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 22-FEB-2023, entry version 85.
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}.
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; 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; 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; 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:SF246; LOW QUALITY PROTEIN: (S)-SCOULERINE 9-O-METHYLTRANSFERASE-LIKE; 1.
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 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
//
