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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)DescriptionActionsGraphical viewLength
Binding sitei104FAD (covalent; via 2 links, pros nitrogen)1 Publication1
Binding sitei166FAD (covalent; via 2 links)1 Publication1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
ChainiPRO_000002042524 – 538Reticuline oxidaseAdd BLAST515

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 891 Publication
Glycosylationi38N-linked (GlcNAc...)1
Glycosylationi423N-linked (GlcNAc...)Sequence analysis1
Glycosylationi471N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1538
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 33Combined sources7
Beta strandi39 – 41Combined sources3
Beta strandi46 – 48Combined sources3
Helixi49 – 56Combined sources8
Helixi61 – 63Combined sources3
Beta strandi65 – 68Combined sources4
Beta strandi72 – 75Combined sources4
Helixi80 – 91Combined sources12
Turni92 – 94Combined sources3
Beta strandi96 – 102Combined sources7
Turni109 – 111Combined sources3
Beta strandi117 – 121Combined sources5
Beta strandi128 – 131Combined sources4
Turni132 – 135Combined sources4
Beta strandi136 – 140Combined sources5
Helixi145 – 155Combined sources11
Beta strandi157 – 160Combined sources4
Helixi171 – 176Combined sources6
Helixi184 – 187Combined sources4
Helixi190 – 193Combined sources4
Beta strandi194 – 200Combined sources7
Helixi209 – 212Combined sources4
Helixi214 – 220Combined sources7
Beta strandi225 – 228Combined sources4
Beta strandi230 – 237Combined sources8
Beta strandi243 – 254Combined sources12
Helixi256 – 272Combined sources17
Beta strandi277 – 286Combined sources10
Beta strandi289 – 300Combined sources12
Helixi302 – 312Combined sources11
Helixi314 – 316Combined sources3
Helixi320 – 322Combined sources3
Beta strandi324 – 326Combined sources3
Helixi328 – 335Combined sources8
Helixi341 – 345Combined sources5
Beta strandi355 – 362Combined sources8
Helixi369 – 381Combined sources13
Beta strandi385 – 391Combined sources7
Helixi394 – 397Combined sources4
Beta strandi403 – 405Combined sources3
Beta strandi414 – 422Combined sources9
Helixi424 – 429Combined sources6
Helixi430 – 444Combined sources15
Helixi445 – 447Combined sources3
Helixi457 – 459Combined sources3
Helixi462 – 464Combined sources3
Helixi472 – 476Combined sources5
Helixi478 – 490Combined sources13
Helixi491 – 493Combined sources3
Helixi494 – 504Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP30986.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30986.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini67 – 241FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST175

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
PDB 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.
SMRiP30986.
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: November 2, 2016
This is version 92 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.