BOA5_BOTFB
ID BOA5_BOTFB Reviewed; 375 AA.
AC B1GVX6;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Trans-enoyl reductase BOA5 {ECO:0000303|PubMed:21722295};
DE EC=1.-.-.- {ECO:0000305|PubMed:21722295};
DE AltName: Full=Botcinic acid biosynthesis cluster A protein 5 {ECO:0000303|PubMed:21722295};
GN Name=BOA5 {ECO:0000303|PubMed:21722295};
GN Synonyms=OxR {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, DOMAIN, 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.
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: Trans-enoyl reductase; 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 -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:21722295}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
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 -!- DOMAIN: BOA5 is composed of an enoyl reductase (ER) domain and
CC presumably acts in concert with the polyketide synthase BOA6 that
CC misses an ER domain. {ECO:0000305|PubMed:21722295}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AM930231; CAP58785.1; -; Genomic_DNA.
DR AlphaFoldDB; B1GVX6; -.
DR SMR; B1GVX6; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NADP; Nucleotide-binding; Oxidoreductase; Virulence.
FT CHAIN 1..375
FT /note="Trans-enoyl reductase BOA5"
FT /id="PRO_0000444656"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 121..128
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 185..188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 208..211
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 226
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 273..274
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 294..298
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 363..364
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 375 AA; 39899 MW; DDE23595BA656FB3 CRC64;
MQAVIQTGPG TLQLTENVPK PSVEPGSRKV LVKVHAVALN HSDWKMVDFS AKPGAISGYD
MAGVLEAIDD SMNSDLAVGD RVLGVTSIHG GAFAEYVVTD GDLLVKIPEN MDFQHAASYG
VGIVTTGLAL YGNECLALNW PNTDGTGSAA PQKTRVGPRG WSGGDALTDN DNETPRIPVL
VYGASTSTGT LAIQLLKLSG YEPIAVCSPH NFGLVQSRGA SKCFDYHSQG CGAMIKQYTY
NRLEYALDCI TTASSMRLCY EAIGATGGKY VSLDPFNARV QRSRADVKPF FCYALTIFGL
PIELSGEFAR GAKPEDRKLA EKFVKIAEKL IEKGRLKAHP TMLKSGGLGG IASSIDLLRK
GKVSGSKLVF DVVGN
