ID   BOA11_BOTFB             Reviewed;         470 AA.
AC   A6SSW1;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Acyltransferase BOA11 {ECO:0000303|PubMed:21722295};
DE            EC=2.3.1.- {ECO:0000305|PubMed:21722295};
DE   AltName: Full=Botcinic acid biosynthesis cluster B protein 11 {ECO:0000303|PubMed:21722295};
GN   Name=BOA11 {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: Acyltransferase; part of the gene cluster B that mediates the
CC       biosynthesis of botcinic acid and its botcinin derivatives, acetate-
CC       derived polyketides that contribute to virulence when combined with the
CC       sesquiterpene botrydial (PubMed:21722295). Botcinic acid and its
CC       derivatives have been shown to induce chlorosis and necrosis during
CC       host plant infection, but also have antifungal activities
CC       (PubMed:21722295). Two polyketide synthases, BOA6 and BOA9, are
CC       involved in the biosynthesis of botcinins. BOA6 mediates the formation
CC       of the per-methylated tetraketide core by condensation of four units of
CC       malonyl-CoA with one unit of acetyl-CoA, which would be methylated in
CC       activated methylene groups to yield a bicyclic acid intermediate that
CC       could then either be converted to botrylactone derivatives or lose the
CC       starter acetate unit through a retro-Claisen type C-C bond cleavage to
CC       yield botcinin derivatives (PubMed:23203902). The second polyketide
CC       synthase, BOA9, is probably required for the biosynthesis of the
CC       tetraketide side chain of botcinins (Probable). The methyltransferase
CC       (MT) domain within BOA6 is probably responsible for the incorporation
CC       of four methyl groups (Probable). The trans-enoyl reductase BOA5 might
CC       take over the enoyl reductase function of BOA6 that misses an ER domain
CC       (Probable). The monooxygenases BOA2, BOA3 and BOA4 might be involved in
CC       further hydroxylations at C4, C5 and C8, whereas BOA7, close to BOA9,
CC       could potentially be involved in the hydroxylation at C4 in the side
CC       chain of botcinins (Probable). {ECO:0000269|PubMed:21722295,
CC       ECO:0000269|PubMed:23203902, 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 plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; FR718882; CBX87036.1; -; Genomic_DNA.
DR   RefSeq; XP_001545614.1; XM_001545564.1.
DR   AlphaFoldDB; A6SSW1; -.
DR   SMR; A6SSW1; -.
DR   GeneID; 5426076; -.
DR   KEGG; bfu:BCIN_01g00110; -.
DR   OMA; GRPEFIR; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Transferase; Virulence.
FT   CHAIN           1..470
FT                   /note="Acyltransferase BOA11"
FT                   /id="PRO_0000444647"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ   SEQUENCE   470 AA;  52718 MW;  F5AB4CF656520C02 CRC64;
     MASATKTLIT ELTPLDHLMP RTYVIGMNYI WPISRRSNIE DIHKHLKRGL EQTIKEIPFL
     GGSVVPTGSP GKFCIETLPG DFEGNQLIFN DLRTGSGNSW PNSYKNVRKA RFPSTLFTDD
     CLSPVKGYMT RERLPVIAAQ ANFIDGGLIL HLSVLHTACD VLAWNNILSI LSKNVKASWP
     TEAEVSLNDD LQDYKVLPSF LDRSPLMRGN LNVERMDVRE YKLQLANSKL EDPRNHLINP
     PPKSITEMEN ALFCISNSKL GELRDSISAE GSATSWLTVN DALAALMWCC VNRARISNGS
     QKLLRGNLSV AYDGRTVLDP PLPKRFMGNS ALGFPITLDI HPKSVFEAAL AISESRNDFN
     DKHIRDIIGF LDGLGDITQE RVSYAKTLNP ILVISNLKDM GFYEQDWGGS LGFPDALRMA
     NPFLDYIPRV VPMPAQRNGN VYLIVWIEKS AAKRLREDET WNKWITPVFE