ID   C719E_ARGME             Reviewed;         494 AA.
AC   B1NF20;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Cheilanthifoline synthase {ECO:0000305};
DE            Short=CHS {ECO:0000305};
DE            EC=1.14.19.65 {ECO:0000269|PubMed:21094631};
DE   AltName: Full=Cytochrome P450 719A14 {ECO:0000303|PubMed:21094631};
GN   Name=CYP719A14 {ECO:0000303|PubMed:21094631};
OS   Argemone mexicana (Mexican prickly poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Argemone.
OX   NCBI_TaxID=54796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=21094631; DOI=10.1016/j.abb.2010.11.016;
RA   Diaz Chavez M.L., Rolf M., Gesell A., Kutchan T.M.;
RT   "Characterization of two methylenedioxy bridge-forming cytochrome P450-
RT   dependent enzymes of alkaloid formation in the Mexican prickly poppy
RT   Argemone mexicana.";
RL   Arch. Biochem. Biophys. 507:186-193(2011).
CC   -!- FUNCTION: Methylenedioxy bridge-forming cytochrome P450 involved in the
CC       biosynthesis of isoquinoline alkaloids. Converts (S)-scoulerine into
CC       (S)-cheilanthifoline, a precursor of sanguinarine. Catalyzes an
CC       oxidative reaction that does not incorporate oxygen into the product.
CC       {ECO:0000269|PubMed:21094631}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-scoulerine + O2 + reduced [NADPH--hemoprotein reductase] =
CC         (S)-cheilanthifoline + H(+) + 2 H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:20485, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16233, ChEBI:CHEBI:17129, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.19.65;
CC         Evidence={ECO:0000269|PubMed:21094631};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Note=kcat is 3.3 min(-1) for (S)-scoulerine.
CC         {ECO:0000269|PubMed:21094631};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:21094631};
CC       Temperature dependence:
CC         Optimum temperature is between 30-35 degrees Celsius.
CC         {ECO:0000269|PubMed:21094631};
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,
CC       leaves and plantlets. {ECO:0000269|PubMed:21094631}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; EF451152; ABR14722.1; -; mRNA.
DR   AlphaFoldDB; B1NF20; -.
DR   SMR; B1NF20; -.
DR   KEGG; ag:ABR14722; -.
DR   BioCyc; MetaCyc:MON-18679; -.
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:0047053; F:(S)-cheilanthifoline 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..494
FT                   /note="Cheilanthifoline synthase"
FT                   /id="PRO_0000418922"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         437
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   494 AA;  55780 MW;  3A21A92511ED39E7 CRC64;
     MDETIWLIIS TVIIVLGIAK FLLGKSSSSS LSTMEWPVGP KKLPIIGNLH QLGGDVFHVV
     LANLAKVYGS VFTIWVGSWR PMIIVSDIDK AWEVLVNKSS DYSARDMPDI TKIISANWKN
     ISCSDSGPFW HNLRKGLQGV ALTPLNVASQ YHLQERDMKN LINSMYKDAS RKNGILKPLD
     YLKEETVRLL SRLIFGQDFQ DEKLVVGMHH ALDDLVRISG YASLADAFKF CENLPSHKKS
     IREVHEVKKR VENLIRPHIV SNPPTNTYLY FLKTQDFNED IIISAILEVY DLGVDSTAST
     TVWALTFLVR EQEIQEKLYR EIVNVTGGKR SVKVEDVNKM PYLQAVMKET MRMKPIAPMA
     IPHKTSKDTS LMGKKINKGS VIMVNLYAIH HNPKVFPEPY KFMPERFLKD VNSDESLGNI
     KTMESSLLAF SAGMRICAGM ELGKLQLAFG LASLVHEFKW SCSVDGKLPD LSEDHCFILL
     MKNPLEAKIT CRIH