ID   C80B2_ESCCA             Reviewed;         488 AA.
AC   O64900;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=(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   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].
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:0000250|UniProtKB:O64899};
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}.
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DR   EMBL; AF014801; AAC39453.1; -; mRNA.
DR   PIR; T07963; T07963.
DR   KEGG; ag:AAC39453; -.
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: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; Microsome;
KW   Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..488
FT                   /note="(S)-N-methylcoclaurine 3'-hydroxylase isozyme 2"
FT                   /id="PRO_0000052158"
FT   TRANSMEM        3..23
FT                   /note="Helical"
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"
SQ   SEQUENCE   488 AA;  54896 MW;  5DBFFECBAAC1A3F2 CRC64;
     MEVVTVALIA VIISSILYLL FGSSGHKNLP PGPKPWPIVG NLLQLGEKPH AQFAELAQTY
     GDIFTLKMGT ETVVVASTSS AASEILKTHD RILSARYVFQ SFRVKGHVEN SIVWSDCTET
     WKNLRKVCRT ELFTQKMIES QAHVREKKCE EMVEYLMKKQ GEEVKIVEVI FGTLVNIFGN
     LIFSQNIFEL GXPNSGSSEF KEYLWRMLEL GNSTNPADYF PMLGKFDLFG QRKEVAECLK
     GIYAIWGAML QERKLAKKVD GYQSKNDFVD VCLDSGLNDY QINALLMELF GAGTETSAST
     IEWAMTELTK NPKITAKLRS ELQTVVGERS VKESDFPNLP YLEATVKETL RLHPPTPLLL
     PRRALETCTI LNYTIPKDCQ IMVNAWGIGR DPKTWIDPLT FSPERFLNSS VDFRGNDFSL
     IPFGAGRRIC PGLPIANQFI ALLVATFVQN LDWCLPNGMS VDHLIVEEKF GLTLQKEPPL
     FIVPKSRV