ID   C80BX_PAPSO             Reviewed;         440 AA.
AC   I3V6B1;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=(S)-N-methylcoclaurine 3'-hydroxylase-like protein {ECO:0000305};
DE            EC=1.14.-.- {ECO:0000305};
DE   AltName: Full=Cytochrome P450 80BX {ECO:0000305};
GN   Name=CYP80BX {ECO:0000305};
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469 {ECO:0000312|EMBL:AFK73713.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=22527754; DOI=10.1007/s11103-012-9913-2;
RA   Desgagne-Penix I., Farrow S.C., Cram D., Nowak J., Facchini P.J.;
RT   "Integration of deep transcript and targeted metabolite profiles for eight
RT   cultivars of opium poppy.";
RL   Plant Mol. Biol. 79:295-313(2012).
RN   [2]
RP   FUNCTION.
RX   PubMed=22725256; DOI=10.1111/j.1365-313x.2012.05084.x;
RA   Desgagne-Penix I., Facchini P.J.;
RT   "Systematic silencing of benzylisoquinoline alkaloid biosynthetic genes
RT   reveals the major route to papaverine in opium poppy.";
RL   Plant J. 72:331-344(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of benzylisoquinoline alkaloids.
CC       Probably involved in papaverine biosynthesis since its transcripts are
CC       abundant only in cultivars with substantial papaverine accumulation.
CC       May catalyze the 3'-hydroxylation of (S)-coclaurine.
CC       {ECO:0000269|PubMed:22527754, ECO:0000269|PubMed:22725256}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000255|RuleBase:RU000461}.
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DR   EMBL; JN185327; AFK73713.1; -; mRNA.
DR   AlphaFoldDB; I3V6B1; -.
DR   SMR; I3V6B1; -.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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   Alkaloid metabolism; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..440
FT                   /note="(S)-N-methylcoclaurine 3'-hydroxylase-like protein"
FT                   /id="PRO_0000433983"
FT   TRANSMEM        2..21
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   BINDING         430
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:P04798"
SQ   SEQUENCE   440 AA;  49423 MW;  7ED9BC2BE554BBD0 CRC64;
     MEIVTVALIA IVFTTFLYLI VRESSPNGLP PGPKPWPIVG NLLQLGEKPH SQFAQLAETY
     GDLFTLKLGT QTVVVASTPL AASEVLKAHD RTLCGRYVFQ SFRVKNHVEN SIVWNECNET
     WKKLRKVCRT QLFTQKMIEN QAEVREIKTM EMVKYLKKNE GIEVKIVEVI FGTLVNMFGN
     LIFSQDIFKL GDESSGSLEM KQHIWRMLEL GNSANPGDYV PLLGSLDLFG QRKDVADCLQ
     GVYGVWGAML KERRIAKRQI NGDTKNDFVD VLLDSGLDDQ QINSLLLDMF SAGTETTAST
     IEWALTELTK NPQVTADIRS ELLSVVGKRA VKESDILNLP YLQAFVKETL RLHPPTPLLI
     PRRALETCQV LNYTIPKECQ IMVNAWGIGR DPKTWTDPLK FSPDRFLNSS IDFKGNDFEL
     IPFGAGRRIC PGVPPGNSVY