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 13-SEP-2023, entry version 37.
DE RecName: Full=(S)-tetrahydroprotoberberine N-methyltransferase 1 {ECO:0000303|PubMed:19624470};
DE Short=PbTNMT1 {ECO:0000303|PubMed:19624470};
DE EC=2.1.1.- {ECO:0000269|PubMed:19624470};
GN Name=TNMT1 {ECO:0000303|PubMed:19624470};
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, INDUCTION BY ELICITOR, AND PATHWAY.
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)-stylopine + S-adenosyl-L-methionine = (S)-cis-N-
CC methylstylopine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:75975,
CC ChEBI:CHEBI:444, ChEBI:CHEBI:18285, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; Evidence={ECO:0000269|PubMed:19624470};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-tetrahydropalmatine + S-adenosyl-L-methionine = (S)-cis-N-
CC methyltetrahydropalmatine + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:76047, ChEBI:CHEBI:16563, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:194514;
CC 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 -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:19624470}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q108P1}.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43832; -; 1.
DR PANTHER; PTHR43832:SF1; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR Pfam; PF02353; CMAS; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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|UniProtKB:P9WPB7"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:C3SBW0"
FT BINDING 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:C3SBW0"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:C3SBW0"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:C3SBW0"
FT BINDING 186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:C3SBW0"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:C3SBW0"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:C3SBW0"
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
//
