THS2_PAPSO
ID THS2_PAPSO Reviewed; 160 AA.
AC A0A2U9GGW3;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Thebaine synthase 2 {ECO:0000303|PubMed:29807982};
DE EC=4.2.99.24 {ECO:0000269|PubMed:29807982};
GN Name=THS2 {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, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND BIOTECHNOLOGY.
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THEBAINE, AND ACTIVE
RP SITE.
RX PubMed=32703404; DOI=10.1016/j.bbrc.2020.05.199;
RA Chen C.C., Xue J., Peng W., Wang B., Zhang L., Liu W., Ko T.P., Huang J.W.,
RA Zhou S., Min J., Ma L., Dai L., Guo R.T., Yu X.;
RT "Structural insights into thebaine synthase 2 catalysis.";
RL Biochem. Biophys. Res. Commun. 529:156-161(2020).
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. No
CC visible activity toward (7S)-salutaridinol (at pH 7).
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 -!- ACTIVITY REGULATION: Slightly inhibited by salutaridine and (7S)-
CC salutaridinol. {ECO:0000269|PubMed:29807982}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=3.2 nmol/min/ug enzyme {ECO:0000269|PubMed:29807982};
CC pH dependence:
CC Optimum pH is 8. {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 -!- BIOTECHNOLOGY: Can be used to improve thebaine yield in engineered
CC yeast. {ECO:0000269|PubMed:29807982}.
CC -!- SIMILARITY: Belongs to the MLP family. {ECO:0000305}.
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DR EMBL; MH011343; AWQ63980.1; -; mRNA.
DR PDB; 6KA2; X-ray; 2.35 A; A/B/C/D=1-160.
DR PDB; 6KA3; X-ray; 1.95 A; A/B/C/D=1-160.
DR PDBsum; 6KA2; -.
DR PDBsum; 6KA3; -.
DR AlphaFoldDB; A0A2U9GGW3; -.
DR SMR; A0A2U9GGW3; -.
DR EnsemblPlants; RZC84754; RZC84754; C5167_047537.
DR Gramene; RZC84754; RZC84754; C5167_047537.
DR OMA; VDAHILE; -.
DR BioCyc; MetaCyc:MON-20778; -.
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 3D-structure; Alkaloid metabolism; Lyase.
FT CHAIN 1..160
FT /note="Thebaine synthase 2"
FT /id="PRO_0000446002"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:32703404,
FT ECO:0007744|PDB:6KA3"
FT BINDING 74
FT /ligand="thebaine"
FT /ligand_id="ChEBI:CHEBI:59953"
FT /evidence="ECO:0000269|PubMed:32703404,
FT ECO:0007744|PDB:6KA3"
FT BINDING 105
FT /ligand="thebaine"
FT /ligand_id="ChEBI:CHEBI:59953"
FT /evidence="ECO:0000269|PubMed:32703404,
FT ECO:0007744|PDB:6KA3"
FT STRAND 9..21
FT /evidence="ECO:0007829|PDB:6KA3"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:6KA3"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:6KA3"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6KA3"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:6KA3"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:6KA3"
FT STRAND 70..81
FT /evidence="ECO:0007829|PDB:6KA3"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:6KA3"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:6KA3"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:6KA3"
FT STRAND 100..111
FT /evidence="ECO:0007829|PDB:6KA3"
FT STRAND 115..130
FT /evidence="ECO:0007829|PDB:6KA3"
FT HELIX 137..155
FT /evidence="ECO:0007829|PDB:6KA3"
SQ SEQUENCE 160 AA; 18066 MW; 8BCDE6D79E34CFF8 CRC64;
MAPLGVSGLV GKLSTELEVD CDAEKYYNMY KHGEDVKKAV PHLCVDVKII SGDPTSSGCI
KEWNVNIDGK TIRSVEETTH DDETKTLRHR VFEGDVMKDF KKFDTIMVVN PKPDGNGCVV
TRSIEYEKTN ENSPTPFDYL QFGHQAIEDM NKYLRDSESN
