ID   TNMT_ESCCA              Reviewed;         350 AA.
AC   C3SBS8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=(S)-tetrahydroprotoberberine N-methyltransferase;
DE            Short=EcTNMT;
DE            EC=2.1.1.122;
OS   Eschscholzia californica (California poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae;
OC   Eschscholzioideae; Eschscholzia.
OX   NCBI_TaxID=3467;
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 broad substrate range, accepting
CC       protoberberine alkaloids (R,S)-stylopine and (R,S)-tetrahydropalmatine,
CC       and to a lesser extent (R,S)-canadine and (S)-scoulerine.
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=40 uM for (R,S)-stylopine {ECO:0000269|PubMed:19624470};
CC         KM=32 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:19624470};
CC         Vmax=10.3 pmol/sec/mg enzyme toward S-adenosyl-L-methionine
CC         {ECO:0000269|PubMed:19624470};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Up-regulated 2 hours after elicitor treatment.
CC       {ECO:0000269|PubMed:19624470}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR   EMBL; EU882977; ACO90222.1; -; mRNA.
DR   AlphaFoldDB; C3SBS8; -.
DR   SMR; C3SBS8; -.
DR   SABIO-RK; C3SBS8; -.
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..350
FT                   /note="(S)-tetrahydroprotoberberine N-methyltransferase"
FT                   /id="PRO_0000411112"
FT   ACT_SITE        325
FT                   /evidence="ECO:0000250"
FT   BINDING         90..91
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         152..157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   350 AA;  40302 MW;  4BFE46CC6ABA1086 CRC64;
     MGSSAGEIMG RLMKGEIEDE ELKKLIRHQW DRRIEWGYKP THEKQLAFNL DFIKGLKEMV
     MSGEIDTMNK ETYELPTAFL EAVFGKTVKQ SCCYFKDENS TIDEAEEAAH ELYCERAQIK
     DGQTVLDIGC GQGGLVLYIA EKYKNCHVTG LTNSKAQANY IEQQAEKLEL TNVDVIFADV
     TKFDTDKTYD RILVVETIEH MKNIQLFMKK LSTWMTEDSL LFVDHISHKT FNHNFEALDE
     DDWYSGFIFP KGCVTILSSS TLLYFQDDVS ALDHWVVNGM HMARSVEAWR KKLDETIEAA
     REILEPGLGS KEAVNQVITH IRTFCIGGYE QFSYNNGEEW MITQILFKKK