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Protein

Reticuline oxidase

Gene

BBE1

Organism
Eschscholzia californica (California poppy)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

(S)-reticuline + O2 = (S)-scoulerine + H2O2.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: (S)-scoulerine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (S)-scoulerine from (S)-reticuline.
Proteins known to be involved in this subpathway in this organism are:
  1. Reticuline oxidase (BBE1)
This subpathway is part of the pathway (S)-scoulerine biosynthesis, which is itself part of Alkaloid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-scoulerine from (S)-reticuline, the pathway (S)-scoulerine biosynthesis and in Alkaloid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041FAD (covalent; via 2 links, pros nitrogen)1 Publication
Binding sitei166 – 1661FAD (covalent; via 2 links)1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Alkaloid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12338.
BRENDAi1.21.3.3. 2173.
UniPathwayiUPA00319; UER00450.

Protein family/group databases

CAZyiAA7. Auxiliary Activities 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Reticuline oxidase (EC:1.21.3.3)
Alternative name(s):
Berberine bridge-forming enzyme
Short name:
BBE
Tetrahydroprotoberberine synthase
Gene namesi
Name:BBE1
OrganismiEschscholzia californica (California poppy)
Taxonomic identifieri3467 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesPapaveraceaeEschscholzioideaeEschscholzia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 538515Reticuline oxidasePRO_0000020425Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 891 Publication
Glycosylationi38 – 381N-linked (GlcNAc...)
Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence analysis
Glycosylationi471 – 4711N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1
538
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 337Combined sources
Beta strandi39 – 413Combined sources
Beta strandi46 – 483Combined sources
Helixi49 – 568Combined sources
Helixi61 – 633Combined sources
Beta strandi65 – 684Combined sources
Beta strandi72 – 754Combined sources
Helixi80 – 9112Combined sources
Turni92 – 943Combined sources
Beta strandi96 – 1027Combined sources
Turni109 – 1113Combined sources
Beta strandi117 – 1215Combined sources
Beta strandi128 – 1314Combined sources
Turni132 – 1354Combined sources
Beta strandi136 – 1405Combined sources
Helixi145 – 15511Combined sources
Beta strandi157 – 1604Combined sources
Helixi171 – 1766Combined sources
Helixi184 – 1874Combined sources
Helixi190 – 1934Combined sources
Beta strandi194 – 2007Combined sources
Helixi209 – 2124Combined sources
Helixi214 – 2207Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi230 – 2378Combined sources
Beta strandi243 – 25412Combined sources
Helixi256 – 27217Combined sources
Beta strandi277 – 28610Combined sources
Beta strandi289 – 30012Combined sources
Helixi302 – 31211Combined sources
Helixi314 – 3163Combined sources
Helixi320 – 3223Combined sources
Beta strandi324 – 3263Combined sources
Helixi328 – 3358Combined sources
Helixi341 – 3455Combined sources
Beta strandi355 – 3628Combined sources
Helixi369 – 38113Combined sources
Beta strandi385 – 3917Combined sources
Helixi394 – 3974Combined sources
Beta strandi403 – 4053Combined sources
Beta strandi414 – 4229Combined sources
Helixi424 – 4296Combined sources
Helixi430 – 44415Combined sources
Helixi445 – 4473Combined sources
Helixi457 – 4593Combined sources
Helixi462 – 4643Combined sources
Helixi472 – 4765Combined sources
Helixi478 – 49013Combined sources
Helixi491 – 4933Combined sources
Helixi494 – 50411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray1.63A24-538[»]
4EC3X-ray2.65A24-538[»]
4PZFX-ray2.20A/B/C/D1-538[»]
ProteinModelPortaliP30986.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30986.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 241175FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

KOiK00307.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR012951. BBE.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
[Graphical view]
PfamiPF08031. BBE. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30986-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENKTPIFFS LSIFLSLLNC ALGGNDLLSC LTFNGVRNHT VFSADSDSDF
60 70 80 90 100
NRFLHLSIQN PLFQNSLISK PSAIILPGSK EELSNTIRCI RKGSWTIRLR
110 120 130 140 150
SGGHSYEGLS YTSDTPFILI DLMNLNRVSI DLESETAWVE SGSTLGELYY
160 170 180 190 200
AITESSSKLG FTAGWCPTVG TGGHISGGGF GMMSRKYGLA ADNVVDAILI
210 220 230 240 250
DANGAILDRQ AMGEDVFWAI RGGGGGVWGA IYAWKIKLLP VPEKVTVFRV
260 270 280 290 300
TKNVAIDEAT SLLHKWQFVA EELEEDFTLS VLGGADEKQV WLTMLGFHFG
310 320 330 340 350
LKTVAKSTFD LLFPELGLVE EDYLEMSWGE SFAYLAGLET VSQLNNRFLK
360 370 380 390 400
FDERAFKTKV DLTKEPLPSK AFYGLLERLS KEPNGFIALN GFGGQMSKIS
410 420 430 440 450
SDFTPFPHRS GTRLMVEYIV AWNQSEQKKK TEFLDWLEKV YEFMKPFVSK
460 470 480 490 500
NPRLGYVNHI DLDLGGIDWG NKTVVNNAIE ISRSWGESYF LSNYERLIRA
510 520 530
KTLIDPNNVF NHPQSIPPMA NFDYLEKTLG SDGGEVVI
Length:538
Mass (Da):59,958
Last modified:July 1, 1993 - v1
Checksum:i1A505F86A06CDB24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S65550 mRNA. Translation: AAB20352.1.
AF005655 Genomic DNA. Translation: AAC39358.1.
PIRiA41533.

Genome annotation databases

KEGGiag:AAC39358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S65550 mRNA. Translation: AAB20352.1.
AF005655 Genomic DNA. Translation: AAC39358.1.
PIRiA41533.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray1.63A24-538[»]
4EC3X-ray2.65A24-538[»]
4PZFX-ray2.20A/B/C/D1-538[»]
ProteinModelPortaliP30986.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA7. Auxiliary Activities 7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC39358.

Phylogenomic databases

KOiK00307.

Enzyme and pathway databases

UniPathwayiUPA00319; UER00450.
BioCyciMetaCyc:MONOMER-12338.
BRENDAi1.21.3.3. 2173.

Miscellaneous databases

EvolutionaryTraceiP30986.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR012951. BBE.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
[Graphical view]
PfamiPF08031. BBE. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRETO_ESCCA
AccessioniPrimary (citable) accession number: P30986
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 7, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.