ID   OMT3B_PAPSO             Reviewed;         339 AA.
AC   A0A2S1WC15;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-JUL-2018, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Probable scoulerine-9-O-methyltransferase OMT3B {ECO:0000305};
DE            EC=2.1.1.117 {ECO:0000250|UniProtKB:I3PLQ7};
DE   AltName: Full=O-methyltransferase 3b {ECO:0000303|PubMed:29723437};
DE            Short=OMT3b {ECO:0000303|PubMed:29723437};
GN   Name=OMT3B {ECO:0000303|PubMed:29723437};
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Marianne;
RX   PubMed=29723437; DOI=10.1111/tpj.13947;
RA   Park M.R., Chen X., Lang D.E., Ng K.K.S., Facchini P.J.;
RT   "Heterodimeric O-methyltransferases involved in the biosynthesis of
RT   noscapine in opium poppy.";
RL   Plant J. 95:252-267(2018).
CC   -!- FUNCTION: Methyltransferase involved in the biosynthesis of the
CC       benzylisoquinoline alkaloid noscapine (By similarity). Catalyzes the
CC       conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine (By
CC       similarity). {ECO:0000250|UniProtKB:I3PLQ7}.
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; Evidence={ECO:0000250|UniProtKB:I3PLQ7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23809;
CC         Evidence={ECO:0000250|UniProtKB:I3PLQ7};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000305}.
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DR   EMBL; MH029295; AWJ64119.1; -; mRNA.
DR   AlphaFoldDB; A0A2S1WC15; -.
DR   SMR; A0A2S1WC15; -.
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:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..339
FT                   /note="Probable scoulerine-9-O-methyltransferase OMT3B"
FT                   /id="PRO_0000447595"
FT   ACT_SITE        246
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q5C9L7"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5C9L7"
FT   BINDING         165
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q5C9L7"
FT   BINDING         191
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:I3V6A7"
FT   BINDING         214
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         228..229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:I3V6A7"
FT   BINDING         242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:I3V6A7"
FT   BINDING         243..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5C9L7"
SQ   SEQUENCE   339 AA;  37691 MW;  1471137C0161D775 CRC64;
     MEVVSKIDQE NQAKIWKQIF GFAESLVLKC AVQLEIAETL HNNVKPMSLS ELASKLPAQP
     VNEDRLYRIL HFLVHMKLFN KDATTQKYSL APPAKYLLKG WEKSMVPSIL SVTDKDFTAP
     WNHLGDGLTG NCNAFEKALG KGIRVYMREN PEKDQLFNEG MACDTRLFAS ALVNECKSIF
     SDGINTLAGV GRGTGTAVKA ISKAFPDIKC TIHDLPEITS KNSKISRDVF KSVPSADAIF
     MKSILHEWND EECIQILKRC KEAIPKGGKV IIADVVIDMD STHPYSKSRL AMDLAMMLHT
     GGKERTEEDW KKLIDAAGFA SCKITKLSAL QSVIEAYPH