NOMT2_NARAP
ID NOMT2_NARAP Reviewed; 239 AA.
AC A0A077EW86;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Norbelladine 4'-O-methyltransferase 2 {ECO:0000303|PubMed:25061748};
DE Short=NpN4OMT2 {ECO:0000303|PubMed:25061748};
DE EC=2.1.1.336 {ECO:0000250|UniProtKB:A0A077EWA5};
GN Name=N4OMT2 {ECO:0000303|PubMed:25061748};
OS Narcissus aff. pseudonarcissus MK-2014 (Daffodil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Amaryllidoideae; Narcissus.
OX NCBI_TaxID=1540222;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Carlton; TISSUE=Bulb;
RX PubMed=25061748; DOI=10.1371/journal.pone.0103223;
RA Kilgore M.B., Augustin M.M., Starks C.M., O'Neil-Johnson M., May G.D.,
RA Crow J.A., Kutchan T.M.;
RT "Cloning and characterization of a norbelladine 4'-O-methyltransferase
RT involved in the biosynthesis of the Alzheimer's drug galanthamine in
RT Narcissus sp. aff. pseudonarcissus.";
RL PLoS ONE 9:E103223-E103223(2014).
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 (By similarity).
CC {ECO:0000250|UniProtKB:A0A077EWA5, ECO:0000250|UniProtKB:A0A2H5AIZ6}.
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:0000250|UniProtKB:A0A077EWA5}.
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; KJ584562; AIL54542.1; -; mRNA.
DR AlphaFoldDB; A0A077EW86; -.
DR SMR; A0A077EW86; -.
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 2"
FT /id="PRO_0000450642"
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; 27093 MW; 7BDF63BBDA18B658 CRC64;
MGASIDDYSL VHKNILHSED LLKYILETSA YPREHEQLKG LREVTEKHEW SSALVPADEG
LFLSMLLKLM NAKRTIEIGV YTGYSLLTTA LALPEDGKIT AIDVNKSFFE IGLPFIQKAG
VEHKINFIES EALPVLDQML QETKEEDLYD YAFVDADKSN YANYHERLVK LVRIGGAILY
DNTLWYGSVA YPEYPGLHPE EEVARLSFRN LNTFLAADPR VEISQVSIGD GVTICRRLY