ID   BOA1_BOTFB              Reviewed;         300 AA.
AC   B1GVX5;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Oxidoreductase BOA1 {ECO:0000303|PubMed:21722295};
DE            EC=1.3.1.- {ECO:0000305|PubMed:21722295};
DE   AltName: Full=Botcinic acid biosynthesis cluster A protein 1 {ECO:0000303|PubMed:21722295};
GN   Name=BOA1 {ECO:0000303|PubMed:21722295};
GN   Synonyms=ORF1 {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, 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: Oxidoreductase; part of the gene cluster A 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:18208491, PubMed:21722295). Botcinic
CC       acid and its derivatives have been shown to induce chlorosis and
CC       necrosis during host plant infection, but also have antifungal
CC       activities (PubMed:18208491, PubMed:21722295). Two polyketide
CC       synthases, BOA6 and BOA9, are involved in the biosynthesis of
CC       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   -!- INDUCTION: Expression of the botcinic acid clusters genes is
CC       coregulated by BCG1 during both in vitro and in planta growth.
CC       {ECO:0000269|PubMed:18208491, ECO:0000269|PubMed:21722295}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; AM930230; CAP58784.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1GVX5; -.
DR   SMR; B1GVX5; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Virulence.
FT   CHAIN           1..300
FT                   /note="Oxidoreductase BOA1"
FT                   /id="PRO_0000444657"
SQ   SEQUENCE   300 AA;  32775 MW;  A90B9CC207E1571A CRC64;
     MVRVAVAGGT GGVGYAIVDA LKAQTEHEFI VLSRTESPEY AAKNNVKVVS IDYSDVSQIS
     KILDEHHIHT VISALCIVSK EHSDSQLNLV RGAAGSQSVK RFVPSEYGSA YEEKHALARP
     STGLKAVAVK ELAKTHLEYT SFVNGLFLDY LCMPTVPSHL AAGIRFFDIP SRTSVGIGSG
     TVPLVMTHTR DVGRFVVASL SLPKWENRSF IVGDRQSWHD VINIAGKITG EKWPSLRPSK
     SSGSHEPAHR AAYSASLKEH GDWFESGTFS STLSSGSVYL NELFPEIIPS YGRRWPQDFD