BOA2_BOTFB
ID BOA2_BOTFB Reviewed; 529 AA.
AC B1GVX4;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=FAD-binding monooxygenase BOA2 {ECO:0000303|PubMed:21722295};
DE EC=1.14.13.- {ECO:0000305|PubMed:21722295};
DE AltName: Full=Botcinic acid biosynthesis cluster A protein 2 {ECO:0000303|PubMed:21722295};
GN Name=BOA2 {ECO:0000303|PubMed:21722295};
GN Synonyms=MO1 {ECO:0000303|PubMed:18208491};
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], AND INDUCTION.
RC STRAIN=B05.10;
RX PubMed=18208491; DOI=10.1111/j.1365-2958.2008.06105.x;
RA Schumacher J., Viaud M., Simon A., Tudzynski B.;
RT "The Galpha subunit BCG1, the phospholipase C (BcPLC1) and the calcineurin
RT phosphatase co-ordinately regulate gene expression in the grey mould fungus
RT Botrytis cinerea.";
RL Mol. Microbiol. 67:1027-1050(2008).
RN [2]
RP FUNCTION, INDUCTION, AND PATHWAY.
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 [3]
RP FUNCTION, AND PATHWAY.
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-binding monooxygenase; part of the gene cluster A 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:18208491,
CC PubMed:21722295). Botcinic acid and its derivatives have been shown to
CC induce chlorosis and necrosis during host plant infection, but also
CC have antifungal activities (PubMed:18208491, PubMed:21722295). Two
CC polyketide synthases, BOA6 and BOA9, are involved in the biosynthesis
CC of botcinins. BOA6 mediates the formation of the per-methylated
CC tetraketide core by condensation of four units of malonyl-CoA with one
CC unit of acetyl-CoA, which would be methylated in activated methylene
CC groups to yield a bicyclic acid intermediate that could then either be
CC converted to botrylactone derivatives or lose the starter acetate unit
CC through a retro-Claisen type C-C bond cleavage to yield botcinin
CC derivatives (PubMed:23203902). The second polyketide synthase, BOA9, is
CC probably required for the biosynthesis of the tetraketide side chain of
CC botcinins (Probable). The methyltransferase (MT) domain within BOA6 is
CC probably responsible for the incorporation of four methyl groups
CC (Probable). The trans-enoyl reductase BOA5 might take over the enoyl
CC reductase function of BOA6 that misses an ER domain (Probable). The
CC monooxygenases BOA2, BOA3 and BOA4 might be involved in further
CC hydroxylations at C4, C5 and C8, whereas BOA7, close to BOA9, could
CC potentially be involved in the hydroxylation at C4 in the side chain of
CC botcinins (Probable). {ECO:0000269|PubMed:18208491,
CC ECO:0000269|PubMed:21722295, ECO:0000269|PubMed:23203902,
CC ECO:0000305|PubMed:23203902}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:H3JQW0};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:H3JQW0};
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:21722295,
CC ECO:0000305|PubMed:23203902}.
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:18208491, ECO:0000269|PubMed:21722295}.
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AM930229; CAP58783.1; -; Genomic_DNA.
DR AlphaFoldDB; B1GVX4; -.
DR SMR; B1GVX4; -.
DR VEuPathDB; FungiDB:Bcin01g00020; -.
DR PHI-base; PHI:2289; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Virulence.
FT CHAIN 1..529
FT /note="FAD-binding monooxygenase BOA2"
FT /id="PRO_0000444658"
FT BINDING 58..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 68..70
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 70..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 198..204
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 221..222
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
SQ SEQUENCE 529 AA; 61060 MW; FBC694BFAE7945B5 CRC64;
MSSEKMPIET LQADEHRFAI ILGAGAAGII QGCTFIREKT LPLEEFQILE RQSAFGGVWW
KNTYPGAACD IPSHEYQISF ALNPYWSRTF APQPEIQKYF EDVALQYELH KSTTFNTEIV
EAKWDDSRLL WLVETTDLTT GDTKLWSCHV LIGALGAFTV PKKAPVKNVD AFKGEEWHSV
DWPKNANLKG KTVAVIGTGP SACQFIPNIY PEVKSLIVYQ RSPGHVLPRN DVVVGSLTKW
MFAHIPFLMR FNRWFWMKKD EILRPRLFTV GSWLQKIVIS MTRNHLYKQI KDDTLRRKLE
SKDVFGCKRP LMLSDYYPIF NNDNVELVTD SVTELTENGI KSRNTDTGEE MERETDVLIW
GTGYNPVDFG LPVPTKGRSG QLLCDKYQPE LFSLYGVAVD DFPNYFNFLG PNSSSFETSV
MELFELQAHH NSIATEYLFQ KNVGTFRYAI MPKEERVRSW TLSLRPGQAK LPPANPNCKS
YYRSKIGHVY RYPYPYWQYK ALIAKLDFKR DWVLLQQRIG QKEVKVLEF
