ID   CNMT_THLFG              Reviewed;         361 AA.
AC   Q5C9L6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=(S)-coclaurine N-methyltransferase;
DE            Short=TfCNMT;
DE            EC=2.1.1.140;
OS   Thalictrum flavum subsp. glaucum (Yellow meadow rue).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Thalictrum.
OX   NCBI_TaxID=150095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15722473; DOI=10.1105/tpc.104.028654;
RA   Samanani N., Park S.U., Facchini P.J.;
RT   "Cell type-specific localization of transcripts encoding nine consecutive
RT   enzymes involved in protoberberine alkaloid biosynthesis.";
RL   Plant Cell 17:915-926(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
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: Involved in the biosynthesis of protoberberine alkaloids. N-
CC       methyltransferase with a substrate preference for (R,S)-norreticuline
CC       but also active with dimethoxytetrahydroisoquinoline.
CC       {ECO:0000269|PubMed:19624470}.
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:19624470};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=41 uM for (R,S)-norreticuline {ECO:0000269|PubMed:19624470};
CC         KM=43 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:19624470};
CC         Vmax=1.1 pmol/sec/mg enzyme toward (R,S)-norreticuline
CC         {ECO:0000269|PubMed:19624470};
CC         Vmax=1.1 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   -!- TISSUE SPECIFICITY: Highly expressed in rhizomes. Detected in roots,
CC       petioles, flower buds and leaves. Expressed between the developing
CC       stele and ground tissues near the root apical meristem, in the immature
CC       endodermis, the pericycle and the spokes of developing xylem in the
CC       apical region of the root and in the protoderm of leaf primordia in
CC       rhizomes. {ECO:0000269|PubMed:15722473}.
CC   -!- INDUCTION: Not induced by elicitor treatment.
CC       {ECO:0000269|PubMed:19624470}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR   EMBL; AY610508; AAU20766.1; -; mRNA.
DR   AlphaFoldDB; Q5C9L6; -.
DR   SMR; Q5C9L6; -.
DR   KEGG; ag:AAU20766; -.
DR   SABIO-RK; Q5C9L6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030794; F:(S)-coclaurine-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..361
FT                   /note="(S)-coclaurine N-methyltransferase"
FT                   /id="PRO_0000411113"
FT   ACT_SITE        336
FT                   /evidence="ECO:0000250"
FT   BINDING         100..101
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         162..167
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  41903 MW;  C4A66879F11EBDFB CRC64;
     MAVEGKQVAP KKAIIVELLK KLELGLVPDD EIKKLIRIQL GRRLQWGCKS TYEEQIAQLV
     NLTHSLRQMK IATEVETLDD QMYEVPIDFL KIMNGSNLKG SCCYFKNDST TLDEAEIAML
     ELYCERAQIK DGHSVLDLGC GQGALTLYVA QKYKNSRVTA VTNSVSQKEF IEEESRKRNL
     SNVEVLLADI TTHKMPDTYD RILVVELFEH MKNYELLLRK IKEWMAKDGL LFVEHICHKT
     FAYHYEPIDE DDWFTEYVFP AGTMIIPSAS FFLYFQDDVS VVNHWTLSGK HFSRTNEEWL
     KRLDANVELI KPMFVTITGQ CRQEAMKLIN YWRGFCLSGM EMFGYNNGEE WMASHVLFKK
     K