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   16-JUN-2009, entry version 58.
DE   RecName: Full=(S)-N-methylcoclaurine 3'-hydroxylase isozyme 2;
DE            EC=1.14.13.71;
DE   AltName: Full=Cytochrome P450 80B2;
GN   Name=CYP80B2;
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.
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DR   EMBL; AF014801; AAC39453.1; -; mRNA.
DR   PIR; T07963; T07963.
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    488       (S)-N-methylcoclaurine 3'-hydroxylase
FT                                isozyme 2.
FT                                /FTId=PRO_0000052158.
FT   TRANSMEM      3     23       Potential.
FT   METAL       430    430       Iron (heme axial ligand) (By similarity).
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
//