ID   BBLC2_TOBAC             Reviewed;         565 AA.
AC   A0A1S3ZQ17;
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 C-2 {ECO:0000305};
DE            EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE   Flags: Precursor;
GN   ORFNames=LOC107789210 {ECO:0000312|RefSeq:XP_016466471.1};
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_016466471.1; XM_016610985.1.
DR   SMR; A0A1S3ZQ17; -.
DR   GeneID; 107789210; -.
DR   KEGG; nta:107789210; -.
DR   OMA; AKFAGLN; -.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..565
FT                   /note="Berberine bridge enzyme-like C-2"
FT                   /id="PRO_5010190032"
FT   DOMAIN          72..248
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         109
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FI21"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        32..94
FT                   /evidence="ECO:0000250|UniProtKB:O64743"
SQ   SEQUENCE   565 AA;  62999 MW;  F5C611FD0010058C CRC64;
     MFPIIILISF SFTFLFASVT SGAGGVTNLS TCLINHNVHN FSIYPTKNDQ SSSNYFNLLD
     FSLQNLRFAA SYMPKPTVII LPNSKEELVS TILCCRQTSY EIRVRCGGHS YEGTSYVSFD
     GSPFVIVDLM KLDDVSVDLD SETAWAQGGA TIGQIYYAIS RVSDVHAFSA GSGPTVGSGG
     HISGGGFGLM SRKFGLAADS VVDALLIDAE GRLLDRKAMG EDVFWAIRGG GGGNWGIIYA
     WKIRLLKVPK IVTTCMIYRP GSKQYVAQLL QKWQIVTPNL ADDFTLGVLM RPIDLRADMN
     YGNTTPIETF PQFNALYLGP KTEAVSILNE AFPELDAKND DAKEMTWIES ALFFSELDNV
     FGNSSDDISR LKERYMDAKT FFKGKSDFVK TPFSMDAMMT ALVELEKNPK SFLVFDPYGG
     VMDKISDQAI AFPHRKGNLF AVQYYAFWNE EDDAKSNEYI EWTRGFYNKM APFVSSSPRG
     AYINYLDMDL GVNMDDDYLL RNASSRSSSS SVDAVERARA WGEMYFLHNY DRLVKAKTQI
     DPLNVFRHEQ SIPPMLGSTQ EHSSE