C719D_ARGME
ID C719D_ARGME Reviewed; 504 AA.
AC B1NF19;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Trifunctional (S)-stylopine synthase/(S)-nandinine synthase/(S)-canadine synthase {ECO:0000305};
DE Short=STS {ECO:0000305};
DE EC=1.14.19.64 {ECO:0000269|PubMed:21094631};
DE EC=1.14.19.68 {ECO:0000269|PubMed:21094631};
DE EC=1.14.19.73 {ECO:0000269|PubMed:21094631};
DE AltName: Full=Cytochrome P450 719A13 {ECO:0000303|PubMed:21094631};
GN Name=CYP719A13 {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)-cheilanthifoline
CC to (S)-stylopine, (S)-scoulerine to (S)-nandinine and (S)-
CC tetrahydrocolumbamine to (S)-canadine. Can be involved in both
CC sanguinarine and berberine biosynthesis. Catalyzes an oxidative
CC reaction that does not incorporate oxygen into the product.
CC {ECO:0000269|PubMed:21094631}.
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:21094631};
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:21094631};
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: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 13.8 min(-1) for (S)-cheilanthifoline.
CC {ECO:0000269|PubMed:21094631};
CC pH dependence:
CC Optimum pH is 8.0. {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; EF451151; ABR14721.1; -; mRNA.
DR AlphaFoldDB; B1NF19; -.
DR SMR; B1NF19; -.
DR KEGG; ag:ABR14721; -.
DR BioCyc; MetaCyc:MON-18680; -.
DR BRENDA; 1.14.19.64; 9127.
DR BRENDA; 1.14.19.65; 9127.
DR BRENDA; 1.14.19.68; 9127.
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; IDA:UniProtKB.
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..504
FT /note="Trifunctional (S)-stylopine synthase/(S)-nandinine
FT synthase/(S)-canadine synthase"
FT /id="PRO_0000418925"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 448
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 504 AA; 57452 MW; D0C0800367FC2186 CRC64;
MEEKIMTNNS PWILTSSTTT TTTILLSLLF TIFIILRRNK SSSSKMVWPT GPKTLPIIGN
MNILGGTALH VVLHNLAKTY GNVMTIWIGS WRPVIVVSDI DRAWEVLVNK SSDYSARDMP
EITKLATADW KTISSSDSGP FWTNLRKGLQ NVALSPQNLS SQSKFQERDI IKTIQNLKEE
AKMNNGIVKP LDHLKKAMVR LISRLIYGQD FDNDEYVEEM HHTIEELIRV SGYARLAEAF
YYAKYLPSHK KAVREVLQAN QRVQNLVRPL LSLNSPTNTY LHFLRSQNYE DEVIIFAIFE
AYLLGVDSTS STTAWALAYL IREPNVQEKL YEELKNFTND NDRKMVKFED LNKLQYLQAV
VKETMRMKPI APLAIPHKAC RETSLMGRKV NQGTRVMVNI YALHHNQNVW KEPYKFNPER
FLQKNQDGVD GKAMEQSLLP FSAGMRICAG MELGKLQFSF ALANLVNAFK WSCVSDGVFP
DMSDQLGFVL LMKTPLEAGI VPRM
