ID   THS1_PAPSO              Reviewed;         180 AA.
AC   A0A2U9GHG9;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Thebaine synthase 1 {ECO:0000303|PubMed:29807982};
DE            EC=4.2.99.24 {ECO:0000269|PubMed:29807982};
GN   Name=THS1 {ECO:0000303|PubMed:29807982};
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, DISRUPTION PHENOTYPE, CATALYTIC
RP   ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND SUBUNIT.
RC   TISSUE=Latex;
RX   PubMed=29807982; DOI=10.1038/s41589-018-0059-7;
RA   Chen X., Hagel J.M., Chang L., Tucker J.E., Shiigi S.A., Yelpaala Y.,
RA   Chen H.-Y., Estrada R., Colbeck J., Enquist-Newman M., Ibanez A.B.,
RA   Cottarel G., Vidanes G.M., Facchini P.J.;
RT   "A pathogenesis-related 10 protein catalyzes the final step in thebaine
RT   biosynthesis.";
RL   Nat. Chem. Biol. 14:738-743(2018).
CC   -!- FUNCTION: Catalyzes the formation of thebaine from (7S)-salutaridinol
CC       7-O-acetate at the expense of labile hydroxylated by-products, which
CC       are preferentially produced by spontaneous allylic elimination.
CC       {ECO:0000269|PubMed:29807982}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7S)-O-acetylsalutaridinol = acetate + H(+) + thebaine;
CC         Xref=Rhea:RHEA:56908, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57672, ChEBI:CHEBI:59953; EC=4.2.99.24;
CC         Evidence={ECO:0000269|PubMed:29807982};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56909;
CC         Evidence={ECO:0000269|PubMed:29807982};
CC   -!- PATHWAY: Alkaloid biosynthesis; morphine biosynthesis.
CC       {ECO:0000269|PubMed:29807982}.
CC   -!- SUBUNIT: Homodimer (allosteric) and oligomers.
CC       {ECO:0000269|PubMed:29807982}.
CC   -!- TISSUE SPECIFICITY: Expressed in poppy latex.
CC       {ECO:0000269|PubMed:29807982}.
CC   -!- DISRUPTION PHENOTYPE: Plants lacking both THS1 and THS2 exhibit reduced
CC       thebaine levels but accumulation of the upstream intermediates
CC       salutaridinol and reticuline. {ECO:0000269|PubMed:29807982}.
CC   -!- SIMILARITY: Belongs to the MLP family. {ECO:0000305}.
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DR   EMBL; MH011342; AWQ63979.1; -; mRNA.
DR   AlphaFoldDB; A0A2U9GHG9; -.
DR   SMR; A0A2U9GHG9; -.
DR   BioCyc; MetaCyc:MON-20777; -.
DR   BRENDA; 4.2.99.24; 4515.
DR   UniPathway; UPA00852; -.
DR   GO; GO:0016835; F:carbon-oxygen lyase activity; IMP:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0009820; P:alkaloid metabolic process; IMP:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   Gene3D; 3.30.530.20; -; 1.
DR   InterPro; IPR000916; Bet_v_I/MLP.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   Pfam; PF00407; Bet_v_1; 1.
DR   SMART; SM01037; Bet_v_1; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; Lyase.
FT   CHAIN           1..180
FT                   /note="Thebaine synthase 1"
FT                   /id="PRO_0000446001"
FT   ACT_SITE        111
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A2U9GGW3"
FT   BINDING         96
FT                   /ligand="thebaine"
FT                   /ligand_id="ChEBI:CHEBI:59953"
FT                   /evidence="ECO:0000250|UniProtKB:A0A2U9GGW3"
FT   BINDING         127
FT                   /ligand="thebaine"
FT                   /ligand_id="ChEBI:CHEBI:59953"
FT                   /evidence="ECO:0000250|UniProtKB:A0A2U9GGW3"
SQ   SEQUENCE   180 AA;  20573 MW;  2BA983CE34DB8969 CRC64;
     MDSINSSIYF CAYFRELIIK LLMAPLGVSG LVGKLSTELE VDCDAEKYYN MYKHGEDVQK
     AVPHLCVDVK VISGDPTRSG CIKEWNVNID GKTIRSVEET THNDETKTLR HRVFEGDMMK
     DFKKFDTIMV VNPKPDGNGC VVTRSIEYEK TNENSPTPFD YLQFGHQAIE DMNKYLRDSE