TMT1_BRAOL
ID TMT1_BRAOL Reviewed; 226 AA.
AC Q93V78;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Thiocyanate methyltransferase 1;
DE EC=2.1.1.n4;
GN Name=TMT1;
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 [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 155-199,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CATALYTIC ACTIVITY.
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.
CC Also accepts halid ions as substrates with a lower affinity.
CC {ECO:0000269|PubMed:10933880}.
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 Evidence={ECO:0000269|PubMed:12369626};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.65 uM for thiocyanate {ECO:0000269|PubMed:12369626};
CC KM=8000 uM for iodide {ECO:0000269|PubMed:12369626};
CC KM=52 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:12369626};
CC Note=The KM values of the recombinant protein shown here are slightly
CC lower than those of the native isoform.;
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:12369626};
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12369626}.
CC -!- DEVELOPMENTAL STAGE: Higher expression in young seedlings than in
CC mature plants. {ECO:0000269|PubMed:12369626}.
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; AF387791; AAK69760.1; -; mRNA.
DR EMBL; AF387793; AAK69762.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93V78; -.
DR SMR; Q93V78; -.
DR BioCyc; MetaCyc:MON-16290; -.
DR BRENDA; 2.1.1.9; 947.
DR GO; GO:0102215; F:thiocyanate methyltransferase activity; IEA:RHEA.
DR GO; GO:0018708; F:thiol S-methyltransferase activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Direct protein sequencing; Methyltransferase; Phosphoprotein;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..226
FT /note="Thiocyanate methyltransferase 1"
FT /id="PRO_0000393280"
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; 25128 MW; E6E39E518196798C CRC64;
MAEEQQKAGH SNGENIIPPE EVAKFLPETV EEGGWEKCWE DGITPWDQGR ATPLVVHLVD
SSSLPLGRAL VPGCGGGHDV VAMASPERFV VGLDISESAL EKAAETYGSS PKAKYFTFVK
EDFFTWRPNE LFDLIFDYVV FCAIEPEMRP AWAKSMYELL KPDGELITLM YPITDHDGGP
PYKVAVSTYE DVLVPVGFKA VSIEENPYSI ATRKGKEKLG RWKKIN
