ID   TNMT1_PAPBR             Reviewed;         358 AA.
AC   C3SBU5;
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=(S)-tetrahydroprotoberberine N-methyltransferase 1;
DE            Short=PbTNMT1;
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], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, 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   -!- FUNCTION: N-methyltransferase with a strict substrate specificity for
CC       (R,S)-tetrahydropalmatine or (R,S)-stylopine.
CC       {ECO:0000269|PubMed:19624470}.
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; Evidence={ECO:0000269|PubMed:19624470};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.0 uM for (R,S)-stylopine {ECO:0000269|PubMed:19624470};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Up-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; EU882994; ACO90237.1; -; mRNA.
DR   AlphaFoldDB; C3SBU5; -.
DR   SMR; C3SBU5; -.
DR   SABIO-RK; C3SBU5; -.
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   1: Evidence at protein level;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..358
FT                   /note="(S)-tetrahydroprotoberberine N-methyltransferase 1"
FT                   /id="PRO_0000411110"
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;  40885 MW;  BFEB9ADD8909C37F CRC64;
     MGSIDEVKKE SAGETLGRLL KGEIKDEELK KLIKFQFEKR LQWGYKSSHQ EQLSFNLDFI
     KSLKKMEMSG EIETMNKETY ELPSEFLEAV FGKTVKQSMC YFKHESATID EAEEAAHELY
     CERAQIKDGQ TVLDIGCGQG GLVLYIARKY KKCHVTGLTN SKAQVNYLLK QAEKLGLTNV
     DAILADVTQY ESDKTYDRLL MIEAIEHMKN LQLFMKKLST WMTEESLLFV DHVCHKTFAH
     FFEAVDEDDW YSGFIFPPGC ATILAANSLL YFQDDVSVVD HWVVNGMHMA RSVDIWRKAL
     DKNMEAAKEI LLPGLGGSHE AVNGVVTHIR TFCMGGYEQF SMNDGDEWMV AQLLFKKK