BOA9_BOTFB
ID BOA9_BOTFB Reviewed; 2294 AA.
AC G0LET7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Reducing polyketide synthase BOA9 {ECO:0000303|PubMed:21722295};
DE EC=2.3.1.- {ECO:0000305|PubMed:21722295};
DE AltName: Full=Botcinic acid biosynthesis cluster B protein 9 {ECO:0000303|PubMed:21722295};
GN Name=BOA9 {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, DOMAIN, DISRUPTION
RP PHENOTYPE, 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, 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 B 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: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 -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:21722295,
CC ECO:0000305|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:21722295). {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; an enoyl reductase (ER)
CC domain that reduces enoyl groups to alkyl group; a ketoreductase (KR)
CC domain that catalyzes beta-ketoreduction steps; and an acyl-carrier
CC protein (ACP) that serves as the tether of the growing and completed
CC polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:21722295, ECO:0000305|PubMed:23203902}.
CC -!- DISRUPTION PHENOTYPE: Abolishes botcinic acid and botcinin production.
CC {ECO:0000269|PubMed:21722295}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR718878; CBX87032.1; -; Genomic_DNA.
DR AlphaFoldDB; G0LET7; -.
DR SMR; G0LET7; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 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; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Transferase; Virulence.
FT CHAIN 1..2294
FT /note="Reducing polyketide synthase BOA9"
FT /id="PRO_0000444646"
FT DOMAIN 2214..2292
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 7..412
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT REGION 537..853
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT REGION 930..1104
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT REGION 1618..1908
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT REGION 1934..2107
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21722295,
FT ECO:0000305|PubMed:23203902"
FT ACT_SITE 630
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 962
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2251
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2294 AA; 251664 MW; 9B89812F3C81A9D4 CRC64;
MSFPEPVAII GMGCRFPGDS DTPDEFWKML AEERSGLSRP PLSRWNIDGF HANKARPGSL
TPEGGYFINE DIWKFDPAFF GIVQEEAKAM DPQQRKLLEC VYESFESGGI TLSQLSGSNT
GCYIGNFTSD YYLQGHRDHN NPKPYSLLGS GYTIISNRVS YLFDLCGPRA LQTKEIDAAV
VGGTNLMLAV ETQMSTDKVG VLSATSTCHT FDESADGYGR AEGVGAIFLK RLSDAIRDND
PIRGVIRGTA TNANGKTSGI TQPSAKGHET VMRTAYEFAG LDPRDTSYFE THGTGTQVGD
PIEIKGVGNF FFNGTDRQKL LVGSVKTNVG HSEAASALAS IIKVCLAMEK RTIPATIGIK
KLNPKIDFKG GRIEVVQKMT PWPKGFSVCR ASINSFGYGG ANATAIVEAA DSVLPGKLTY
TRRGQDERDL EASSEESESV EMVGTKSASQ VRAVSRSEFL LLFSAHDIST LKSNIERCRD
VAEDYNILDL AYTLGCRRSN FFNCAYTVAR EDDVEEDLME HEITFGKRGN GGNIGFIFTG
QGAQNAQMGR ELMLTFPSYI DTIRKLDRSL QSLGDDSPDW TIEDVLMEPA VTSKINDVEI
SQPVCTAVQI ALVELLRLWN VTPVACIGHS SGEIASSYAA NLIPAEEAII SAFYRGRGVG
TLKVKGTMLA VGAGPEEIQP YLTDGLRIAC YNSPNSVTLS GDIEPATIVQ KKLESDRVFV
RELKTGGRAY HSHHMLNIGN DYESRLSEAL SRFGASQTTN QAQVQNPVFF SSVTAQQMPS
NFKPGPSYWR QNLESPVRFT EAVEAALAAD LGISQFVEIG PHSALAGPLR QIRDNLGITP
KDLDYAATLV RGQSSVTRLL DLAGTLTMRG FSVNVERVNA IEKREGGAII TKTGLPIVDL
PRFSWNYSAG EIRNKNRPDE EHRLRKFKYH DLLGAILPGS SVEQRQWRNM LDSKNFPWLE
EHKLGPQPVL PGTGYLAIAT EAARQFFHDK LTVSGAFRYF FPNISITSAL NIPPSGSQVE
IVTTMKFATI TASITSKTIA EFTISSIQAG NWTNHCVGTV TKKKAVTMAP RFDESKLQEP
KAARTWYRGF QKVSLNYGPA FNGLSNIRTN PALEEAVADT ELCPDGVSEH DSAYIVHPAA
MDTCIQVALI GAHKGSLAGL KRSFVPTSMA NVSLWSWADD DHITQLTPGK GKVLAHAEFF
SLRAMNGWCQ LFSPEGKPLF EIEELSCTQY SEALDDLGTI DRHPYLRTVW KPDVDKMVSN
LTDNSLLDLI VHKRPGFNIC EILNTESMIS DNLHRVLESG SSLRRYKTYT VMALGDVDIE
PIKVKYEAFP GVVVQKLVLD DVPETFFDLL IVPQFPSDEI DLAKLKGLLT PGGNMLLYSS
EFKNGNTIKT DLQLAGLYTL LEDKESLLIS PHQRTSSDLP AGEIVLVTRT SPTVFDSHIF
SGLSKSGRLI TSISLQDFKF HAHTKATYVF IVESESSIFH GSLTSQELAT IQSVASGATN
MLWVTHGNLL EGDDPNAGIV IGLGRCLQTE HPTLTFKTLD LDHRDPIQTI SNITTILNAA
DSGDEDKEFM VKNGIFYVSR LSQDPLLDQQ FVSGVESEPK MIPYEPEKRI RLGIERVGIF
DTIHFKDDEL EASLKPGEVE VDVKAVGLNM KDFATLQGTY NSEILGLEGA GIVRSIGTGV
TNVAIGDRKL KPEETLDQMS SIMMPFLTAI YGLIYLAKLQ PGESVLINSA TGGVGLAAIQ
IAKMIGAEIF ATVGTPEKKK FLMQEYGLQD DHVLSSKDAS FAAEIMQTTG GRGVDVSLNS
LVREQLRATW NCIGHHGRHI ELGQTDILDQ GILDMSPFKR GASFIAMDLV LVFEHKPDLI
SQILGEIMHY YRDCKIQPLP NLSVFPVSAI GKAFEEFGKN SRIGRVVVSF DTETINTRLS
LRRRRSQLLS SQMVHTYLLG VLEALVDVWL VTWLKKGARH LIFLGRSGED RPEAASMIKD
FRNDGITVDV VKGDVTRISD VQKAVDLAAG PLFGVVQGVM ALDDRLFTSH DLNSWEYAVR
PKVTGTWNLH NAVASHSLDF FVMLGSSSAL SGFPTQSNYC AGNSFLEFFA RYRQSKGLPA
TTISLTVVTE VGFVSQNERI EDGLARTGVH TINEAGVIDL IDTAMMKAPS SSWNLDPLAN
SFIVTGVEPL QLSANLDIDS IPFWRQPRIG PVFNAVLAKK SGNETGPGQN KRRLLLPDIL
EMIIEKFSQT FNVAVEDIDP GTEIVRFGMD SMIGTSLRTW CYKTLGADIA ASDFMSLNLT
ADSLAKKIYD IRKG
