ID   BOA10_BOTFB             Reviewed;         270 AA.
AC   G0LET9;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Probable thioesterase BOA10 {ECO:0000303|PubMed:21722295};
DE            EC=3.1.-.- {ECO:0000305|PubMed:21722295};
DE   AltName: Full=Botcinic acid biosynthesis cluster B protein 10 {ECO:0000303|PubMed:21722295};
GN   Name=BOA10 {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: Probable thioesterase; 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   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:21722295}.
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 AMT4 thioesterase family. {ECO:0000305}.
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DR   EMBL; FR718880; CBX87034.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0LET9; -.
DR   SMR; G0LET9; -.
DR   VEuPathDB; FungiDB:Bcin01g00100; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Virulence.
FT   CHAIN           1..270
FT                   /note="Probable thioesterase BOA10"
FT                   /id="PRO_0000444648"
SQ   SEQUENCE   270 AA;  30265 MW;  DFCE5E473AE24E6A CRC64;
     MENPVLIQKA PRRYKSAIPL FLFHDGGGTV LPYYFLESLN RNVWGVSYPH LNDGGTFEHG
     IKGMGELYAG YIRGKVSRGK VLLGGWSAGG SIAIQVAKCL ENIPELCVAG IILLDTPFPD
     FPDWRPKNSP PVQFHIPVVP DQTAKSRLAQ QQAVNDIIHA LSVWELPTWE NGRRPPPAVF
     IRALKVVPTE KVVEVDWFRE EYALGWQKYP YNFIVEELRV DGDHFSIFTP SYLPELSTKL
     REALDLLDSK PETGILLDSK LNSSIVISAL