ID   C719A_COPJA             Reviewed;         491 AA.
AC   Q948Y1;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=(S)-canadine synthase;
DE            EC=1.14.19.68 {ECO:0000269|PubMed:12732624};
DE   AltName: Full=(S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming);
DE   AltName: Full=Cytochrome P450 719A1;
GN   Name=CYP719A1;
OS   Coptis japonica (Japanese goldthread).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Coptidoideae;
OC   Coptis.
OX   NCBI_TaxID=3442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=12732624; DOI=10.1074/jbc.m302470200;
RA   Ikezawa N., Tanaka M., Nagayoshi M., Shinkyo R., Sakaki T., Inouye K.,
RA   Sato F.;
RT   "Molecular cloning and characterization of CYP719, a methylenedioxy bridge-
RT   forming enzyme that belongs to a novel P450 family, from cultured Coptis
RT   japonica cells.";
RL   J. Biol. Chem. 278:38557-38565(2003).
CC   -!- FUNCTION: Involved in the last but one step of the biosynthesis of
CC       berberine, an antimicrobial benzylisoquinoline alkaloid. Converts (S)-
CC       tetrahydrocolumbamine (THC) to (S)-tetrahydroberberine (THB) also
CC       called (S)-canadine. {ECO:0000269|PubMed:12732624}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-tetrahydrocolumbamine + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (S)-canadine + H(+) + 2 H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:21456, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16592, ChEBI:CHEBI:17772,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.19.68;
CC         Evidence={ECO:0000269|PubMed:12732624};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in roots.
CC       {ECO:0000269|PubMed:12732624}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB026122; BAB68769.1; -; mRNA.
DR   AlphaFoldDB; Q948Y1; -.
DR   SMR; Q948Y1; -.
DR   KEGG; ag:BAB68769; -.
DR   SABIO-RK; Q948Y1; -.
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:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR   GO; GO:0047056; F:(S)-canadine 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; Microsome;
KW   Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..491
FT                   /note="(S)-canadine synthase"
FT                   /id="PRO_0000395196"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         434
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   491 AA;  55353 MW;  6E8308431B9540AC CRC64;
     MEMNPLLVCA TVAIVFATTT IIRILFSSSS LPQMKWPSGP RKLPIIGNLH QLGDDVLHVA
     LAKLAKVHGS VMTIWIGSWR PVIVISDIEK AWEVLVNKSA DYGARDMPEI TKIASASWHT
     ISTSDAGSFW QNVRKGLQSG AMGPLNVAAQ NQYQERDMKR LIKAMSDEAA NNNGIVKPLD
     HIKKNTVRLL TRLIFGQAFD DNKFIESMHY EIEDIIRISG YARLAEAFYY AKYLPSHKKA
     EREAFLVKCR VEELVRPLLS SKPPTNSYLY FLLSQNFEEE VIIFCIFELY LLGVDSTSST
     TTWALAYLIR EQGAQEKLYQ DIRMTLGDVD LVKIEDVNKL KYLQGVVKET MRMKPIAPLA
     IPHKTAKETT LMGTKVAKGT RIMVNLYALH HNQNIWPDPY KFMPERFLEG ETGTAYNKAM
     EQSFLPFSAG MRICAGMDLG KLQFAFALAN LVNAFKWSCV EEGKLPDMGE ELSFVLLMKT
     PLEARIAGRN V