C7193_ESCCA
ID C7193_ESCCA Reviewed; 495 AA.
AC Q50LH4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Trifunctional (S)-stylopine synthase 2/(S)-nandinine synthase/(S)-canadine synthase {ECO:0000305};
DE Short=STS {ECO:0000303|PubMed:17250743};
DE EC=1.14.19.64 {ECO:0000269|PubMed:17250743};
DE EC=1.14.19.68 {ECO:0000269|PubMed:17250743};
DE EC=1.14.19.73 {ECO:0000269|PubMed:17250743};
DE AltName: Full=Cytochrome P450 719A3 {ECO:0000303|PubMed:17250743};
DE Short=EcCYP719A3 {ECO:0000303|PubMed:17250743};
DE Short=EcCYPA {ECO:0000303|PubMed:17250743};
GN Name=CYP719A3 {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 (S)-cheilanthifoline
CC to (S)-stylopine, (S)-scoulerine to (S)-nandinine and (S)-
CC tetrahydrocolumbamine to (S)-canadine, but only the ring A (2,3-
CC position) of the substrates is converted. Catalyzes an oxidative
CC 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 -!- 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:17250743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-scoulerine + O2 + reduced [NADPH--hemoprotein reductase] =
CC (S)-nandinine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:50364, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17129, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:132749; EC=1.14.19.73;
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=0.54 uM for (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; AB126256; BAD98249.1; -; mRNA.
DR AlphaFoldDB; Q50LH4; -.
DR SMR; Q50LH4; -.
DR PRIDE; Q50LH4; -.
DR KEGG; ag:BAD98249; -.
DR BRENDA; 1.14.19.73; 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:0047056; F:(S)-canadine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102632; F:(S)-nandinine synthase activity; IDA:UniProtKB.
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="Trifunctional (S)-stylopine synthase 2/(S)-nandinine
FT synthase/(S)-canadine synthase"
FT /id="PRO_0000418924"
FT TRANSMEM 10..30
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; 56806 MW; 7C9803BA27ABCB80 CRC64;
MEEMKFLIMN NPWVLFATSA TLLISIFLFF RRKSPNMAWP EGPKTLPIIG NMHLLGGTAL
QVVLYNLAKV HGRVMTIWIG SWRPVIVVSD IEQAWEVLVN KSSDYSARDM PDITKIVTAD
WRTISTSDSG PHWSNLRKGL QNIAISPNNL AAQFQFQEKD IIKMIQILEQ EAKDNNGIVK
PLDHLKKATI RLISRLVFGR DFEEDKYVED MHHAIEELIR ISGYARLAEA FYYAKYLPSH
RKAVRYVEEL KQIVKNLIRP FLSVNPPTNT YLHFLRSQNY DEEVVIFAIF ETYLLGVDST
SSTTAWALAY LVREPSVQDR LHQELDHFAK QNDRKILKVE DMNKLQYLQA VIKETMRMKP
IAPLAIPHKA CKDTSLMGNK INKGTRVMVN LYALHHNKNV FNDPFKFMPE RFLKVDNQDA
KGKAMEQSLL PFSAGMRICA GMELGKLQFS FALANLIFAF KWSCVDDGVL PDMSDELGFV
LLMKTPLKAR INPRN
