OMT2B_PAPSO
ID OMT2B_PAPSO Reviewed; 356 AA.
AC A0A2S1WBY6;
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 OMT2B {ECO:0000305};
DE EC=2.1.1.117 {ECO:0000250|UniProtKB:I3PLQ6};
DE AltName: Full=Inactive 3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-methyltransferase OMT2B {ECO:0000305};
DE AltName: Full=O-methyltransferase 2b {ECO:0000303|PubMed:29723437};
DE Short=OMT2b {ECO:0000303|PubMed:29723437};
GN Name=OMT2B {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], FUNCTION, AND POLYMORPHISM.
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). The heterodimers OMT2B-SOMT3 and OMT2B-6OMT do not possess
CC 3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-methyltransferase activity
CC (PubMed:29723437). {ECO:0000250|UniProtKB:I3PLQ6,
CC ECO:0000269|PubMed:29723437}.
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:I3PLQ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23809;
CC Evidence={ECO:0000250|UniProtKB:I3PLQ6};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305}.
CC -!- POLYMORPHISM: A single amino acid substitution of Ser-122 in cultivar
CC Bea's Choice (AC I3PLQ6) to Tyr-122 in cultivar Marianne (AC
CC A0A2S1WBY6) abolishes the 3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-
CC methyltransferase activity. {ECO:0000269|PubMed:29723437}.
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; MH029293; AWJ64117.1; -; mRNA.
DR AlphaFoldDB; A0A2S1WBY6; -.
DR SMR; A0A2S1WBY6; -.
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..356
FT /note="Probable scoulerine-9-O-methyltransferase OMT2B"
FT /id="PRO_0000447593"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5C9L7"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5C9L7"
FT BINDING 177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5C9L7"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:I3V6A7"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 245..246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:I3V6A7"
FT BINDING 259
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:I3V6A7"
FT BINDING 260..264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5C9L7"
SQ SEQUENCE 356 AA; 39163 MW; 0DCBBE0148B9E733 CRC64;
MEIHLESQEQ EMKYQSQIWN QICGTVDTSV LRCAIQLGIF DAIHNSGKPM ITLTELSSIV
SSPSSSSIEP CNLYRLVRYL SQMDLISIGE CLNEATVSLT GTSKLLLRNQ EKSLIDWVLA
IYCEMMVVVW HELSSSVSTP ADEPPIFQKV HGKNALELAG EFPEWNDLIN NAMTSDTSVT
KPALIQGCGK ILNGVTSLID VGGGHGATMA YIVEAFPHIK GAVIDLPHVV EAAPERPGVE
FISGDIFKSI SNADAVLLKY VLHNWEDTEC VNLLKRCKEA VPADKGKVII MDLVIDDDDN
SILTQAKLSL DLTVMNHGGG RERTKEDWRN LIEMSGFSRH EIIPISAMPS IIVAYP
