ID   C80B2_COPJA             Reviewed;         488 AA.
AC   Q9FXW4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Probable (S)-N-methylcoclaurine 3'-hydroxylase isozyme 2;
DE            EC=1.14.14.102 {ECO:0000250|UniProtKB:O64899};
DE   AltName: Full=Cytochrome P450 80B2;
GN   Name=CYP80B2;
OS   Coptis japonica (Japanese goldthread).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Coptidoideae;
OC   Coptis.
OX   NCBI_TaxID=3442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=12732624; DOI=10.1074/jbc.m302470200;
RA   Ikezawa N., Tanaka M., Nagayoshi M., Shinkyo R., Sakaki T., Inouye K.,
RA   Sato F.;
RT   "Molecular cloning and characterization of CYP719, a methylenedioxy bridge-
RT   forming enzyme that belongs to a novel P450 family, from cultured Coptis
RT   japonica cells.";
RL   J. Biol. Chem. 278:38557-38565(2003).
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:0000250|UniProtKB:O64899};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
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   -!- TISSUE SPECIFICITY: Expressed at low levels in roots.
CC       {ECO:0000269|PubMed:12732624}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB025030; BAB12433.1; -; mRNA.
DR   AlphaFoldDB; Q9FXW4; -.
DR   SMR; Q9FXW4; -.
DR   UniPathway; UPA00306; UER00443.
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:0019438; P:aromatic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound 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; Microsome;
KW   Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..488
FT                   /note="Probable (S)-N-methylcoclaurine 3'-hydroxylase
FT                   isozyme 2"
FT                   /id="PRO_0000395197"
FT   TRANSMEM        2..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         427
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   488 AA;  54782 MW;  5E97EE12B971C53B CRC64;
     MEVLSIAIVS FSFLLFLFFI LRDSRPKNLP PGPRPSPIVG NLLQLGDKPH AEFAKLAQKY
     GELFSLKLGS QTVVVASSPA AAAEILKTHD KILSGRYVFQ SFRVKEHVEN SIVWSECNDN
     WKLLRKVCRT ELFTPKMIES QSEIREAKAR EMVKFLRGKE GEVVKIVEVV FGTLVNIFGN
     LIFSKDVFDL EDPTGGSVEL KEHLWKLLDM GNSTNPADYF PIMGKLDLFG QRRAVAEVLQ
     QIYDVWGVML KERRGTKGSE SKNDFVDVLL NAGLDDQKIN ALLMELFGAG TETSASTIEW
     AITELTKKPL VVSKIRLELV NVVGDNTVKE SDLPHLPYLQ AFVKETLRLH PPTPLLLPRR
     ALETCTVMNY TIPKECQIMV NAWAIGRDPK TWDDPLNFKP ERFLSSDVDY KGNDFELIPF
     GGGRRICPGL PLASQFSNLI VATLVQNFEW SLPQGMSTSE LSMDEKFGLT LQKDPPLLIV
     LKARASNI