BOA6_BOTFB
ID BOA6_BOTFB Reviewed; 2460 AA.
AC B1GVX7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Reducing polyketide synthase BOA6 {ECO:0000303|PubMed:21722295};
DE EC=2.3.1.- {ECO:0000305|PubMed:21722295};
DE AltName: Full=Botcinic acid biosynthesis cluster A protein 6 {ECO:0000303|PubMed:21722295};
DE AltName: Full=Polyketide synthase 6 {ECO:0000303|PubMed:18208491};
DE Short=PKS6 {ECO:0000303|PubMed:18208491};
GN Name=BOA6 {ECO:0000303|PubMed:21722295};
GN Synonyms=PKS6 {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, DISRUPTION PHENOTYPE, 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, DOMAIN, 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: Reducing polyketide synthase; 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:0000269|PubMed:21722295,
CC ECO:0000269|PubMed:23203902}.
CC -!- INDUCTION: Expression is up-regulated during tomato leaf infection
CC (PubMed:21722295). Expression of the botcinic acid clusters genes BOA1-
CC 13 and BOA17 is coregulated by BCG1 during both in vitro and in planta
CC growth (PubMed:18208491, PubMed:21722295).
CC {ECO:0000269|PubMed:18208491, ECO:0000269|PubMed:21722295}.
CC -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC that reduces hydroxyl groups to enoyl groups; a methyltransferase (MT)
CC domain responsible for the incorporation of methyl groups; a
CC ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC an acyl-carrier protein (ACP) that serves as the tether of the growing
CC and completed polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:21722295, ECO:0000305|PubMed:23203902}.
CC -!- DISRUPTION PHENOTYPE: Abolishes botcinic acid and botcinin production.
CC Exhibits markedly reduced virulence when the synthesis of botrydoal is
CC also blocked. {ECO:0000269|PubMed:21722295}.
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DR EMBL; AM930232; CAP58786.1; -; Genomic_DNA.
DR AlphaFoldDB; B1GVX7; -.
DR SMR; B1GVX7; -.
DR PHI-base; PHI:2290; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Multifunctional enzyme; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Transferase; Virulence.
FT CHAIN 1..2460
FT /note="Reducing polyketide synthase BOA6"
FT /id="PRO_0000444645"
FT DOMAIN 2378..2456
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:21722295"
FT REGION 8..441
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT REGION 549..864
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT REGION 938..1244
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT REGION 1399..1586
FT /note="Methyltransferase (MT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT REGION 2098..2266
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT MOD_RES 2416
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2460 AA; 268877 MW; 64F7C27629B27C7C CRC64;
MVVPNEPIAV IGTGCRFPGG ASSPSKLWNL LHHPYDLTQK VPSSRFNIKA FYHPNGEHHG
TTNATKSYFL NEDPTTFDAP FFNINPREAE ALDPQQRLLL ETVYEALEAA GLSIEEMQGT
STAVYVGLMC ADYFDVLMRD IEDIPQYLAT GTARSIMSNR ISYFFDWKGP SMTIDTACSS
SLVAVHNAIS TLRSGQSRTA IAAGANLIFG PEMYIGESNL HMLSPTGRSQ MWDSRADGYA
RGEGTAAIVL KTLKNALEDG DDIEYIIRET GVNSDGKSKG ITMPLAASQA DLIRQTYARA
GLDCTKPSER CQYFEAHGTG TPAGDPVEAE AISSAFFPQR SDILNSEPLH VGSIKTVIGH
LEGAAGLAGI IKAGLALKEK TIPPNLHFQS LNSAIEPFYG NLNVPTAPLP WPAVEGPLRA
SVNSFGFGGT NAHAILESYE VCTPTPSLES TALIPFTISA ISEDCLIQNI TNFSDYIEEH
EGVNLIDLGY SLLGRSNFPT KATFVASNTE DLLDQLEKVI IAKEENPNLA IGIRSTNVND
KSSRKILGVF TGQGAQWPAM GKMLIANIPS FSQTIDSLEK SLRELPDAPK WSLKDEIVAS
VGKSSIEKAE FSQPLCTALQ IALVDLLKLI GVTFSAVVGH SSGEIGAAYA AGRLTAGDAI
RIAYYRGLHA HLAKGKGGEE GSMMAAGLSF DEALEFCAGE EYQGKISIAA SNAPKTVTLS
GNKDAIEKAK STLDDRGVFA RVLKVDTAYH SDHMLPCSEP YTRSLAACKI SPKPSLLDCT
WISSVHLKNM SSESSELETK YWVDNLVSPV RFFEAVSIAA KEFGSFDAAV EVGPHPALKG
PVAQTFKHAV NAVVPYTGVL SRGDNDSIAF ANALGFLLNY INGKRISFKK YLDAISGGVV
TTPKLLKGLP TYSWDHSRTF WFESRISRNY RNRVDPPHEL LGVRCADDTD MEYRWRNIFK
LDELPWVSGH KFQRQTLVPA AFYCSMALES SKVLANGKPI RLVELHQVDI ERAINLEENN
AAVEVMFALK PRSSSASGSD EIVCADFWCT AAPSGKPMSM IFSGRIKMTL GTPSPDAMSI
RSPVRPVLGP LNVDRFYDSL ANVGLEFTGI FRGIEKGQRR MHISSLEGRR CLSDTGLLVH
PAFLDMTLHA TLAAFASPGD ERFWTPYLPR RIAKMSFNIA LCEAAFEKET ALAGMDGYIT
EVTPTTANDA ATYVGDVDVF DPLTNEIEIQ IEGLQMQSFT AARPSQDRQL YLETLWAADI
SGGIISEVDI EDDDPKALHL IDLGERLSYA YMRHLMSEIK PENIPDHHRP LFNWINHVTD
LVSKGTHPSI KPEWNNDDLQ ELITMASIYP ECVDLELMQA VGNNLPDVVR GTTTMLEHML
PNGLLDRLYT EGIGMATSNK FVTAAMKKIG HRYPKMRVLE IGAGTGGATK GIFTGIGDAF
AHYTFTDIST GFFMKAREVF SDYANRMTFS LLNCEKDPLE QGYEAHSFDV IVASNVLHAT
EFLEKTMRNV RTLLKPGGYL CLLECTGHLE RTGFLMAGLP GWWLGGADGR PYRPTISPPE
WDSVLKKTGF SGVDAIVNDF KDKSRYTVSV ILSQALDDDV QKLREPLQYH PESTGKDLIV
IGGSSIATQL LVETIKQDIP SWETRKTIVL ATWEEASKLT IPFGTTILSV ADLDEPIFKS
MNAERLKGIQ TVINSAESVL WVTTGCKADE PYANMAIGLG RSIISEMPHL NLQFLDVDLK
GNAAKVIGET LVRLEVATGL LDSRKENLLW SIEPEMIYEN GQLYLPRVKP IKKLNDVLNS
TRRVITEEVL LASKKVTITP PTVGNRFNLE VQEVVMDHLD SENELEISVS FSSLYTVNID
GNFLYIILGK TKSGSSILAL SASNQSLITV PKDWAIPASQ ATPEYLECAM AYLLAKQILN
KGSSSVLLHE PSFALSQAVE SIAKADGKSI SNIASTKSTT SIQNCIKVHP TLSKRAIRDL
LPASIQSFVD ISGTGKHVKD ALTKLTSIIE IDGFLGVTPA KSSSSVDPST VLADVVAYAD
STKTKDIEGR FLLNAGSLKH GHVSSFSPLS VVDWTSNTTL TVDVKPFSQN QIFDKNKSYL
LAGLTGDLGQ SICRWMVEAG ARYIIIGSRS VKSGTPWQQE LQRMGATVLV YTIDFTDKEA
VTRLREEAIK TMPPIAGVMN GCMVLDDKPF SDMPFETLER VIRPKVLSTI NIDAVFGLEL
DFFVLFSSLA AVNGIPGQSN YAAANMYMAS LAEQRRKRGG VASVIHIGMI LGVGYVERSG
RFTESALRSY NYLTIPEHEF LQVLSEAVQS GHPASNRCPE IIIGMVAPLT GEERDKPRWH
ANPRFAFVMN DFTNEESDSQ GEVEVPTKEQ LAKAQTKDEV LGVMQKCFAK QLELILQADS
GSIDESAPLT QLGIDSLIAV EIRSWFLKEA GVSLPVLKIL GGAAAKDLCE LACEEYKVTE
