ID   BOA16_BOTFB             Reviewed;         158 AA.
AC   G0LEU4;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Botcinic acid biosynthesis cluster B protein 16 {ECO:0000303|PubMed:21722295};
GN   Name=BOA16 {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, 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: Part of the gene cluster B that mediates the biosynthesis of
CC       botcinic acid and its botcinin derivatives, acetate-derived polyketides
CC       that contribute to virulence when combined with the sesquiterpene
CC       botrydial (PubMed:21722295). Botcinic acid and its derivatives have
CC       been shown to induce chlorosis and necrosis during host plant
CC       infection, but also have antifungal activities (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:21722295,
CC       ECO:0000269|PubMed:23203902, ECO:0000305|PubMed:23203902}.
CC   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:21722295}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FR718885; CBX87039.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0LEU4; -.
PE   4: Predicted;
KW   Virulence.
FT   CHAIN           1..158
FT                   /note="Botcinic acid biosynthesis cluster B protein 16"
FT                   /id="PRO_0000444652"
SQ   SEQUENCE   158 AA;  16833 MW;  B6975549EC2C921E CRC64;
     MALEAAKALQ QLRTGDLNAF NFVYISGEGA TSNPGPFTPL FGRVKGETET GLMKIQSKVA
     NFRLFIVRPS HVDSKGHKAI APYIPQPTVL LRAANLALGP ALRGFLKPYN SPTAPLGEFL
     VDLATGAQQG RLHGDGVECR GASTIISNVG FRRLMGLS