[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. PubMed=1946465 [NCBI, ExPASy, EBI, Israel, Japan] Dittrich H., Kutchan T.M.; "Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack."; Proc. Natl. Acad. Sci. U.S.A. 88:9969-9973(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1023/A:1005917808232; PubMed=9484487 [NCBI, ExPASy, EBI, Israel, Japan] Hauschild K., Pauli H.H., Kutchan T.M.; "Isolation and analysis of a gene bbe1 encoding the berberine bridge enzyme from the California poppy Eschscholzia californica."; Plant Mol. Biol. 36:473-478(1998).

Comments

FUNCTION: Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine.
CATALYTIC ACTIVITY: (S)-reticuline + O₂ = (S)-scoulerine + H₂O₂.
COFACTOR: FAD.
COFACTOR: Metal ion.
PATHWAY: Alkaloid biosynthesis; (S)-scoulerine biosynthesis; (S)-scoulerine from (S)-reticuline: step 1/1 .
SUBCELLULAR LOCATION: Cytoplasmic vesicle.
SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
SIMILARITY: Contains 1 FAD-binding PCMH-type domain.

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

S65550; AAB20352.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF005655; AAC39358.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A41533; A41533.

3D structure databases

ModBase

P30986.

Ontologies

GO:0031410;	Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0050468;	Molecular function: reticuline oxidase activity (inferred from electronic annotation from EC).
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

IPR012951; BBE.
IPR006094; Oxid_FAD_bind_N.
IPR006093; Oxy_OxRdtase_FAD_BS.
Graphical view of domain structure.

Pfam

PF08031; BBE; 1.
PF01565; FAD_binding_4; 1.
Pfam graphical view of domain structure.

PROSITE

PS51387; FAD_PCMH; 1.
PS00862; OX2_COVAL_FAD; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P30986.

Other

UniRef

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

Keywords

Alkaloid metabolism; Cytoplasmic vesicle; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 538`	`515`	`Reticuline oxidase.`	`PRO_0000020425`
`DOMAIN`	`67 241`	`175`	`FAD-binding PCMH-type.`
`MOD_RES`	`104 104`		`Tele-8alpha-FAD histidine (By similarity).`
`CARBOHYD`	`38 38`		`N-linked (GlcNAc...).`
`CARBOHYD`	`423 423`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`471 471`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 538 AA [This is the length of the unprocessed precursor]

Molecular weight: 59958 Da [This is the MW of the unprocessed precursor]

CRC64: 1A505F86A06CDB24 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MENKTPIFFS LSIFLSLLNC ALGGNDLLSC LTFNGVRNHT VFSADSDSDF NRFLHLSIQN 

        70         80         90        100        110        120 
PLFQNSLISK PSAIILPGSK EELSNTIRCI RKGSWTIRLR SGGHSYEGLS YTSDTPFILI 

       130        140        150        160        170        180 
DLMNLNRVSI DLESETAWVE SGSTLGELYY AITESSSKLG FTAGWCPTVG TGGHISGGGF 

       190        200        210        220        230        240 
GMMSRKYGLA ADNVVDAILI DANGAILDRQ AMGEDVFWAI RGGGGGVWGA IYAWKIKLLP 

       250        260        270        280        290        300 
VPEKVTVFRV TKNVAIDEAT SLLHKWQFVA EELEEDFTLS VLGGADEKQV WLTMLGFHFG 

       310        320        330        340        350        360 
LKTVAKSTFD LLFPELGLVE EDYLEMSWGE SFAYLAGLET VSQLNNRFLK FDERAFKTKV 

       370        380        390        400        410        420 
DLTKEPLPSK AFYGLLERLS KEPNGFIALN GFGGQMSKIS SDFTPFPHRS GTRLMVEYIV 

       430        440        450        460        470        480 
AWNQSEQKKK TEFLDWLEKV YEFMKPFVSK NPRLGYVNHI DLDLGGIDWG NKTVVNNAIE 

       490        500        510        520        530 
ISRSWGESYF LSNYERLIRA KTLIDPNNVF NHPQSIPPMA NFDYLEKTLG SDGGEVVI

P30986 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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