ID   RETO_PAPSO              Reviewed;         535 AA.
AC   P93479;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Reticuline oxidase;
DE            EC=1.21.3.3;
DE   AltName: Full=Berberine bridge-forming enzyme;
DE            Short=BBE;
DE   AltName: Full=Tetrahydroprotoberberine synthase;
DE   Flags: Precursor;
GN   Name=BBE1;
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND INDUCTION BY ELICITOR AND METHYL JASMONATE.
RC   STRAIN=cv. Marianne;
RX   PubMed=8972604; DOI=10.1104/pp.112.4.1669;
RA   Facchini P.J., Penzes C., Johnson A.G., Bull D.;
RT   "Molecular characterization of berberine bridge enzyme genes from opium
RT   poppy.";
RL   Plant Physiol. 112:1669-1677(1996).
CC   -!- FUNCTION: Essential to the formation of benzophenanthridine alkaloids
CC       in the response of plants to pathogenic attack. Catalyzes the
CC       stereospecific conversion of the N-methyl moiety of (S)-reticuline into
CC       the berberine bridge carbon of (S)-scoulerine. Involved in the
CC       biosynthesis of sanguinarine. {ECO:0000269|PubMed:8972604}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-reticuline + O2 = (S)-scoulerine + H(+) + H2O2;
CC         Xref=Rhea:RHEA:19885, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17129, ChEBI:CHEBI:57873; EC=1.21.3.3;
CC         Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P30986};
CC       Note=Binds 1 FAD per subunit in a bicovalent manner.
CC       {ECO:0000250|UniProtKB:P30986};
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000250|UniProtKB:P30986};
CC   -!- PATHWAY: Alkaloid biosynthesis; (S)-scoulerine biosynthesis; (S)-
CC       scoulerine from (S)-reticuline: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000305|PubMed:8972604}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and stems. Not detected in
CC       leaves or reproductive organs. {ECO:0000269|PubMed:8972604}.
CC   -!- DEVELOPMENTAL STAGE: Transiently induced 3 days after seed imbibition.
CC       {ECO:0000269|PubMed:8972604}.
CC   -!- INDUCTION: Up-regulated upon fungal elicitor treatment and by methyl
CC       jasmonate. {ECO:0000269|PubMed:8972604}.
CC   -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC       N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:P30986}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AF025430; AAC61839.1; -; Genomic_DNA.
DR   PIR; T07969; T07969.
DR   AlphaFoldDB; P93479; -.
DR   SMR; P93479; -.
DR   CAZy; AA7; Auxiliary Activities 7.
DR   KEGG; ag:AAC61839; -.
DR   BioCyc; MetaCyc:MON-20626; -.
DR   BRENDA; 1.21.3.3; 4515.
DR   UniPathway; UPA00319; UER00450.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050468; F:reticuline oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   2: Evidence at transcript level;
KW   Alkaloid metabolism; Cytoplasmic vesicle; FAD; Flavoprotein; Glycoprotein;
KW   Oxidoreductase; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..535
FT                   /note="Reticuline oxidase"
FT                   /id="PRO_0000020426"
FT   DOMAIN          71..245
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        108..170
FT                   /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT                   Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P30986"
SQ   SEQUENCE   535 AA;  59903 MW;  F0341EF38AB41239 CRC64;
     MMCRSLTLRF FLFIVLLQTC VRGGDVNDNL LSSCLNSHGV HNFTTLSTDT NSDYFKLLHA
     SMQNPLFAKP TVSKPSFIVM PGSKEELSST VHCCTRESWT IRLRSGGHSY EGLSYTADTP
     FVIVDMMNLN RISIDVLSET AWVESGATLG ELYYAIAQST DTLGFTAGWC PTVGSGGHIS
     GGGFGMMSRK YGLAADNVVD AILIDSNGAI LDREKMGDDV FWAIRGGGGG VWGAIYAWKI
     KLLPVPEKLT VFRVTKNVGI EDASSLLHKW QYVADELDED FTVSVLGGVN GNDAWLMFLG
     LHLGRKDAAK TIIDEKFPEL GLVDKEFQEM SWGESMAFLS GLDTISELNN RFLKFDERAF
     KTKVDFTKVS VPLNVFRHAL EMLSEQPGGF IALNGFGGKM SEISTDFTPF PHRKGTKLMF
     EYIIAWNQDE ESKIGEFSEW LAKFYDYLEP FVSKEPRVGY VNHIDLDIGG IDWRNKSSTT
     NAVEIARNWG ERYFSSNYER LVKAKTLIDP NNVFNHPQSI PPMMKFEEIY MLKEL