ID   P6H_PAPSO               Reviewed;         541 AA.
AC   L7X0L7;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Protopine 6-monooxygenase;
DE            EC=1.14.14.98 {ECO:0000250|UniProtKB:F2Z9C1};
DE   AltName: Full=Protopine 6-hydroxylase;
DE            Short=P6H;
GN   Name=CYP82N3;
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].
RX   PubMed=23313486; DOI=10.1016/j.bbrc.2012.12.129;
RA   Beaudoin G.A., Facchini P.J.;
RT   "Isolation and characterization of a cDNA encoding (S)-cis-N-
RT   methylstylopine 14-hydroxylase from opium poppy, a key enzyme in
RT   sanguinarine biosynthesis.";
RL   Biochem. Biophys. Res. Commun. 431:597-603(2013).
CC   -!- FUNCTION: Catalyzes the conversion of protopine and allocryptopine to
CC       dihydrosanguinarine and dihydrochelerythrine, respectively, in the
CC       biosynthesis of isoquinoline alkaloid sanguinarine.
CC       {ECO:0000250|UniProtKB:F2Z9C1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + protopine + reduced [NADPH--hemoprotein reductase] = 6-
CC         hydroxyprotopine + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:22644, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16415, ChEBI:CHEBI:17104, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.98;
CC         Evidence={ECO:0000250|UniProtKB:F2Z9C1};
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; KC154002; AGC92397.1; -; mRNA.
DR   AlphaFoldDB; L7X0L7; -.
DR   SMR; L7X0L7; -.
DR   KEGG; ag:AGC92397; -.
DR   BRENDA; 1.14.13.55; 4515.
DR   BRENDA; 1.14.14.98; 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:0047087; F:protopine 6-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033075; P:isoquinoline alkaloid biosynthetic process; IEA:UniProt.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..541
FT                   /note="Protopine 6-monooxygenase"
FT                   /id="PRO_0000430259"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         476
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   541 AA;  61438 MW;  2F3DD32004999B5A CRC64;
     MDFSSLLLLL LNTWISAYSM AALLALVLVY NLRMTKSSSS KTTSLKGKKI ITRPPAVTGA
     WPVFGHLHLF GSGEHPHEML SKLAEKYGPS FTMKFGKHTT LVVSDTRVVK ECFTTNDTLF
     SNRPSTIAFD LMTYATDSIA FTPYSPYWRE LRKISTLKLL SNNRLESIKQ LRTSEVSVCF
     KELYDLTNKK NDNGAPVPID LKRWFDEVSN NVIMRVIFGK QNFGSKIVLG EDQEAVHYKK
     IMDELSRLSS LTMLSDMVPL LGWLDYFKGD LRAMKRNGKE LNSILQKWLE EHKSKKSSDA
     RQDFMDVMLS ISKDTQLYGH DQDTFIKATC LAMIMGGTNS TEVALTWILS LLMNNRCALH
     KAREEIDLLV GKDRQVEDSD VKNLTYMNAI IKETMRLYPL GFLLERDTKE DCEVSGFNIK
     GGTRLLINVW KLQRDPNVWT DPMEFKPERF LTENADIDVG GQHFELLPFG AGRRVCPGVS
     FALQFMHLVL ARLIHGYDME TLNGEDVDLS VSSGGHVNIK STPLELILTP RLHPELYDCE
     T