NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-24.
STRAIN=WOLF V29;
PubMed=7892226 [NCBI, ExPASy, EBI, Israel, Japan]
Kraus P.F.X., Kutchan T.M.;
"Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C-O phenol-coupling cytochrome P450 from the higher plant Berberis stolonifera.";
Proc. Natl. Acad. Sci. U.S.A. 92:2071-2075(1995).

Comments

FUNCTION: Forms the bisbenzylisoquinoline alkaloid berbamunine by phenol oxidation of N-methylcoclaurine without the incorporation of oxygen into the product. Oxidatively couples either two molecules of (R)-N-methylcoclaurine to form the (R,R) dimer guattegaumerine or one molecule each of (R)- and (S)-N-methylcoclaurine to form the (R,S) dimer berbamunine.
CATALYTIC ACTIVITY: (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + O₂ = berbamunine + NADP⁺ + 2 H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Alkaloid biosynthesis; berbamunine biosynthesis; berbamunine from (R)-N-methylcoclaurine and (S)-N-methylcoclaurine: step 1/1 .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
SIMILARITY: Belongs to the cytochrome P450 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U09610; AAC48987.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P47195.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0047054;	Molecular function: berbamunine synthase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0004497;	Molecular function: monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0009820;	Biological process: alkaloid metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

ProtoNet

P47195.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alkaloid metabolism; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 487`	`487`	`Berbamunine synthase.`	`PRO_0000052156`
`METAL`	`429 429`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 487 AA [This is the length of the unprocessed precursor]

Molecular weight: 55539 Da [This is the MW of the unprocessed precursor]

CRC64: AB2CBE4FFD26C672 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDYIVGFVSI SLVALLYFLL FKPKHTNLPP SPPAWPIVGH LPDLISKNSP PFLDYMSNIA 

        70         80         90        100        110        120 
QKYGPLIHLK FGLHSSIFAS TKEAAMEVLQ TNDKVLSGRQ PLPCFRIKPH IDYSILWSDS 

       130        140        150        160        170        180 
NSYWKKGRKI LHTEIFSQKM LQAQEKNRER VAGNLVNFIM TKVGDVVELR SWLFGCALNV 

       190        200        210        220        230        240 
LGHVVFSKDV FEYSDQSDEV GMDKLIHGML MTGGDFDVAS YFPVLARFDL HGLKRKMDEQ 

       250        260        270        280        290        300 
FKLLIKIWEG EVLARRANRN PEPKDMLDVL IANDFNEHQI NAMFMETFGP GSDTNSNIIE 

       310        320        330        340        350        360 
WALAQLIKNP DKLAKLREEL DRVVGRSSTV KESHFSELPY LQACVKETMR LYPPISIMIP 

       370        380        390        400        410        420 
HRCMETCQVM GYTIPKGMDV HVNAHAIGRD PKDWKDPLKF QPERFLDSDI EYNGKQFQFI 

       430        440        450        460        470        480 
PFGSGRRICP GRPLAVRIIP LVLASLVHAF GWELPDGVPN EKLDMEELFT LSLCMAKPLR 


VIPKVRI

P47195 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools