ID   TNMT2_PAPBR             Reviewed;         358 AA.
AC   C3SBU4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Probable (S)-tetrahydroprotoberberine N-methyltransferase 2;
DE            Short=PbTNMT2;
DE            EC=2.1.1.122;
OS   Papaver bracteatum (Great scarlet poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=215227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY ELICITOR.
RX   PubMed=19624470; DOI=10.1111/j.1365-313x.2009.03980.x;
RG   Natural Products Genomics Resource (NAPGEN);
RA   Liscombe D.K., Ziegler J., Schmidt J., Ammer C., Facchini P.J.;
RT   "Targeted metabolite and transcript profiling for elucidating enzyme
RT   function: isolation of novel N-methyltransferases from three
RT   benzylisoquinoline alkaloid-producing species.";
RL   Plant J. 60:729-743(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-canadine + S-adenosyl-L-methionine = (S)-N-methylcanadine
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12805, ChEBI:CHEBI:16512,
CC         ChEBI:CHEBI:16592, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC         EC=2.1.1.122;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Down-regulated by elicitor treatment.
CC       {ECO:0000269|PubMed:19624470}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR   EMBL; EU882993; ACO90236.1; -; mRNA.
DR   AlphaFoldDB; C3SBU4; -.
DR   SMR; C3SBU4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030782; F:(S)-tetrahydroprotoberberine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..358
FT                   /note="Probable (S)-tetrahydroprotoberberine N-
FT                   methyltransferase 2"
FT                   /id="PRO_0000411111"
FT   ACT_SITE        333
FT                   /evidence="ECO:0000250"
FT   BINDING         97..98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         132..140
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..164
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  40843 MW;  6EC5DD8453E13F45 CRC64;
     MGSIEEVKKE SAEETLGRLL RGEINDEELK KLIKYQLEKR LQWGYKSSHQ EQLSFNLDFI
     NSLKKMGMSG QVEAFTNEVY ELPTECFEAA YGKSMKLSGC YFKHESSTID EAEEASHELY
     CERAQIKDGQ TVLDIGCGQG GLVLYVAQKY KNCHVTGLTN SKEQVNYILK QAEKLGLRNV
     DVILADVTQY ESDKTYDRIL VIGVVEHMKN MQLFIKKLST WMAEDSLLFV DHSCHKTFNH
     FFEALDEDDW YSGYIFPPGC ATFLSADSLL YFQDDVSVVD HWVVNGMHFA RTVDAWRKKL
     DKNMEAVKEI LLPGLGGNHE AVNGVITHIR TCCVGGYVQF SLNDGDEWMN AQLLFKKK