ID   C7192_ESCCA             Reviewed;         495 AA.
AC   Q50LH3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=(S)-stylopine synthase 1 {ECO:0000305};
DE            Short=STS {ECO:0000303|PubMed:17250743};
DE            EC=1.14.19.64 {ECO:0000269|PubMed:17250743};
DE   AltName: Full=Cytochrome P450 719A2 {ECO:0000303|PubMed:17250743};
DE            Short=EcCYP719A2 {ECO:0000303|PubMed:17250743};
DE            Short=EcCYPB {ECO:0000303|PubMed:17250743};
GN   Name=CYP719A2 {ECO:0000303|PubMed:17250743};
OS   Eschscholzia californica (California poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae;
OC   Eschscholzioideae; Eschscholzia.
OX   NCBI_TaxID=3467;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION BY METHYL
RP   JASMONATE.
RX   PubMed=17250743; DOI=10.1111/j.1742-4658.2007.05652.x;
RA   Ikezawa N., Iwasa K., Sato F.;
RT   "Molecular cloning and characterization of methylenedioxy bridge-forming
RT   enzymes involved in stylopine biosynthesis in Eschscholzia californica.";
RL   FEBS J. 274:1019-1035(2007).
CC   -!- FUNCTION: Methylenedioxy bridge-forming cytochrome P450 involved in the
CC       biosynthesis of isoquinoline alkaloids. Converts (R,S)-cheilanthifoline
CC       to (S)-stylopine with a high substrate specificity. Catalyzes an
CC       oxidative reaction that does not incorporate oxygen into the product.
CC       {ECO:0000269|PubMed:17250743}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-cheilanthifoline + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (S)-stylopine + H(+) + 2 H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:13773, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16233, ChEBI:CHEBI:18285,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.19.64;
CC         Evidence={ECO:0000269|PubMed:17250743};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=32.3 uM for (R,S)-scoulerine {ECO:0000269|PubMed:17250743};
CC   -!- PATHWAY: Alkaloid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and at lower levels in stems and
CC       leaves. {ECO:0000269|PubMed:17250743}.
CC   -!- INDUCTION: Up-regulated by methyl jasmonate treatment.
CC       {ECO:0000269|PubMed:17250743}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB126257; BAD98250.1; -; mRNA.
DR   AlphaFoldDB; Q50LH3; -.
DR   SMR; Q50LH3; -.
DR   KEGG; ag:BAD98250; -.
DR   BRENDA; 1.14.19.64; 2173.
DR   BRENDA; 1.14.21.1; 2173.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047052; F:(S)-stylopine synthase activity; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033075; P:isoquinoline alkaloid biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..495
FT                   /note="(S)-stylopine synthase 1"
FT                   /id="PRO_0000418923"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         439
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q96242"
SQ   SEQUENCE   495 AA;  56420 MW;  E197618A3DA117DC CRC64;
     MEEMKILMMN NPWILTATAT TLLISIFLFF TRKSSKMVWP AGPKTLPIIG NMHLLGGTAL
     QVVLHNLAKV HGSVMTIWIG SWRPVIVVSD IERAWEVLVN KSSDYSARDM PDITKIISAD
     WKTISTSDSG PHWTNLRKGL QNVALSPHNL AAQFQFQEKD MTKMIQTLEE EARNNNGIVK
     PLDHMKKATL RLISRLVFGQ DFNNDKYVDD MHLAIEELIR VSGYARLAEA FYYAKYLPSH
     KKAVREVEEA QRRVQNLVSP FLSLNPPTNT YLHFLRSQKY DDEVIIFAIF EAYLLGVDST
     SLTTAWALAF LIREPNVQEK LYQELESFAS KNDRRILKVE DINKLQYLQA VIKETMRMKP
     IAPLAIPHKA CRDTSLMGKK IDKGTRVMVN IFALHHNKNV FNDPFKFMPE RFMKVDSQDA
     NGKAMEQSLL PFSAGMRICA GMELGKLQFS FALANLAYAF KWSCVADGVL PDMSDQLGFV
     LLMKTPLEAR INRRN