BOA17_BOTFB
ID BOA17_BOTFB Reviewed; 274 AA.
AC A6SSW9;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Oxidoreductase BOA17 {ECO:0000303|PubMed:21722295};
DE EC=1.-.-.- {ECO:0000305|PubMed:21722295};
DE AltName: Full=Botcinic acid biosynthesis cluster B protein 17 {ECO:0000303|PubMed:21722295};
GN Name=BOA17 {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: Oxidoreductase; 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 short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; FR718886; CBX87040.1; -; Genomic_DNA.
DR RefSeq; XP_001545622.1; XM_001545572.1.
DR AlphaFoldDB; A6SSW9; -.
DR SMR; A6SSW9; -.
DR GeneID; 5426072; -.
DR KEGG; bfu:BCIN_01g00160; -.
DR VEuPathDB; FungiDB:Bcin01g00160; -.
DR OMA; MAVTSMG; -.
DR OrthoDB; 1166094at2759; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NAD; NADP; Oxidoreductase; Virulence.
FT CHAIN 1..274
FT /note="Oxidoreductase BOA17"
FT /id="PRO_0000444654"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 6..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 33..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 56..58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 149..153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 182..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 274 AA; 28929 MW; C1E75B88FEA6F84D CRC64;
MTKIWFITGS SRGLGLAIAE AALNNGDSVI ATARKPEQLT NLVNKFGKER VFPVALDVTD
NNQVLQAVKS GHEKFGRIDV VINNAGYANT AAVEDIDVDD FCAQVEANLM GVVYVSKAVL
PILRQQKSGH IFQVSSLGGR IGAPGLSAYQ SAKWAVGGFS TVLAQEVASF GIKITVLEPG
GIRTDWAGSS MQVPTVSEPY QATVGAFAES LRKSSGSEVS IPSKIANIVL KVLGEKEPPL
RLLVGPDAVE YAGKAAEVLS ASDEKWRELS LASA
