BBLD1_TOBAC
ID BBLD1_TOBAC Reviewed; 567 AA.
AC A0A1S3YTK9; F1T162;
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-1 {ECO:0000303|PubMed:21343426};
DE Short=NtBBLd {ECO:0000303|PubMed:21343426};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE Flags: Precursor;
GN Name=BBLD {ECO:0000303|PubMed:21343426};
GN ORFNames=LOC107779537 {ECO:0000312|RefSeq:XP_016455473.1};
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], TISSUE SPECIFICITY, AND INDUCTION BY JASMONIC
RP 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 [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 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 [4]
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 -!- TISSUE SPECIFICITY: Mostly expressed in roots at low levels.
CC {ECO:0000269|PubMed:21343426}.
CC -!- INDUCTION: By jasmonic acid (MeJA). {ECO:0000269|PubMed:21343426}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB604221; BAK18781.1; -; mRNA.
DR RefSeq; XP_016455473.1; XM_016599987.1.
DR SMR; A0A1S3YTK9; -.
DR STRING; 4097.A0A1S3YTK9; -.
DR GeneID; 107779537; -.
DR KEGG; nta:107779537; -.
DR OMA; EACKEMS; -.
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 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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..567
FT /note="Berberine bridge enzyme-like D-1"
FT /id="PRO_0000455772"
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 DISULFID 42..103
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CONFLICT 360
FT /note="D -> N (in Ref. 1; BAK18781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 63010 MW; 3DAEDC11601FE612 CRC64;
MKRNISMFLQ LLLIILMMIS FLFTSLLVPS VSATTLNTIS TCLINYKVSN FSVYPTRNHA
GNSYYNLLDF SIQNLRFAAC SKPKPTVIIV PESKEQLVSS VLCCRQGSYE IRVRCGGHSY
EGTSSVSFDG SPFVVIDLMK LDGVSVDVDS ETAWVQGGAT LGQTYYAISR ASNVHGFSAG
SCPTVGVGGH ISGGGYGFLS RKYGLAADNV VDALLVDAEG RLLDRKAMGE EIFWAIRGGG
GGIWGIIYAW KIRLLKVPKT VTSFIIPRPG SKRYVSQLVH KWQLVAPKLE DEFYLSISMS
SPSKGNIPIE INAQFSGFYL GTKTEAISIL NEAFSELGVL EGDCKEMSWI ESTLFFSELD
DVANSSDVSR LKERYFENKS YFKAKSDYVK TPISVGGIMT ALNVLEKEPN GHVILDPYGG
AMQRISEEAI AFPHRKGNLF GIQYLVVWKE KDNNNIVKSN IGYIEWIREF YNTMAPHVSS
SPRAAYVNYM DLDLGVMDDY LLPCTSTTAS ANHAVERARV WGEKYFLNNY DRLVKAKTKI
DPLNVFRHQQ GIPPLFASMQ EYTYSSK
