ID   CNMT_PAPSO              Reviewed;         351 AA.
AC   Q7XB08;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=(S)-coclaurine N-methyltransferase {ECO:0000303|PubMed:12946416};
DE            Short=PsCNMT {ECO:0000303|PubMed:12946416};
DE            EC=2.1.1.140 {ECO:0000269|PubMed:22725256};
GN   Name=CNMT {ECO:0000303|PubMed:12946416};
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469 {ECO:0000312|EMBL:AAP45316.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INDUCTION BY ELICITOR AND WOUNDING.
RC   STRAIN=cv. Marianne;
RX   PubMed=12946416; DOI=10.1016/s0031-9422(03)00292-9;
RA   Facchini P.J., Park S.U.;
RT   "Developmental and inducible accumulation of gene transcripts involved in
RT   alkaloid biosynthesis in opium poppy.";
RL   Phytochemistry 64:177-186(2003).
RN   [2]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16813579; DOI=10.1111/j.1365-313x.2006.02801.x;
RA   Samanani N., Alcantara J., Bourgault R., Zulak K.G., Facchini P.J.;
RT   "The role of phloem sieve elements and laticifers in the biosynthesis and
RT   accumulation of alkaloids in opium poppy.";
RL   Plant J. 47:547-563(2006).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22725256; DOI=10.1111/j.1365-313x.2012.05084.x;
RA   Desgagne-Penix I., Facchini P.J.;
RT   "Systematic silencing of benzylisoquinoline alkaloid biosynthetic genes
RT   reveals the major route to papaverine in opium poppy.";
RL   Plant J. 72:331-344(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of benzylisoquinoline alkaloids.
CC       N-methyltransferase methylating (S)-coclaurine. 4'-O-methylcoclaurine
CC       and norlaudanine can also be used as substrates.
CC       {ECO:0000269|PubMed:22725256}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-coclaurine + S-adenosyl-L-methionine = (S)-N-
CC         methylcoclaurine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:17409, ChEBI:CHEBI:15378, ChEBI:CHEBI:57581,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:57993, ChEBI:CHEBI:59789;
CC         EC=2.1.1.140; Evidence={ECO:0000269|PubMed:22725256};
CC   -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-
CC       reticuline from (S)-norcoclaurine: step 2/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16813579}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, flower buds and at lower
CC       levels, in leaves (PubMed:12946416, PubMed:16813579). Restricted to
CC       sieve elements of the phloem adjacent or proximal to laticifers
CC       (PubMed:16813579). {ECO:0000269|PubMed:12946416,
CC       ECO:0000269|PubMed:16813579}.
CC   -!- DEVELOPMENTAL STAGE: Transiently induced from 4 to 7 days after seed
CC       imbibition. {ECO:0000269|PubMed:12946416, ECO:0000269|PubMed:16813579}.
CC   -!- INDUCTION: Up-regulated upon fungal elicitor treatment or wounding.
CC       {ECO:0000269|PubMed:12946416}.
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; AY217336; AAP45316.1; -; mRNA.
DR   AlphaFoldDB; Q7XB08; -.
DR   SMR; Q7XB08; -.
DR   BRENDA; 2.1.1.140; 4515.
DR   UniPathway; UPA00306; UER00442.
DR   PRO; PR:Q7XB08; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030794; F:(S)-coclaurine-N-methyltransferase activity; IMP:UniProtKB.
DR   GO; GO:1901012; P:(S)-reticuline biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IDA:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
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   Alkaloid metabolism; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..351
FT                   /note="(S)-coclaurine N-methyltransferase"
FT                   /id="PRO_0000433981"
FT   ACT_SITE        326
FT                   /evidence="ECO:0000305"
FT   BINDING         91..92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT   BINDING         126..134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT   BINDING         130..132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT   BINDING         153..158
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
SQ   SEQUENCE   351 AA;  41032 MW;  211CFC34A16AC546 CRC64;
     MQLKAKEELL RNMELGLIPD QEIRQLIRVE LEKRLQWGYK ETHEEQLSQL LDLVHSLKGM
     KMATEMENLD LKLYEAPMEF LKIQHGSNMK QSAGYYTDES TTLDEAEIAM LDLYMERAQI
     KDGQSVLDLG CGLGAVALFG ANKFKKCQFT GVTSSVEQKD YIEGKCKELK LTNVKVLLAD
     ITTYETEERF DRIFAVELIE HMKNYQLLLK KISEWMKDDG LLFVEHVCHK TLAYHYEPVD
     AEDWYTNYIF PAGTLTLSSA SMLLYFQDDV SVVNQWTLSG KHYSRSHEEW LKNMDKNIVE
     FKEIMRSITK TEKEAIKLLN FWRIFCMCGA ELFGYKNGEE WMLTHLLFKK K