BOA11_BOTFB
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