ID   C7195_ESCCA             Reviewed;         490 AA.
AC   B5UAQ8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Cheilanthifoline synthase;
DE            Short=CHS;
DE            EC=1.14.19.65 {ECO:0000269|PubMed:18854999};
DE   AltName: Full=Cytochrome P450 719A5;
GN   Name=CYP719A5;
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], TISSUE SPECIFICITY, INDUCTION BY METHYL
RP   JASMONATE, CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=18854999; DOI=10.1007/s00299-008-0624-8;
RA   Ikezawa N., Iwasa K., Sato F.;
RT   "CYP719A subfamily of cytochrome P450 oxygenases and isoquinoline alkaloid
RT   biosynthesis in Eschscholzia californica.";
RL   Plant Cell Rep. 28:123-133(2009).
CC   -!- FUNCTION: Methylenedioxy bridge-forming cytochrome P450 involved in the
CC       biosynthesis of isoquinoline alkaloids. Converts (S)-scoulerine into
CC       (R,S)-cheilanthifoline. Catalyzes an oxidative reaction that does not
CC       incorporate oxygen into the product. {ECO:0000269|PubMed:18854999}.
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:18854999};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
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. Detected in leaves and stems.
CC       {ECO:0000269|PubMed:18854999}.
CC   -!- INDUCTION: Up-regulated by methyl jasmonate treatment.
CC       {ECO:0000269|PubMed:18854999}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB434654; BAG75113.1; -; mRNA.
DR   AlphaFoldDB; B5UAQ8; -.
DR   SMR; B5UAQ8; -.
DR   BioCyc; MetaCyc:MON-12340; -.
DR   BRENDA; 1.14.19.65; 2173.
DR   BRENDA; 1.14.21.2; 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: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..490
FT                   /note="Cheilanthifoline synthase"
FT                   /id="PRO_0000418921"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         432
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"
SQ   SEQUENCE   490 AA;  55179 MW;  B82BF135E54FC7C3 CRC64;
     MEESLWVVTA TVVVVFAIAK LLKKSSSIST MEWPKGPKKL PIIGNLHQLG GEAFHVVLAN
     LAKIHGTVMT IWVGAWRPMI VISDIDKAWE VLVNKSSDYA GRDFPEITKI ISANWKNISC
     SDSGPFWQNL RKGLQGGALA PLNVISQYQL QERDMKNLIT SMQEKASKNN GILKPLDYLK
     EETIRLLSRL IFGQSFNDEN FVKGVHLALD DLVRISGYAS LADAFKFCEN LPSHKKSIRE
     VHEVNERVVN LVKPYLVKNP PTNTYLYFLN SQKFSDEVII SAVLEVYDLG VDSTASTAVW
     ALTFLVREPR VQEKLYKEII DLTGGERSVK VEDVSKLPYL QAVMKETMRM KPIAPMAIPH
     KTSRDTSLMG KKVNKGTSIM VNLYAIHHNP KVFPEPYKFI PERFLQGQES KYGDIKEMEQ
     SLLPFSAGMR ICAGMELGKL QYGFSLASLV EAFKWTCAVD GKLPDLSEDH CFILLMKNPL
     EARITPRTQL