BOA7_BOTFB
ID BOA7_BOTFB Reviewed; 535 AA.
AC G0LET5;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Cytochrome P450 monooxygenase BOA7 {ECO:0000303|PubMed:21722295};
DE EC=1.-.-.- {ECO:0000305|PubMed:21722295};
DE AltName: Full=Botcinic acid biosynthesis cluster B protein 7 {ECO:0000303|PubMed:21722295};
GN Name=BOA7 {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, AND PATHWAY.
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: Cytochrome P450 monooxygenase; part of the gene cluster B
CC that 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:21722295).
CC Botcinic acid and its derivatives have been shown to induce chlorosis
CC and necrosis during host plant infection, but also have antifungal
CC activities (PubMed:21722295). Two polyketide synthases, BOA6 and BOA9,
CC are involved in the biosynthesis of botcinins. BOA6 mediates the
CC formation of the per-methylated tetraketide core by condensation of
CC four units of malonyl-CoA with one unit of acetyl-CoA, which would be
CC methylated in activated methylene groups to yield a bicyclic acid
CC intermediate that could then either be converted to botrylactone
CC derivatives or lose the starter acetate unit through a retro-Claisen
CC type C-C bond cleavage to yield botcinin derivatives (PubMed:23203902).
CC The second polyketide synthase, BOA9, is probably required for the
CC biosynthesis of the tetraketide side chain of botcinins (Probable). The
CC methyltransferase (MT) domain within BOA6 is probably responsible for
CC the incorporation of four methyl groups (Probable). The trans-enoyl
CC reductase BOA5 might take over the enoyl reductase function of BOA6
CC that misses an ER domain (Probable). The monooxygenases BOA2, BOA3 and
CC BOA4 might be involved in further hydroxylations at C4, C5 and C8,
CC whereas BOA7, close to BOA9, could potentially be involved in the
CC hydroxylation at C4 in the side chain of botcinins (Probable).
CC {ECO:0000269|PubMed:21722295, ECO:0000269|PubMed:23203902,
CC ECO:0000305|PubMed:23203902}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:21722295,
CC ECO:0000305|PubMed:23203902}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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 cytochrome P450 family. {ECO:0000305}.
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DR EMBL; FR717895; CBX55165.1; -; Genomic_DNA.
DR AlphaFoldDB; G0LET5; -.
DR SMR; G0LET5; -.
DR VEuPathDB; FungiDB:Bcin01g00070; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..535
FT /note="Cytochrome P450 monooxygenase BOA7"
FT /id="PRO_0000444641"
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 478
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 535 AA; 60666 MW; 37E6C15C38083B59 CRC64;
MYQRLKEINF RKPLELEWNS IFLILGFFVL AAILIAWTQR PDEELLLERL KDLDLPIVGV
GPNINVSESL EIGTQTYPNS PYVVPADRVP IVILPNSAIN IIKSLPEAKI SFEKEVYARH
LAHLLLKKDQ KIFSEPILNS IKQDLTRNIS KTLDTLWDEV DYAFEKNIGT LPDDDDGWKN
VSVYGKVLNV VALLSGRVFV GAPLCRDEEW IKATIAYTII LGVTVGMLWK RPWWQRKILA
PLYFRTLVGV HKKAEELLKP LLEREAALDP SEWEKKAGEQ NDGQLIRWLL SHTPQKGGKI
DVKQLAHDQL TVSLAAIHTT SITISHLLYD LATYPEHVAP LRTELESVIA DHKTAGGNGK
LSKVELTKLW KMDSFIKESQ RLNPPILVQM RRYLTSPLAL PSGHILPSGT FCGVDAQMTN
RTVPYYEASP ITHQQTPFDT FDGFRFSKLR SVPGNENRYQ FVTSSTESLN FGHGTHACPG
RFFASNEIKI AFAEVLLKWD VRLKPGEGRP ANLYTDTNVM PNMKGEVQMR RRELI
