ID   BBLD2_TOBAC             Reviewed;         566 AA.
AC   A0A1S4CPU8;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Berberine bridge enzyme-like D-2 {ECO:0000305};
DE            EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE   Flags: Precursor;
GN   ORFNames=LOC107821171 {ECO:0000312|RefSeq:XP_016503076.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90;
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2]
RP   REVIEW ON ALKALOID BIOSYNTHESIS IN NICOTIANA TABACUM.
RX   PubMed=23953973; DOI=10.1016/j.phytochem.2013.06.002;
RA   Dewey R.E., Xie J.;
RT   "Molecular genetics of alkaloid biosynthesis in Nicotiana tabacum.";
RL   Phytochemistry 94:10-27(2013).
RN   [3]
RP   REVIEW ON NICOTINE BIOSYNTHESIS.
RX   PubMed=25582664; DOI=10.1007/s00438-015-0989-7;
RA   Wang X., Bennetzen J.L.;
RT   "Current status and prospects for the study of Nicotiana genomics,
RT   genetics, and nicotine biosynthesis genes.";
RL   Mol. Genet. Genomics 290:11-21(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural
CC       products, leading mainly to the production of anabasine, anatabine,
CC       nicotine and nornicotine, effective deterrents against herbivores with
CC       antiparasitic and pesticide properties (neurotoxins); nornicotine
CC       serves as the precursor in the synthesis of the carcinogen compound N'-
CC       nitrosonornicotine (NNN) (By similarity). Catalyzes a late oxidation
CC       step subsequent to the pyridine ring condensation reaction in the
CC       biosynthesis of alkaloids (By similarity).
CC       {ECO:0000250|UniProtKB:F1T160}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:F1T160};
CC   -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC       {ECO:0000250|UniProtKB:F1T160}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:F1T160}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   RefSeq; XP_016503076.1; XM_016647590.1.
DR   SMR; A0A1S4CPU8; -.
DR   STRING; 4097.A0A1S4CPU8; -.
DR   GeneID; 107821171; -.
DR   KEGG; nta:107821171; -.
DR   OMA; GYPFPGG; -.
DR   OrthoDB; 1049549at2759; -.
DR   UniPathway; UPA00107; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW   Oxidoreductase; Reference proteome; Signal; Vacuole.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..566
FT                   /note="Berberine bridge enzyme-like D-2"
FT                   /id="PRO_5010171957"
FT   DOMAIN          81..257
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         118
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FI21"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        42..103
FT                   /evidence="ECO:0000250|UniProtKB:O64743"
SQ   SEQUENCE   566 AA;  63149 MW;  06C178E8CC0F6A41 CRC64;
     MKRNISMSLQ RLLIILMMIS FLFTSLLVPS VSATNLNTIS TCLINYKVSN FSVYPTRNHA
     GNRYYNLLDF SIQNLRFAAS SKPKPTVIIV PESKEQLVSS VLCCRQGSYE IRVRCGGHSY
     EGTSYVSFDG SPFVVIDLMK LDDVSVDLDS ETAWVQGGAT LGQTYYAISR ASDVHGFSAG
     SCPTVGVGGH ISGGGFGFLS RKYGLAADNV VDALLVDAEG RLLDRKAMGE EVFWAIRGGG
     GGIWGIIYAW KIRLLKVPKT VTSFIVPRPG SKRYVSQLVH KWQLVAPKLD DDFYLSISMS
     SASKGNIPIE INAQFSGFYL GTKTEAISIL NEAFPELGVV ESDCKEMSWI ESTLFFSELD
     NVANTSDVSR LKERYFENKS YFKAKSDHVK TPISVGGIMT ALDVLEKEPN GHVIFDPYGA
     AMQRISEEAI AFPHRKGNLF RIQYLVVWKE KDNNNIAKSN GYIEWIREFY NTMAPHVSSS
     PRAAYVNYMD LDLGVMDDYL MLNTSITASA DHAVERARVW GEKYFLNNYD RLVKAKTKID
     PLNVFRHQQG IPPMFASMPE HTYSSK