ID   C80B1_ESCCA             Reviewed;         487 AA.
AC   O64899;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=(S)-N-methylcoclaurine 3'-hydroxylase isozyme 1;
DE            EC=1.14.14.102 {ECO:0000269|PubMed:9681018};
DE   AltName: Full=Cytochrome P450 80B1;
DE   Flags: Fragment;
GN   Name=CYP80B1;
OS   Eschscholzia californica (California poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae;
OC   Eschscholzioideae; Eschscholzia.
OX   NCBI_TaxID=3467;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
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   -!- FUNCTION: 3'-hydroxylation of (S)-N-methylcoclaurine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-N-methylcoclaurine + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (S)-3'-hydroxy-N-methylcoclaurine + H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:16649,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57993, ChEBI:CHEBI:58010, ChEBI:CHEBI:58210;
CC         EC=1.14.14.102; Evidence={ECO:0000269|PubMed:9681018};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-
CC       reticuline from (S)-norcoclaurine: step 3/4.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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; AF014800; AAC39452.1; -; mRNA.
DR   PIR; T07960; T07960.
DR   AlphaFoldDB; O64899; -.
DR   SMR; O64899; -.
DR   KEGG; ag:AAC39452; -.
DR   BioCyc; MetaCyc:MON-8429; -.
DR   SABIO-RK; O64899; -.
DR   UniPathway; UPA00306; UER00443.
DR   PRO; PR:O64899; -.
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:0050593; F:N-methylcoclaurine 3'-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   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..487
FT                   /note="(S)-N-methylcoclaurine 3'-hydroxylase isozyme 1"
FT                   /id="PRO_0000052157"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         429
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"
FT   NON_TER         1
SQ   SEQUENCE   487 AA;  54644 MW;  2EF90A9B67500AE2 CRC64;
     GTSTVALIAV IISSILYLLF GGSGHKNLPP GPKPWPIVGN LLQLGEKPHA QFAELAQTYG
     DIFTLKMGTE TVVVASTSSA ASEILKTHDR ILSARYVFQS FRVKGHVENS IVWSDCTETW
     KNLRKVCRTE LFTQKMIESQ AHVREKKCEE MVEYLMKKQG EEVKIVEVIF GTLVNIFGNL
     IFSQNIFELG DPNSGSSEFK EYLWRMLELG NSTNPADYFP MLGKFDLFGQ RKEVAECLKG
     IYAIWGAMLQ ERKLAKKVDG YKSKNDFVDV CLDSGLNDYQ INALLMELFG AGTETSASTI
     EWAMTELTKN PKITAKIRSE IQTVVGERSV KESDFPNLPY LEATVKETLR LHPPTPLLLP
     RRALETCTIL NYTIPKDCQI MVNAWGIGRD PKTWTDPLTF SPERFLNSSV DFRGNDFSLI
     PFGAGRRICP GLPIANQFIA LLVATFVQNL DWCLPNGMSV DHLIVEEKFG LTLQKEPPLF
     IVPKSRV