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Reticuline oxidase (EC 1.21.3.3) (Berberine bridge-forming enzyme) (BBE) (Tetrahydroprotoberberine synthase)

 RETO_PAPSO              Reviewed;         535 AA.
P93479;
20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
12-SEP-2018, entry version 90.
RecName: Full=Reticuline oxidase;
EC=1.21.3.3;
AltName: Full=Berberine bridge-forming enzyme;
Short=BBE;
AltName: Full=Tetrahydroprotoberberine synthase;
Flags: Precursor;
Name=BBE1;
Papaver somniferum (Opium poppy).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Ranunculales;
Papaveraceae; Papaveroideae; Papaver.
NCBI_TaxID=3469;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND INDUCTION BY ELICITOR AND METHYL JASMONATE.
STRAIN=cv. Marianne;
PubMed=8972604; DOI=10.1104/pp.112.4.1669;
Facchini P.J., Penzes C., Johnson A.G., Bull D.;
"Molecular characterization of berberine bridge enzyme genes from
opium poppy.";
Plant Physiol. 112:1669-1677(1996).
-!- 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.
Involved in the biosynthesis of sanguinarine.
{ECO:0000269|PubMed:8972604}.
-!- CATALYTIC ACTIVITY: (S)-reticuline + O(2) = (S)-scoulerine +
H(2)O(2). {ECO:0000305}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:P30986};
-!- COFACTOR:
Name=a metal cation; Xref=ChEBI:CHEBI:25213;
Evidence={ECO:0000250|UniProtKB:P30986};
-!- PATHWAY: Alkaloid biosynthesis; (S)-scoulerine biosynthesis; (S)-
scoulerine from (S)-reticuline: step 1/1.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
{ECO:0000305|PubMed:8972604}.
-!- TISSUE SPECIFICITY: Expressed in roots and stems. Not detected in
leaves or reproductive organs. {ECO:0000269|PubMed:8972604}.
-!- DEVELOPMENTAL STAGE: Transiently induced 3 days after seed
imbibition. {ECO:0000269|PubMed:8972604}.
-!- INDUCTION: Up-regulated upon fungal elicitor treatment and by
methyl jasmonate. {ECO:0000269|PubMed:8972604}.
-!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
oxidoreductase family. {ECO:0000305}.
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EMBL; AF025430; AAC61839.1; -; Genomic_DNA.
PIR; T07969; T07969.
ProteinModelPortal; P93479; -.
SMR; P93479; -.
CAZy; AA7; Auxiliary Activities 7.
KEGG; ag:AAC61839; -.
KO; K00307; -.
BRENDA; 1.21.3.3; 4515.
UniPathway; UPA00319; UER00450.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0050468; F:reticuline oxidase activity; IEA:UniProtKB-EC.
GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
Gene3D; 3.30.43.10; -; 1.
InterPro; IPR012951; BBE.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR006094; Oxid_FAD_bind_N.
InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
Pfam; PF08031; BBE; 1.
Pfam; PF01565; FAD_binding_4; 1.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS51387; FAD_PCMH; 1.
PROSITE; PS00862; OX2_COVAL_FAD; 1.
2: Evidence at transcript level;
Alkaloid metabolism; Cytoplasmic vesicle; FAD; Flavoprotein;
Glycoprotein; Oxidoreductase; Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 535 Reticuline oxidase.
/FTId=PRO_0000020426.
DOMAIN 71 245 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
BINDING 108 108 FAD (covalent; via 2 links, pros
nitrogen).
{ECO:0000250|UniProtKB:P30986}.
BINDING 170 170 FAD (covalent; via 2 links).
{ECO:0000250|UniProtKB:P30986}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 475 475 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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