BOA8_BOTFB
ID BOA8_BOTFB Reviewed; 779 AA.
AC G0LET6;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=FAD-dependent monooxygenase BOA8 {ECO:0000303|PubMed:21722295};
DE EC=1.-.-.- {ECO:0000305|PubMed:21722295};
DE AltName: Full=Botcinic acid biosynthesis cluster B protein 8 {ECO:0000303|PubMed:21722295};
GN Name=BOA8 {ECO:0000303|PubMed:21722295};
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND PATHWAY.
RC STRAIN=B05.10;
RX PubMed=21722295; DOI=10.1111/j.1364-3703.2010.00692.x;
RA Dalmais B., Schumacher J., Moraga J., Le Pecheur P., Tudzynski B.,
RA Collado I.G., Viaud M.;
RT "The Botrytis cinerea phytotoxin botcinic acid requires two polyketide
RT synthases for production and has a redundant role in virulence with
RT botrydial.";
RL Mol. Plant Pathol. 12:564-579(2011).
RN [2]
RP FUNCTION.
RX PubMed=23203902; DOI=10.1002/cbic.201200487;
RA Massaroli M., Moraga J., Bastos Borges K., Ramirez-Fernandez J., Viaud M.,
RA Gonzalez Collado I., Duran-Patron R., Hernandez-Galan R.;
RT "A shared biosynthetic pathway for botcinins and botrylactones revealed
RT through gene deletions.";
RL ChemBioChem 14:132-136(2013).
CC -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster B that
CC mediates the biosynthesis of botcinic acid and its botcinin
CC derivatives, acetate-derived polyketides that contribute to virulence
CC when combined with the sesquiterpene botrydial (PubMed:21722295).
CC Botcinic acid and its derivatives have been shown to induce chlorosis
CC and necrosis during host plant infection, but also have antifungal
CC activities (PubMed:21722295). Two polyketide synthases, BOA6 and BOA9,
CC are involved in the biosynthesis of botcinins. BOA6 mediates the
CC formation of the per-methylated tetraketide core by condensation of
CC four units of malonyl-CoA with one unit of acetyl-CoA, which would be
CC methylated in activated methylene groups to yield a bicyclic acid
CC intermediate that could then either be converted to botrylactone
CC derivatives or lose the starter acetate unit through a retro-Claisen
CC type C-C bond cleavage to yield botcinin derivatives (PubMed:23203902).
CC The second polyketide synthase, BOA9, is probably required for the
CC biosynthesis of the tetraketide side chain of botcinins (Probable). The
CC methyltransferase (MT) domain within BOA6 is probably responsible for
CC the incorporation of four methyl groups (Probable). The trans-enoyl
CC reductase BOA5 might take over the enoyl reductase function of BOA6
CC that misses an ER domain (Probable). The monooxygenases BOA2, BOA3 and
CC BOA4 might be involved in further hydroxylations at C4, C5 and C8,
CC whereas BOA7, close to BOA9, could potentially be involved in the
CC hydroxylation at C4 in the side chain of botcinins (Probable).
CC {ECO:0000269|PubMed:21722295, ECO:0000269|PubMed:23203902,
CC ECO:0000305|PubMed:23203902}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:21722295}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression of the botcinic acid clusters genes BOA1-13 and
CC BOA17 is coregulated by BCG1 during both in vitro and in planta growth.
CC {ECO:0000269|PubMed:21722295}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; FR718877; CBX87031.1; -; Genomic_DNA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..779
FT /note="FAD-dependent monooxygenase BOA8"
FT /id="PRO_0000444655"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..685
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 742..762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 54..55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 331
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 341..345
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 779 AA; 87626 MW; C7242137B336C67D CRC64;
MFNSTMDIDP HLRVRERMNQ RKQSRSIYHS INDKKKTISR PNPSINIAIM TQTSQMKVVI
VGGSIAGLTL AHCLSRYGID YIILERRHDI APQVGASTWD ENGRLLSETD APILTGKRLG
YTITFLERET LLEILYRHLP DKSKVLTGKY VRSIEQDSKE AVVICEDGSR YSGDVIAGAD
GIHSTIRSEM RRQIAKEGTT KDLEALKRDE IALSAEYSCL FGISKPIPGL EIGHTHRSSG
KGASTLLFGG VDGKLYWFLF TKNEERTFGD GIPRYKKGDE TNHVAKYMHH HVSGNILLSE
VWKNRIVANF VTIEEMENEH WNWNRVACLG DSIHKMTPNL GQGANCAIES AAEMANSLAK
ALRDDGSKPA IEDINSALSL YHQKRNVRAN LIVKAANKFT RVEALATTGD WVASMFIIPR
LGDILADRGA KVQVGATKLD CLPMPKRALE GTMPWSTNSG IGKEENRKRR AQLALPLILI
ALWFFWKKTP EPKGFPVTKT FSEVKLDMLS SIANAIPFAT IWTIESYRRG NALTVANIFP
TAFLLLAQKL GIELVAPIYF FFHYVQSPQE NFAALDNRLT NIAFAKILPL AILSIFLGPS
YCIWSSIELE SAQWIYDNAW YWYPVYLTMF LRILKFIVKD TTRLNRIYKP TADLSYLRIS
YSISILICAA FYLYGSLSSS TSIAFLTQEL QPPIQPIQAI LGAFSELWAA KQTSLYGAAF
YWTFLHFADL KFVGKSKQSW LLILTIXLSS TFLAGPGVGL IVMWAWREEI MAKKHVVPE
