SOMT3_PAPSO
ID SOMT3_PAPSO Reviewed; 339 AA.
AC I3PLQ7;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Scoulerine-9-O-methyltransferase 3 {ECO:0000303|PubMed:22535422};
DE Short=PsSOMT3 {ECO:0000303|PubMed:22535422};
DE EC=2.1.1.117 {ECO:0000269|PubMed:22535422};
DE AltName: Full=O-methyltransferase 3 {ECO:0000303|PubMed:22653730};
GN Name=SOMT3 {ECO:0000303|PubMed:22535422};
GN Synonyms=OMT3 {ECO:0000303|PubMed:29723437},
GN PSMT3 {ECO:0000303|PubMed:22653730};
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, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=22535422; DOI=10.1104/pp.112.194886;
RA Dang T.T., Facchini P.J.;
RT "Characterization of three O-methyltransferases involved in noscapine
RT biosynthesis in opium poppy.";
RL Plant Physiol. 159:618-631(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=22653730; DOI=10.1126/science.1220757;
RA Winzer T., Gazda V., He Z., Kaminski F., Kern M., Larson T.R., Li Y.,
RA Meade F., Teodor R., Vaistij F.E., Walker C., Bowser T.A., Graham I.A.;
RT "A Papaver somniferum 10-gene cluster for synthesis of the anticancer
RT alkaloid noscapine.";
RL Science 336:1704-1708(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVE SITE, AND SUBUNIT.
RC STRAIN=cv. Bea's Choice;
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).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=27378283; DOI=10.1038/ncomms12137;
RA Li Y., Smolke C.D.;
RT "Engineering biosynthesis of the anticancer alkaloid noscapine in yeast.";
RL Nat. Commun. 7:12137-12137(2016).
RN [5]
RP FUNCTION.
RX PubMed=29610307; DOI=10.1073/pnas.1721469115;
RA Li Y., Li S., Thodey K., Trenchard I., Cravens A., Smolke C.D.;
RT "Complete biosynthesis of noscapine and halogenated alkaloids in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E3922-E3931(2018).
CC -!- FUNCTION: Methyltransferase involved in the biosynthesis of the
CC benzylisoquinoline alkaloid noscapine (PubMed:22535422,
CC PubMed:29723437, PubMed:27378283, PubMed:29610307). Catalyzes the
CC conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine
CC (PubMed:22535422). {ECO:0000269|PubMed:22535422,
CC ECO:0000269|PubMed:27378283, ECO:0000269|PubMed:29610307,
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:0000269|PubMed:22535422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23809;
CC Evidence={ECO:0000305|PubMed:22535422};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50.8 uM for (S)-scoulerine {ECO:0000269|PubMed:22535422};
CC KM=101.2 uM for S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:22535422};
CC Vmax=100.3 nmol/min/mg enzyme with (S)-scoulerine as substrate
CC {ECO:0000269|PubMed:22535422};
CC Vmax=115.6 nmol/min/mg enzyme with S-adenosyl-L-methionine as
CC substrate {ECO:0000269|PubMed:22535422};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer (PubMed:29723437). Forms heterodimer with SOMT2
CC (PubMed:29723437, PubMed:27378283). The heterodimer SOMT2-SOMT3
CC possesses 3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-methyltransferase
CC activity, where SOMT2 is the catalytic subunit (PubMed:29723437,
CC PubMed:27378283). {ECO:0000269|PubMed:27378283,
CC ECO:0000269|PubMed:29723437}.
CC -!- TISSUE SPECIFICITY: Highly expressed in capsules (PubMed:22653730).
CC Expressed is stems (PubMed:22653730, PubMed:22535422). Expressed at low
CC levels in roots (PubMed:22535422). {ECO:0000269|PubMed:22535422,
CC ECO:0000269|PubMed:22653730}.
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; JN185325; AFK73711.1; -; mRNA.
DR EMBL; JQ659001; AFB74613.1; -; Genomic_DNA.
DR EMBL; MH029294; AWJ64118.1; -; mRNA.
DR AlphaFoldDB; I3PLQ7; -.
DR SMR; I3PLQ7; -.
DR EnsemblPlants; RZC84734; RZC84734; C5167_047519.
DR Gramene; RZC84734; RZC84734; C5167_047519.
DR OMA; HNICKET; -.
DR BioCyc; MetaCyc:MON-17767; -.
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 1: Evidence at protein level;
KW Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..339
FT /note="Scoulerine-9-O-methyltransferase 3"
FT /id="PRO_0000447594"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020,
FT ECO:0000305|PubMed:29723437"
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; 37687 MW; 247DCA45DA0C61B3 CRC64;
MEVVSKIDQE NQAKIWKQIF GFAESLVLKC AVQLEIAETL HNNVKPMSLS ELASKLPAQP
VNEDRLYRIL HFLVHMKLFN KDATTQKYSL APPAKYLLKG WEKSMVPSIL SVTDKDFTAP
WNHLGDGLTG NCNAFEKALG KGIRVYMREN PEKDQLFNEG MACDTRLFAS ALVNECKSIF
SDGINTLAGV GRGTGTAVKA ISKAFPDIKC TIHDLPEVTS KNSKIPRDVF KSVPSADAIF
MKSILHEWND EECIQILKRC KEAIPKGGKV IIADVVIDMD STHPYSKSRL AMDLAMMLHT
GGKERTEEDW KKLIDAAGFA SCKITKLSAL QSVIEAYPH
