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

 RETO_ESCCA              Reviewed;         538 AA.
P30986;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
12-SEP-2018, entry version 98.
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;
Eschscholzia californica (California poppy).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Ranunculales;
Papaveraceae; Eschscholzioideae; Eschscholzia.
NCBI_TaxID=3467;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1946465; DOI=10.1073/pnas.88.22.9969;
Dittrich H., Kutchan T.M.;
"Molecular cloning, expression, and induction of berberine bridge
enzyme, an enzyme essential to the formation of benzophenanthridine
alkaloids in the response of plants to pathogenic attack.";
Proc. Natl. Acad. Sci. U.S.A. 88:9969-9973(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9484487; DOI=10.1023/A:1005917808232;
Hauschild K., Pauli H.H., Kutchan T.M.;
"Isolation and analysis of a gene bbe1 encoding the berberine bridge
enzyme from the California poppy Eschscholzia californica.";
Plant Mol. Biol. 36:473-478(1998).
[3]
X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 26-520 IN COMPLEX WITH FAD,
DISULFIDE BOND, GLYCOSYLATION AT ASN-471, AND COFACTOR.
PubMed=19457868; DOI=10.1074/jbc.M109.015727;
Winkler A., Motz K., Riedl S., Puhl M., Macheroux P., Gruber K.;
"Structural and mechanistic studies reveal the functional role of
bicovalent flavinylation in berberine bridge enzyme.";
J. Biol. Chem. 284:19993-20001(2009).
-!- 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 + O(2) = (S)-scoulerine +
H(2)O(2).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:19457868};
-!- COFACTOR:
Name=a metal cation; Xref=ChEBI:CHEBI:25213;
-!- PATHWAY: Alkaloid biosynthesis; (S)-scoulerine biosynthesis; (S)-
scoulerine from (S)-reticuline: step 1/1.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle.
-!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
oxidoreductase family. {ECO:0000305}.
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EMBL; S65550; AAB20352.1; -; mRNA.
EMBL; AF005655; AAC39358.1; -; Genomic_DNA.
PIR; A41533; A41533.
PDB; 3D2D; X-ray; 2.80 A; A=1-21, A=24-538.
PDB; 3D2H; X-ray; 1.65 A; A=1-21, A=24-538.
PDB; 3D2J; X-ray; 2.05 A; A=1-21, A=24-538.
PDB; 3FW7; X-ray; 1.82 A; A=24-520.
PDB; 3FW8; X-ray; 1.50 A; A=26-520.
PDB; 3FW9; X-ray; 1.49 A; A=26-520.
PDB; 3FWA; X-ray; 1.50 A; A=26-522.
PDB; 3GSY; X-ray; 1.63 A; A=24-538.
PDB; 4EC3; X-ray; 2.65 A; A=24-538.
PDB; 4PZF; X-ray; 2.20 A; A/B/C/D=1-538.
PDBsum; 3D2D; -.
PDBsum; 3D2H; -.
PDBsum; 3D2J; -.
PDBsum; 3FW7; -.
PDBsum; 3FW8; -.
PDBsum; 3FW9; -.
PDBsum; 3FWA; -.
PDBsum; 3GSY; -.
PDBsum; 4EC3; -.
PDBsum; 4PZF; -.
ProteinModelPortal; P30986; -.
SMR; P30986; -.
CAZy; AA7; Auxiliary Activities 7.
iPTMnet; P30986; -.
KEGG; ag:AAC39358; -.
KO; K00307; -.
BioCyc; MetaCyc:MONOMER-12338; -.
BRENDA; 1.21.3.3; 2173.
UniPathway; UPA00319; UER00450.
EvolutionaryTrace; P30986; -.
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.
1: Evidence at protein level;
3D-structure; Alkaloid metabolism; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
Glycoprotein; Oxidoreductase; Signal.
SIGNAL 1 23
CHAIN 24 538 Reticuline oxidase.
/FTId=PRO_0000020425.
DOMAIN 67 241 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
BINDING 104 104 FAD (covalent; via 2 links, pros
nitrogen). {ECO:0000269|PubMed:19457868}.
BINDING 166 166 FAD (covalent; via 2 links).
{ECO:0000269|PubMed:19457868}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19457868}.
DISULFID 30 89 {ECO:0000269|PubMed:19457868}.
HELIX 27 33 {ECO:0000244|PDB:3FW9}.
STRAND 39 41 {ECO:0000244|PDB:3FW9}.
STRAND 46 48 {ECO:0000244|PDB:3D2D}.
HELIX 49 56 {ECO:0000244|PDB:3FW9}.
HELIX 61 63 {ECO:0000244|PDB:3FW9}.
STRAND 65 68 {ECO:0000244|PDB:3D2J}.
STRAND 72 75 {ECO:0000244|PDB:3FW9}.
HELIX 80 91 {ECO:0000244|PDB:3FW9}.
TURN 92 94 {ECO:0000244|PDB:3FWA}.
STRAND 96 102 {ECO:0000244|PDB:3FW9}.
TURN 109 111 {ECO:0000244|PDB:3D2H}.
STRAND 117 121 {ECO:0000244|PDB:3FW9}.
STRAND 128 131 {ECO:0000244|PDB:3FW9}.
TURN 132 135 {ECO:0000244|PDB:3FW9}.
STRAND 136 140 {ECO:0000244|PDB:3FW9}.
HELIX 145 155 {ECO:0000244|PDB:3FW9}.
STRAND 157 160 {ECO:0000244|PDB:3FW9}.
HELIX 171 176 {ECO:0000244|PDB:3FW9}.
HELIX 184 187 {ECO:0000244|PDB:3FW9}.
HELIX 190 193 {ECO:0000244|PDB:3FW9}.
STRAND 194 200 {ECO:0000244|PDB:3FW9}.
HELIX 209 212 {ECO:0000244|PDB:3FW9}.
HELIX 214 220 {ECO:0000244|PDB:3FW9}.
STRAND 225 228 {ECO:0000244|PDB:4PZF}.
STRAND 230 237 {ECO:0000244|PDB:3FW9}.
STRAND 243 254 {ECO:0000244|PDB:3FW9}.
HELIX 256 272 {ECO:0000244|PDB:3FW9}.
STRAND 277 286 {ECO:0000244|PDB:3FW9}.
STRAND 289 300 {ECO:0000244|PDB:3FW9}.
HELIX 302 312 {ECO:0000244|PDB:3FW9}.
HELIX 314 316 {ECO:0000244|PDB:3FW9}.
HELIX 320 322 {ECO:0000244|PDB:3FW9}.
STRAND 324 326 {ECO:0000244|PDB:3FW9}.
HELIX 328 335 {ECO:0000244|PDB:3FW9}.
HELIX 341 345 {ECO:0000244|PDB:3FW9}.
STRAND 355 362 {ECO:0000244|PDB:3FW9}.
HELIX 369 381 {ECO:0000244|PDB:3FW9}.
STRAND 385 391 {ECO:0000244|PDB:3FW9}.
HELIX 394 397 {ECO:0000244|PDB:3FW9}.
STRAND 403 405 {ECO:0000244|PDB:3FW9}.
STRAND 414 422 {ECO:0000244|PDB:3FW9}.
HELIX 424 429 {ECO:0000244|PDB:3FW9}.
HELIX 430 444 {ECO:0000244|PDB:3FW9}.
HELIX 445 447 {ECO:0000244|PDB:3FW9}.
HELIX 457 459 {ECO:0000244|PDB:3FW9}.
HELIX 462 464 {ECO:0000244|PDB:3FW9}.
HELIX 472 476 {ECO:0000244|PDB:3FW9}.
HELIX 478 490 {ECO:0000244|PDB:3FW9}.
HELIX 491 493 {ECO:0000244|PDB:3FW9}.
HELIX 494 504 {ECO:0000244|PDB:3FW9}.
SEQUENCE 538 AA; 59958 MW; 1A505F86A06CDB24 CRC64;
MENKTPIFFS LSIFLSLLNC ALGGNDLLSC LTFNGVRNHT VFSADSDSDF NRFLHLSIQN
PLFQNSLISK PSAIILPGSK EELSNTIRCI RKGSWTIRLR SGGHSYEGLS YTSDTPFILI
DLMNLNRVSI DLESETAWVE SGSTLGELYY AITESSSKLG FTAGWCPTVG TGGHISGGGF
GMMSRKYGLA ADNVVDAILI DANGAILDRQ AMGEDVFWAI RGGGGGVWGA IYAWKIKLLP
VPEKVTVFRV TKNVAIDEAT SLLHKWQFVA EELEEDFTLS VLGGADEKQV WLTMLGFHFG
LKTVAKSTFD LLFPELGLVE EDYLEMSWGE SFAYLAGLET VSQLNNRFLK FDERAFKTKV
DLTKEPLPSK AFYGLLERLS KEPNGFIALN GFGGQMSKIS SDFTPFPHRS GTRLMVEYIV
AWNQSEQKKK TEFLDWLEKV YEFMKPFVSK NPRLGYVNHI DLDLGGIDWG NKTVVNNAIE
ISRSWGESYF LSNYERLIRA KTLIDPNNVF NHPQSIPPMA NFDYLEKTLG SDGGEVVI


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