ID   NOMT_NARPS              Reviewed;         239 AA.
AC   A0A2H5AIZ6;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Norbelladine 4'-O-methyltransferase {ECO:0000303|PubMed:29229969};
DE            EC=2.1.1.336 {ECO:0000250|UniProtKB:A0A077EWA5};
GN   Name=N4OMT {ECO:0000303|PubMed:29229969};
OS   Narcissus pseudonarcissus (Daffodil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Amaryllidoideae; Narcissus.
OX   NCBI_TaxID=39639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, REVIEW ON THE AMARYLLIDACEAE ALKALOID
RP   METABOLISM, PATHWAY, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. King Alfred; TISSUE=Bulb;
RX   PubMed=29229969; DOI=10.1038/s41598-017-17724-0;
RA   Singh A., Desgagne-Penix I.;
RT   "Transcriptome and metabolome profiling of Narcissus pseudonarcissus 'King
RT   Alfred' reveal components of Amaryllidaceae alkaloid metabolism.";
RL   Sci. Rep. 7:17356-17356(2017).
CC   -!- FUNCTION: 4'-O-methyltransferase converting norbelladine to 4'-O-
CC       methylnorbelladine (By similarity). 4'-O-methylnorbelladine is a
CC       precursor to all Amaryllidaceae alkaloids such as galanthamine,
CC       lycorine and haemanthamine, and including haemanthamine- and crinamine-
CC       type alkaloids, promising anticancer agents (PubMed:29229969).
CC       {ECO:0000250|UniProtKB:A0A077EWA5, ECO:0000303|PubMed:29229969}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=norbelladine + S-adenosyl-L-methionine = 4'-O-
CC         methylnorbelladine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:51268, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:133993, ChEBI:CHEBI:134001;
CC         EC=2.1.1.336; Evidence={ECO:0000250|UniProtKB:A0A077EWA5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A0A077EWA5};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000303|PubMed:29229969}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in bulbs, and, to a lower extent,
CC       in stems and roots. {ECO:0000269|PubMed:29229969}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; MF416096; AUG71941.1; -; mRNA.
DR   AlphaFoldDB; A0A2H5AIZ6; -.
DR   SMR; A0A2H5AIZ6; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009820; P:alkaloid metabolic process; 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   InterPro; IPR002935; SAM_O-MeTrfase.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   2: Evidence at transcript level;
KW   Alkaloid metabolism; Metal-binding; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..239
FT                   /note="Norbelladine 4'-O-methyltransferase"
FT                   /id="PRO_0000450641"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         79..80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         155
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         181
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         182
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ   SEQUENCE   239 AA;  27194 MW;  9E516ADDDF3CA928 CRC64;
     MGASQDDYSL VHKNILHSED LLKYILETSA YPREHEQLKG LREVTEKHEW SSALVPADEG
     LFLSMLLKLM NAKRTIEIGV YTGYSLLTTA LALPEDGKIT AIDVNKSFFE IGLPFIQKAG
     VEHKINFIES EALPVLDQML QEMKEEDLYD YAFVDADKSN YANYHERLVK LVRIGGAILY
     DNTLWYGSVA YPEYPGLYPE DEVDRLSFRN LNTFLAADPR VEISQVSIGD GVTICRRLY