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P93479 (RETO_PAPSO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismPapaver somniferum (Opium poppy)
Taxonomic identifier3469 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesPapaveraceaePapaver

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 535512Reticuline oxidase
PRO_0000020426

Regions

Domain71 – 245175FAD-binding PCMH-type

Sites

Binding site1041FAD (covalent; via 2 links, pros nitrogen) By similarity
Binding site1661FAD (covalent; via 2 links) By similarity

Amino acid modifications

Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation4751N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P93479 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: F0341EF38AB41239

FASTA53559,903
        10         20         30         40         50         60 
MMCRSLTLRF FLFIVLLQTC VRGGDVNDNL LSSCLNSHGV HNFTTLSTDT NSDYFKLLHA 

        70         80         90        100        110        120 
SMQNPLFAKP TVSKPSFIVM PGSKEELSST VHCCTRESWT IRLRSGGHSY EGLSYTADTP 

       130        140        150        160        170        180 
FVIVDMMNLN RISIDVLSET AWVESGATLG ELYYAIAQST DTLGFTAGWC PTVGSGGHIS 

       190        200        210        220        230        240 
GGGFGMMSRK YGLAADNVVD AILIDSNGAI LDREKMGDDV FWAIRGGGGG VWGAIYAWKI 

       250        260        270        280        290        300 
KLLPVPEKLT VFRVTKNVGI EDASSLLHKW QYVADELDED FTVSVLGGVN GNDAWLMFLG 

       310        320        330        340        350        360 
LHLGRKDAAK TIIDEKFPEL GLVDKEFQEM SWGESMAFLS GLDTISELNN RFLKFDERAF 

       370        380        390        400        410        420 
KTKVDFTKVS VPLNVFRHAL EMLSEQPGGF IALNGFGGKM SEISTDFTPF PHRKGTKLMF 

       430        440        450        460        470        480 
EYIIAWNQDE ESKIGEFSEW LAKFYDYLEP FVSKEPRVGY VNHIDLDIGG IDWRNKSSTT 

       490        500        510        520        530 
NAVEIARNWG ERYFSSNYER LVKAKTLIDP NNVFNHPQSI PPMMKFEEIY MLKEL 

« Hide

References

[1]"Molecular characterization of berberine bridge enzyme genes from opium poppy."
Facchini P.J., Penzes C., Johnson A.G., Bull D.
Plant Physiol. 112:1669-1677(1996) [PubMed: 8972604] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Marianne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF025430 Genomic DNA. Translation: AAC61839.1.
PIRT07969.

3D structure databases

ProteinModelPortalP93479.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR012951. BBE.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016168. FAD-linked_Oxase_FAD-bd_sub2.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
[Graphical view]
Gene3DG3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.
G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit.
PfamPF08031. BBE. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF56176. FAD-binding_2. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRETO_PAPSO
AccessionPrimary (citable) accession number: P93479
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: May 1, 1997
Last modified: October 19, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families