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BBLB_TOBAC
ID   BBLB_TOBAC              Reviewed;         568 AA.
AC   A7WPL6;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Berberine bridge enzyme-like B {ECO:0000303|PubMed:21343426};
DE            Short=NtBBLb {ECO:0000303|PubMed:21343426};
DE            EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE   Flags: Precursor;
GN   Name=BBLB {ECO:0000303|PubMed:21343426};
GN   Synonyms=BBL2.2 {ECO:0000305}, T440 {ECO:0000303|PubMed:12826618,
GN   ECO:0000303|PubMed:18001808};
GN   ORFNames=LOC107830440 {ECO:0000312|RefSeq:XP_016513471.1};
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 [MRNA], AND INDUCTION BY JASMONIC ACID.
RC   STRAIN=cv. Bright Yellow 2; TISSUE=Protoplast;
RX   PubMed=12826618; DOI=10.1073/pnas.1032967100;
RA   Goossens A., Haekkinen S.T., Laakso I., Seppaenen-Laakso T., Biondi S.,
RA   De Sutter V., Lammertyn F., Nuutila A.M., Soederlund H., Zabeau M.,
RA   Inze D., Oksman-Caldentey K.-M.;
RT   "A functional genomics approach toward the understanding of secondary
RT   metabolism in plant cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8595-8600(2003).
RN   [2]
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   [3]
RP   REVIEW.
RC   TISSUE=Protoplast;
RX   PubMed=18001808; DOI=10.1016/j.phytochem.2007.09.010;
RA   Haekkinen S.T., Tilleman S., Swiatek A., De Sutter V., Rischer H.,
RA   Vanhoutte I., Van Onckelen H., Hilson P., Inze D., Oksman-Caldentey K.-M.,
RA   Goossens A.;
RT   "Functional characterisation of genes involved in pyridine alkaloid
RT   biosynthesis in tobacco.";
RL   Phytochemistry 68:2773-2785(2007).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND INDUCTION BY JASMONIC ACID.
RC   STRAIN=cv. Petit Havana SR1;
RX   PubMed=21343426; DOI=10.1104/pp.110.170878;
RA   Kajikawa M., Shoji T., Kato A., Hashimoto T.;
RT   "Vacuole-localized berberine bridge enzyme-like proteins are required for a
RT   late step of nicotine biosynthesis in tobacco.";
RL   Plant Physiol. 155:2010-2022(2011).
RN   [5]
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   [6]
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) (PubMed:21343426). Catalyzes a late oxidation
CC       step subsequent to the pyridine ring condensation reaction in the
CC       biosynthesis of alkaloids (PubMed:21343426).
CC       {ECO:0000269|PubMed:21343426}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O64743};
CC   -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC       {ECO:0000269|PubMed:21343426}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:21343426}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots.
CC       {ECO:0000269|PubMed:21343426}.
CC   -!- INDUCTION: By jasmonic acid (MeJA). {ECO:0000269|PubMed:12826618,
CC       ECO:0000269|PubMed:21343426}.
CC   -!- DISRUPTION PHENOTYPE: Strongly reduced nicotine biosynthesis but
CC       accumulation of dihydromethanicotine (PubMed:21343426). Inhibition of
CC       jasmonate-elicited formation of anatabine and other pyridine alkaloids
CC       (PubMed:21343426). {ECO:0000269|PubMed:21343426}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AM851017; CAO99130.1; -; mRNA.
DR   RefSeq; NP_001313171.1; NM_001326242.1.
DR   RefSeq; XP_016513471.1; XM_016657985.1.
DR   SMR; A7WPL6; -.
DR   GeneID; 107830440; -.
DR   KEGG; nta:107830440; -.
DR   OMA; GEARMAW; -.
DR   OrthoDB; 1049549at2759; -.
DR   UniPathway; UPA00107; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0000325; C:plant-type vacuole; IDA:UniProtKB.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009821; P:alkaloid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0042179; P:nicotine biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
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   2: Evidence at transcript level;
KW   Alkaloid metabolism; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW   Oxidoreductase; Reference proteome; Signal; Vacuole.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..568
FT                   /note="Berberine bridge enzyme-like B"
FT                   /id="PRO_5015086581"
FT   DOMAIN          73..249
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         110
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FI21"
FT   CARBOHYD        41
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        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        33..95
FT                   /evidence="ECO:0000250|UniProtKB:O64743"
SQ   SEQUENCE   568 AA;  63159 MW;  08F26F448DBBFD31 CRC64;
     MFPLIILISF SLTSLSATAT SGAGGGVANL YTCLIDHNVH NFSIYPTKND QSSSNYFNLL
     DFSLQNLRFA ASYMPKPTVI ILPNSKEELV STILCCRQAS YEIRVRCGGH SYEGTSYVSF
     DGSPFVIVDL MKLDEVSVDL DSETAWAQGG ATIGQIYYAI AKVSDVHAFS AGSGPTVGSG
     GHISGGGFGL LSRKFGLAAD NVVDALLIDA DGRLLDRKAM GEDVFWAIRG GGGGNWGIIY
     AWKIRLLKVP KIVTTCMIYR PGSKQYVAQL LQKWQIVTPN LVDDFTLGVL LRPADLPADM
     KYGNSTPIEI FPQFNALYLG PKTEVLSISN EEFPELGVKN DECKEMTWIE SALFFSELAD
     INGNSSNDIS RLKERYMDGK GFFKGKTDYV KKPVSMDGML TFLVELEKNP KGYLVFDPYG
     GAMDKIDDQA IAFPHRKGNL FAIQYLAQWN EEDDYKSDVY MEWIRGFYNT MTPFVSSSPR
     GAYINYLDMD LGVNMDDDYL LRNASSRNSS SSVDAVERAR AWGEMYFLHN YDRLVKAKTQ
     IDPLNVFRHE QSIPPMLGST QEHKYSSE
 
 
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