ID   4OMT_COPJA              Reviewed;         350 AA.
AC   Q9LEL5;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   RecName: Full=3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase;
DE            EC=2.1.1.116;
DE   AltName: Full=S-adenosyl-L-methionine:3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase;
DE            Short=4'-OMT;
OS   Coptis japonica (Japanese goldthread).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Coptidoideae;
OC   Coptis.
OX   NCBI_TaxID=3442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   PubMed=10811648; DOI=10.1074/jbc.m002439200;
RA   Morishige T., Tsujita T., Yamada Y., Sato F.;
RT   "Molecular characterization of the S-adenosyl-L-methionine: 3'-hydroxy-N-
RT   methylcoclaurine 4'O-methyltransferase involved in isoquinoline alkaloid
RT   biosynthesis in Coptis japonica.";
RL   J. Biol. Chem. 275:23398-23405(2000).
CC   -!- FUNCTION: Catalyzes the transfer of the methyl group to the 4'-hydroxyl
CC       group of 3'-hydroxy-N-methylcoclaurine to form reticuline.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-3'-hydroxy-N-methylcoclaurine + S-adenosyl-L-methionine =
CC         (S)-reticuline + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:57873, ChEBI:CHEBI:58010, ChEBI:CHEBI:59789;
CC         EC=2.1.1.116;
CC   -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-
CC       reticuline from (S)-norcoclaurine: step 4/4.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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; D29812; BAB08005.1; -; mRNA.
DR   AlphaFoldDB; Q9LEL5; -.
DR   SMR; Q9LEL5; -.
DR   KEGG; ag:BAB08005; -.
DR   BioCyc; MetaCyc:MONOMER-8441; -.
DR   BRENDA; 2.1.1.116; 1610.
DR   UniPathway; UPA00306; UER00444.
DR   GO; GO:0030784; F:3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   FunFam; 3.40.50.150:FF:000057; O-methyltransferase ZRP4; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR012967; COMT-like_dimerisation.
DR   InterPro; IPR001077; COMT_C.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11746; O-METHYLTRANSFERASE; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..350
FT                   /note="3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-
FT                   methyltransferase"
FT                   /id="PRO_0000204430"
FT   ACT_SITE        257
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         196
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         219
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         240
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   350 AA;  38776 MW;  547835EBCDEF9182 CRC64;
     MAFHGKDDVL DIKAQAHVWK IIYGFADSLV LRCAVELGIV DIIDNNNQPM ALADLASKLP
     VSDVNCDNLY RILRYLVKME ILRVEKSDDG QKKYALEPIA TLLSRNAKRS MVPMILGMTQ
     KDFMTPWHSM KDGLSDNGTA FEKAMGMTIW EYLEGHPDQS QLFNEGMAGE TRLLTSSLIS
     GSRDMFQGID SLVDVGGGNG TTVKAISDAF PHIKCTLFDL PHVIANSYDL PNIERIGGDM
     FKSVPSAQAI ILKLILHDWN DEDSIKILKQ CRNAVPKDGG KVIIVDVALD EESDHELSST
     RLILDIDMLV NTGGKERTKE VWEKIVKSAG FSGCKIRHIA AIQSVIEVFP
//