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   16-JUN-2009, entry version 57.
DE   RecName: Full=(S)-N-methylcoclaurine 3'-hydroxylase isozyme 1;
DE            EC=1.14.13.71;
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; Magnoliophyta; eudicotyledons; Ranunculales;
OC   Papaveraceae; Eschscholzioideae; Eschscholzia.
OX   NCBI_TaxID=3467;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98345996; PubMed=9681018;
RX   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
RT   alleles encoding (S)-N-methylcoclaurine 3'-hydroxylase (CYP80B1), a
RT   new methyl jasmonate-inducible cytochrome P-450-dependent mono-
RT   oxygenase of benzylisoquinoline alkaloid biosynthesis.";
RL   Plant J. 13:793-801(1998).
CC   -!- FUNCTION: 3'-hydroxylation of (S)-N-methylcoclaurine.
CC   -!- CATALYTIC ACTIVITY: (S)-N-methylcoclaurine + NADPH + O(2) = (S)-
CC       3'-hydroxy-N-methylcoclaurine + NADP(+) + H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-
CC       reticuline from (S)-norcoclaurine: step 3/4.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (Potential). Microsome membrane; Single-pass
CC       membrane protein (Potential).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF014800; AAC39452.1; -; mRNA.
DR   PIR; T07960; T07960.
DR   HSSP; P00179; 1DT6.
DR   BRENDA; 1.14.13.71; 2644.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050593; F:N-methylcoclaurine 3'-monooxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase; Transmembrane.
FT   CHAIN        <1    487       (S)-N-methylcoclaurine 3'-hydroxylase
FT                                isozyme 1.
FT                                /FTId=PRO_0000052157.
FT   TRANSMEM      4     24       Potential.
FT   METAL       429    429       Iron (heme axial ligand) (By similarity).
FT   NON_TER       1      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
//