ID   SMT_COPJA               Reviewed;         381 AA.
AC   Q39522;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=(S)-scoulerine 9-O-methyltransferase;
DE            EC=2.1.1.117;
GN   Name=SMT;
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 PROTEIN SEQUENCE OF 89-96; 136-158;
RP   160-183; 190-208; 212-236 AND 344-378.
RC   STRAIN=cv. dissecta;
RX   PubMed=7719631;
RA   Takeshita N., Fujiwara H., Mimura H., Fitchen J.H., Yamada Y., Sato F.;
RT   "Molecular cloning and characterization of S-adenosyl-L-
RT   methionine:scoulerine 9-O-methyltransferase from cultured cells of Coptis
RT   japonica.";
RL   Plant Cell Physiol. 36:29-36(1995).
CC   -!- FUNCTION: Produces a precursor of protoberberine alkaloids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-scoulerine + S-adenosyl-L-methionine = (S)-
CC         tetrahydrocolumbamine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:23808, ChEBI:CHEBI:15378, ChEBI:CHEBI:17129,
CC         ChEBI:CHEBI:17772, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC         EC=2.1.1.117;
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}.
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DR   EMBL; D29809; BAA06192.1; -; mRNA.
DR   AlphaFoldDB; Q39522; -.
DR   SMR; Q39522; -.
DR   KEGG; ag:BAA06192; -.
DR   BRENDA; 2.1.1.117; 1610.
DR   GO; GO:0030777; F:(S)-scoulerine 9-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   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR012967; Plant_MeTrfase_dimerisation.
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; PTHR11746; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..381
FT                   /note="(S)-scoulerine 9-O-methyltransferase"
FT                   /id="PRO_0000204431"
FT   ACT_SITE        284
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         223
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         246
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         266
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         267
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   381 AA;  41665 MW;  2A7F542E68624C0D CRC64;
     MCTSLSELKC PVFSTKRKLL LEFALRTSVD MAAQEGVNYL SGLGLSRLIC LPMALRAAIE
     LNVFEIISQA GPDAQLSPSD IVAKIPTKNP SAAISLDRIL RMLGASSILS VSTTKSGRVY
     GLNEESRCLV ASEDKVSVVP MLLFTSDKAV VESFYNIKDV VLEEGVIPFD RTHGMDFFQY
     AGKEERVNKS FNQAMGAGST IAFDEVFKVY KGFDNLKELV DVGGGIGTSL SNIVAKHPHI
     RGINFELPHV IGDAPDYPGV EHVPGDMFEG VPNAQNILLK WVLHDWDDDR SIKILKNCWK
     ALPENGTVIV IEFVLPQVLG NNAESFNALT PDLLMMALNP GGKERTTIEF DGLAKAAGFA
     ETKFFPISQG LHVMEFHKIN C