ID   NMT4_PAPSO              Reviewed;         356 AA.
AC   A0A1C9U5X7;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=N-methyltransferase 4 {ECO:0000303|PubMed:27634038};
DE            EC=2.1.1.- {ECO:0000269|PubMed:27634038};
GN   Name=NMT4;
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:AOR51553.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=27634038; DOI=10.1074/jbc.m116.750893;
RA   Morris J.S., Facchini P.J.;
RT   "Isolation and characterization of reticuline N-methyltransferase involved
RT   in biosynthesis of the aporphine alkaloid magnoflorine in Opium poppy.";
RL   J. Biol. Chem. 291:23416-23427(2016).
CC   -!- FUNCTION: Probable N-methyltransferase not involved in
CC       benzylisoquinoline metabolism. Shows no detectable activity with (s)-
CC       coclaurine, (R)- or (S)-reticuline, papaverine or (R,S)-
CC       tetrahydropapaverine. {ECO:0000269|PubMed:27634038}.
CC   -!- TISSUE SPECIFICITY: Expressed in stems, roots, flower buds and leaves.
CC       {ECO:0000269|PubMed:27634038}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR   EMBL; KX369613; AOR51553.1; -; mRNA.
DR   AlphaFoldDB; A0A1C9U5X7; -.
DR   SMR; A0A1C9U5X7; -.
DR   KEGG; ag:AOR51553; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..356
FT                   /note="N-methyltransferase 4"
FT                   /id="PRO_0000439850"
FT   BINDING         93..94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT   BINDING         128..136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT   BINDING         155..160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
SQ   SEQUENCE   356 AA;  40733 MW;  03ACA1A9FB7F04AB CRC64;
     MDSKDQHGTK ILERLVKGEI GDEELKELIR IRFEKRLQCG YKPTPQDQLA SEMAFIKSLK
     DMKMSGELEA VNTELYELPT AAVAATLGST LKQSACYFKE ESMSIDEAEI AAYELDCERA
     QIKDGQTILD IGCGFGGLVL HIAQKYKNSH VTGLTNSAEQ RNYIMLQVEK LSLSNVDVIL
     ADVTKHEFEN EKKFDRILVV EAIEHMKNIQ LFLKKISNWM KDEDSFLFVV HLCHKAFSQH
     FEALDEDDWY TSYVLPEGSV TYLSASALLY FQDDVSVVDQ WLLSGTHMAR SQEEWFKRFK
     INLEAASKAL TVGLGSEEAA NQVNIQYKTF FMGYVVQFSF NNGEEWMISH YLFKKK