ID   O64901_ESCCA            Unreviewed;       560 AA.
AC   O64901;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   SubName: Full=(S)-N-methylcoclaurine 3'-hydroxylase {ECO:0000313|EMBL:AAC39454.1};
GN   Name=CYP82B1 {ECO:0000313|EMBL:AAC39454.1};
OS   Eschscholzia californica (California poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae;
OC   Eschscholzioideae; Eschscholzia.
OX   NCBI_TaxID=3467 {ECO:0000313|EMBL:AAC39454.1};
RN   [1] {ECO:0000313|EMBL:AAC39454.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9681018; DOI=10.1046/j.1365-313X.1998.00085.x;
RA   Pauli H.H., Kutchan T.M.;
RT   "Molecular cloning and functional heterologous expression of two alleles
RT   encoding (S)-N-methylcoclaurine 3'-hydroxylase (CYP80B1), a new methyl
RT   jasmonate-inducible cytochrome P-450-dependent mono-oxygenase of
RT   benzylisoquinoline alkaloid biosynthesis.";
RL   Plant J. 13:793-801(1998).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000256|ARBA:ARBA00004913}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|RuleBase:RU000461}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF014802; AAC39454.1; -; mRNA.
DR   PIR; T07964; T07964.
DR   AlphaFoldDB; O64901; -.
DR   KEGG; ag:AAC39454; -.
DR   GO; GO:0016020; C: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   CDD; cd20654; CYP82; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR47947; CYTOCHROME P450 82C3-RELATED; 1.
DR   PANTHER; PTHR47947:SF19; CYTOCHROME P450 82C3-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   560 AA;  63004 MW;  85E3FB4C5DE11FC3 CRC64;
     MEKPILLQLQ AGILGLLALI CFLYYVIKVS LSTRNCNQLV KHPPEAAGSW PIVGHLPQLV
     GSGKPLFRVL GDMADKFGPI FMVRFGVYPT LVVSTWEMAK ECFTSNDKFL ASRPPSAASS
     YMTYDHAMFG FSFYGPYWRE IRKISTLHLL SHRRLELLKH VPHTEIHNFI KGLFGIWKDH
     QKQQQPTGRE DRDSVMLEMS QLFGYLTLNV VLSLVVGKRV CNYHADGHLD DGEEAGQGQK
     LHQTITDFFK LSGVSVASDA LPLLGLFDLG GKKESMKRVA KEMDFFAERW LQDKKLSLSL
     SSETNNKQND AGEGDGDDFM DVLMSILPDD DDSLFTKYSR DTVIKATSLS MVVAASDTTS
     VSLTWALSLL LNNIQVLRKA QDELDTKVGR DRHVEEKDID NLVYLQAIVK ETLRMYPAGP
     LSVPHEAIED CNVGGYHIKT GTRLLVNIWK LQRDPRVWSN PSEFRPERFL DNQSNGTLLD
     FRGQHFEYIP FGSGRRMCPG VNFATLILHM TLARLLQAFD LSTPSSSPVD MTEGSGLTMP
     KVTPLKVLLT PRLPLPLYDY
//