVK
     EDFFTWRPNE LFDLIFDYVV FCAIEPETRP AWAKAMYELL KPDGELITLM YPITDHDGGP
     PYKVAVSTYE DVLVPVGFKA VSIEENPYSI ATRKGKEKLA RWKKIN