ID   TNMT_PAPSO              Reviewed;         358 AA.
AC   Q108P1;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=(S)-tetrahydroprotoberberine N-methyltransferase;
DE            Short=PsTNMT;
DE            EC=2.1.1.122;
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, INDUCTION BY FUNGAL
RP   ELICITOR, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBUNIT.
RC   STRAIN=cv. Marianne;
RX   PubMed=17389594; DOI=10.1074/jbc.m611908200;
RA   Liscombe D.K., Facchini P.J.;
RT   "Molecular cloning and characterization of tetrahydroprotoberberine cis-N-
RT   methyltransferase, an enzyme involved in alkaloid biosynthesis in opium
RT   poppy.";
RL   J. Biol. Chem. 282:14741-14751(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of protopine and
CC       benzophenanthridine alkaloids. Catalyzes the conversion of the
CC       protoberberine alkaloids stylopine, canadine, and tetrahydropalmatine
CC       to their corresponding N-methylated derivatives. No activity with
CC       dimethoxytetrahydroisoquinoline, methylisoquinolinediol,
CC       norlaudanosoline, (R,S)-tetrahydroxyberbine, (S)-scoulerine or (R,S)-
CC       pavine as substrates. {ECO:0000269|PubMed:17389594}.
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:17389594};
CC   -!- ACTIVITY REGULATION: Inhibited by nickel, cobalt, calcium and
CC       magnesium. {ECO:0000269|PubMed:17389594}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.6 uM for (R,S)-stylopine {ECO:0000269|PubMed:17389594};
CC         KM=11.5 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:17389594};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:17389594};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:17389594};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17389594}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flower buds.
CC       {ECO:0000269|PubMed:17389594}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed 1 day after seed imbibition but
CC       detected 4 days after imbibition and remains constant during seedling
CC       growth. {ECO:0000269|PubMed:17389594}.
CC   -!- INDUCTION: Up-regulated by fungal elicitor.
CC       {ECO:0000269|PubMed:17389594}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ028579; AAY79177.1; -; mRNA.
DR   AlphaFoldDB; Q108P1; -.
DR   SMR; Q108P1; -.
DR   KEGG; ag:AAY79177; -.
DR   BRENDA; 2.1.1.122; 4515.
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"
FT                   /id="PRO_0000411109"
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;  40844 MW;  233E1D0E2BDA5EA8 CRC64;
     MGSIDEVKKE SAGETLGRLL KGEIKDEELK KLIKFQFEKR LQWGYKSSHQ EQLSFNLDFI
     KSLKKMEMSG EIETMNKETY ELPSEFLEAV FGKTVKQSMC YFTHESATID EAEEAAHELY
     CERAQIKDGQ TVLDIGCGQG GLVLYIAQKY KNCHVTGLTN SKAQVNYLLK QAEKLGLTNV
     DAILADVTQY ESDKTYDRLL MIEAIEHMKN LQLFMKKLST WMTKESLLFV DHVCHKTFAH
     FFEAVDEDDW YSGFIFPPGC ATILAANSLL YFQDDVSVVD HWVVNGMHMA RSVDIWRKAL
     DKNMEAAKEI LLPGLGGSHE TVNGVVTHIR TFCMGGYEQF SMNNGDEWMV AQLLFKKK