Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P30986 (RETO_ESCCA)

Last modified October 13, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Reticuline oxidase
    EC=1.21.3.3
Alternative name(s):
    Berberine bridge-forming enzyme
      Short name=BBE
    Tetrahydroprotoberberine synthase
Gene names
Name: BBE1
OrganismEschscholzia californica (California poppy)
Taxonomic identifier3467 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › Ranunculales › Papaveraceae › Eschscholzioideae › Eschscholzia

Hide | Top

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (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.

Metal ion.

Pathway

Alkaloid biosynthesis; (S)-scoulerine biosynthesis; (S)-scoulerine from (S)-reticuline: step 1/1.

Subcellular location

Cytoplasmic vesicle.

Sequence similarities

Belongs to the oxygen-dependent FAD-linked oxidoreductase family.

Contains 1 FAD-binding PCMH-type domain.

Hide | Top

Ontologies

Keywords
   Biological processAlkaloid metabolism
   Cellular componentCytoplasmic vesicle
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processalkaloid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

reticuline oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 538515Reticuline oxidase
PRO_0000020425

Regions

Domain67 – 241175FAD-binding PCMH-type

Amino acid modifications

Modified residue1041Tele-8alpha-FAD histidine By similarity
Glycosylation381N-linked (GlcNAc...)
Glycosylation4231N-linked (GlcNAc...) Potential
Glycosylation4711N-linked (GlcNAc...) Potential

Secondary structure

1 .................................................................................. 538
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P30986-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 1A505F86A06CDB24

FASTA53859,958
        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

« Hide

Hide | Top

References

[1]"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."
Dittrich H., Kutchan T.M.
Proc. Natl. Acad. Sci. U.S.A. 88:9969-9973(1991) [PubMed: 1946465] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Isolation and analysis of a gene bbe1 encoding the berberine bridge enzyme from the California poppy Eschscholzia californica."
Hauschild K., Pauli H.H., Kutchan T.M.
Plant Mol. Biol. 36:473-478(1998) [PubMed: 9484487] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

S65550 mRNA. Translation: AAB20352.1.
AF005655 Genomic DNA. Translation: AAC39358.1.
PIRA41533.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3D2DX-ray2.80A1-538[»]
3D2HX-ray1.65A1-538[»]
3D2JX-ray2.05A1-538[»]
3FW7X-ray1.82A24-520[»]
3FW8X-ray1.50A26-520[»]
3FW9X-ray1.49A26-520[»]
3FWAX-ray1.50A26-522[»]
3GSYX-ray1.63A24-535[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.21.3.3. 2644.

Family and domain databases

InterProIPR012951. BBE.
IPR016166. FAD-bd_2.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
[Graphical view]
PfamPF08031. BBE. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
PROSITEPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameRETO_ESCCA
AccessionPrimary (citable) accession number: P30986
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 13, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents