ID   C719B_PAPSO             Reviewed;         505 AA.
AC   B1NF18;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Salutaridine synthase {ECO:0000303|PubMed:19567876};
DE            EC=1.14.19.67 {ECO:0000269|PubMed:19567876, ECO:0000269|PubMed:22098111};
DE   AltName: Full=Cytochrome P450 719B1 {ECO:0000303|PubMed:19567876};
GN   Name=CYP719B1 {ECO:0000303|PubMed:19567876};
GN   Synonyms=SALSYN {ECO:0000303|PubMed:22098111};
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY ELICITOR.
RX   PubMed=19567876; DOI=10.1074/jbc.m109.033373;
RA   Gesell A., Rolf M., Ziegler J., Diaz Chavez M.L., Huang F.C., Kutchan T.M.;
RT   "CYP719B1 is salutaridine synthase, the C-C phenol-coupling enzyme of
RT   morphine biosynthesis in opium poppy.";
RL   J. Biol. Chem. 284:24432-24442(2009).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22098111; DOI=10.1111/j.1365-313x.2011.04855.x;
RA   Wijekoon C.P., Facchini P.J.;
RT   "Systematic knockdown of morphine pathway enzymes in opium poppy using
RT   virus-induced gene silencing.";
RL   Plant J. 69:1052-1063(2012).
CC   -!- FUNCTION: Catalyzes the formation of the morphinan alkaloid
CC       salutaridine by intramolecular phenol oxidation of (R)-reticuline
CC       without the incorporation of oxygen into the product (PubMed:19567876,
CC       PubMed:22098111). Can also use (R)-norreticuline as substrate
CC       (PubMed:19567876). {ECO:0000269|PubMed:19567876,
CC       ECO:0000269|PubMed:22098111}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-reticuline + O2 + reduced [NADPH--hemoprotein reductase] =
CC         H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC         salutaridine; Xref=Rhea:RHEA:17713, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58061, ChEBI:CHEBI:58144,
CC         ChEBI:CHEBI:58210; EC=1.14.19.67;
CC         Evidence={ECO:0000269|PubMed:19567876, ECO:0000269|PubMed:22098111};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.2 uM for (R)-reticuline {ECO:0000269|PubMed:19567876};
CC         Note=kcat is 1.64 min(-1) for (R)-reticuline.;
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:19567876};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:19567876};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Up-regulated by elicitor treatment.
CC       {ECO:0000269|PubMed:19567876}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; EF451150; ABR14720.1; -; mRNA.
DR   AlphaFoldDB; B1NF18; -.
DR   SMR; B1NF18; -.
DR   KEGG; ag:ABR14720; -.
DR   BioCyc; MetaCyc:MON-12299; -.
DR   BRENDA; 1.14.19.67; 4515.
DR   BRENDA; 1.14.21.4; 4515.
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: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:0047055; F:salutaridine synthase activity; IDA:UniProtKB.
DR   GO; GO:0097295; P:morphine biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
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.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..505
FT                   /note="Salutaridine synthase"
FT                   /id="PRO_0000418926"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         444
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:Q94IP1"
SQ   SEQUENCE   505 AA;  56380 MW;  5D226E842913F95C CRC64;
     MAPINIEGND FWMIACTVII VFALVKFMFS KISFYQSANT TEWPAGPKTL PIIGNLHQLG
     GGVPLQVALA NLAKVYGGAF TIWIGSWVPM IVISDIDNAR EVLVNKSADY SARDVPDILK
     IITANGKNIA DCDSGPFWHN LKKGLQSCIN PSNVMSLSRL QEKDMQNLIK SMQERASQHN
     GIIKPLDHAK EASMRLLSRV IFGHDFSNED LVIGVKDALD EMVRISGLAS LADAFKIAKY
     LPSQRKNIRD MYATRDRVYN LIQPHIVPNL PANSFLYFLT SQDYSDEIIY SMVLEIFGLG
     VDSTAATAVW ALSFLVGEQE IQEKLYREIN NRTGGQRPVK VVDLKELPYL QAVMKETLRM
     KPIAPLAVPH VAAKDTTFKG RRIVKGTKVM VNLYAIHHDP NVFPAPYKFM PERFLKDVNS
     DGRFGDINTM ESSLIPFGAG MRICGGVELA KQMVAFALAS MVNEFKWDCV SEGKLPDLSE
     AISFILYMKN PLEAKITPRT KPFRQ