ID   C80A1_BERST             Reviewed;         487 AA.
AC   P47195;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Berbamunine synthase;
DE            EC=1.14.19.66 {ECO:0000269|PubMed:8380416};
DE   AltName: Full=(S)-N-methylcoclaurine oxidase [C-O phenol-coupling];
DE   AltName: Full=CYPLXXX;
DE   AltName: Full=Cytochrome P450 80;
GN   Name=CYP80A1; Synonyms=CYP80;
OS   Berberis stolonifera (Barberry).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Berberidoideae;
OC   Berberis.
OX   NCBI_TaxID=33814;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-24.
RC   STRAIN=WOLF V29;
RX   PubMed=7892226; DOI=10.1073/pnas.92.6.2071;
RA   Kraus P.F.X., Kutchan T.M.;
RT   "Molecular cloning and heterologous expression of a cDNA encoding
RT   berbamunine synthase, a C-O phenol-coupling cytochrome P450 from the higher
RT   plant Berberis stolonifera.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2071-2075(1995).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8380416; DOI=10.1016/s0021-9258(18)54008-4;
RA   Stadler R., Zenk M.H.;
RT   "The purification and characterization of a unique cytochrome P-450 enzyme
RT   from Berberis stolonifera plant cell cultures.";
RL   J. Biol. Chem. 268:823-831(1993).
CC   -!- FUNCTION: Forms the bisbenzylisoquinoline alkaloid berbamunine by
CC       phenol oxidation of N-methylcoclaurine without the incorporation of
CC       oxygen into the product. Oxidatively couples either two molecules of
CC       (R)-N-methylcoclaurine to form the (R,R) dimer guattegaumerine or one
CC       molecule each of (R)- and (S)-N-methylcoclaurine to form the (R,S)
CC       dimer berbamunine. {ECO:0000269|PubMed:8380416}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N-methylcoclaurine + (S)-N-methylcoclaurine + O2 + reduced
CC         [NADPH--hemoprotein reductase] = berbamunine + H(+) + 2 H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:23576,
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:57755, ChEBI:CHEBI:57894, ChEBI:CHEBI:57993,
CC         ChEBI:CHEBI:58210; EC=1.14.19.66;
CC         Evidence={ECO:0000269|PubMed:8380416};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Alkaloid biosynthesis; berbamunine biosynthesis; berbamunine
CC       from (R)-N-methylcoclaurine and (S)-N-methylcoclaurine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U09610; AAC48987.1; -; mRNA.
DR   AlphaFoldDB; P47195; -.
DR   SMR; P47195; -.
DR   PRIDE; P47195; -.
DR   KEGG; ag:AAC48987; -.
DR   BRENDA; 1.14.19.66; 830.
DR   UniPathway; UPA00308; UER00446.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047054; F:berbamunine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035833; P:berbamunine biosynthetic process; IEA:UniProtKB-UniPathway.
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   Alkaloid metabolism; Direct protein sequencing; Endoplasmic reticulum;
KW   Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase;
KW   Oxidoreductase.
FT   CHAIN           1..487
FT                   /note="Berbamunine synthase"
FT                   /id="PRO_0000052156"
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"
SQ   SEQUENCE   487 AA;  55539 MW;  AB2CBE4FFD26C672 CRC64;
     MDYIVGFVSI SLVALLYFLL FKPKHTNLPP SPPAWPIVGH LPDLISKNSP PFLDYMSNIA
     QKYGPLIHLK FGLHSSIFAS TKEAAMEVLQ TNDKVLSGRQ PLPCFRIKPH IDYSILWSDS
     NSYWKKGRKI LHTEIFSQKM LQAQEKNRER VAGNLVNFIM TKVGDVVELR SWLFGCALNV
     LGHVVFSKDV FEYSDQSDEV GMDKLIHGML MTGGDFDVAS YFPVLARFDL HGLKRKMDEQ
     FKLLIKIWEG EVLARRANRN PEPKDMLDVL IANDFNEHQI NAMFMETFGP GSDTNSNIIE
     WALAQLIKNP DKLAKLREEL DRVVGRSSTV KESHFSELPY LQACVKETMR LYPPISIMIP
     HRCMETCQVM GYTIPKGMDV HVNAHAIGRD PKDWKDPLKF QPERFLDSDI EYNGKQFQFI
     PFGSGRRICP GRPLAVRIIP LVLASLVHAF GWELPDGVPN EKLDMEELFT LSLCMAKPLR
     VIPKVRI