OPS1_BEAB2
ID OPS1_BEAB2 Reviewed; 2211 AA.
AC J4UHQ6;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Orsellinic acid synthase {ECO:0000250|UniProtKB:Q5AUX1};
DE Short=OAS {ECO:0000250|UniProtKB:Q5AUX1};
DE EC=2.3.1.- {ECO:0000269|PubMed:26305932};
DE AltName: Full=Non-reducing polyketide synthase OpS1 {ECO:0000303|PubMed:26305932};
DE AltName: Full=Oosporein biosynthesis protein 1 {ECO:0000303|PubMed:26305932};
DE AltName: Full=Oosporein synthase {ECO:0000303|PubMed:26305932};
GN Name=OpS1 {ECO:0000303|PubMed:26305932};
GN Synonyms=PKS9 {ECO:0000303|PubMed:26305932}; ORFNames=BBA_08179;
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860;
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, INDUCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=26305932; DOI=10.1073/pnas.1503200112;
RA Feng P., Shang Y., Cen K., Wang C.;
RT "Fungal biosynthesis of the bibenzoquinone oosporein to evade insect
RT immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11365-11370(2015).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of the bibenzoquinone oosporein, a
CC metabolite required for fungal virulence that acts by evading host
CC immunity to facilitate fungal multiplication in insects
CC (PubMed:26305932). The non-reducing polyketide synthase OpS1 produces
CC orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units
CC (PubMed:26305932). Orsellinic acid is then hydroxylated to benzenetriol
CC by the hydroxylase OpS4 (PubMed:26305932). The intermediate is oxidized
CC either nonenzymatically to 5,5'-dideoxy-oosporein or enzymatically to
CC benzenetetrol by the oxidoreductase OpS7 (PubMed:26305932). The latter
CC is further dimerized to oosporein by the catalase OpS5
CC (PubMed:26305932). OpS6 probably functions en route for protecting
CC cells against oxidative stress by scavenging any leaked free radical
CC form of benzenetetrol by activating the thiol group of glutathione
CC (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA +
CC orsellinate; Xref=Rhea:RHEA:62972, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16162, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384;
CC Evidence={ECO:0000269|PubMed:26305932};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62973;
CC Evidence={ECO:0000269|PubMed:26305932};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26305932}.
CC -!- INDUCTION: Expression is positively regulated by the oosporein cluster
CC specific regulator OpS3 that binds the promoter at a 5'-CGGA-3' motif
CC (PubMed:26305932). Expression is negatively regulated by the global
CC transcription factor Msn2 that binds the stress-response element 5'-
CC AGGGG-3' (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (By similarity).
CC {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DOMAIN: The release of the polyketide chain from the non-reducing
CC polyketide synthase is mediated by the thioesterase (TE) domain
CC localized at the C-ter of the protein (By similarity).
CC {ECO:0000250|UniProtKB:Q5ATJ7}.
CC -!- DISRUPTION PHENOTYPE: Leads to the loss of oosporein production
CC (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
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DR EMBL; JH725181; EJP62792.1; -; Genomic_DNA.
DR RefSeq; XP_008601498.1; XM_008603276.1.
DR AlphaFoldDB; J4UHQ6; -.
DR SMR; J4UHQ6; -.
DR PRIDE; J4UHQ6; -.
DR EnsemblFungi; EJP62792; EJP62792; BBA_08179.
DR GeneID; 19891191; -.
DR HOGENOM; CLU_000022_6_4_1; -.
DR InParanoid; J4UHQ6; -.
DR PHI-base; PHI:5037; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 3.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR003965; Fatty_acid_synthase.
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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase; Virulence.
FT CHAIN 1..2211
FT /note="Orsellinic acid synthase"
FT /id="PRO_0000438571"
FT DOMAIN 1681..1755
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1787..1865
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 44..246
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26305932"
FT REGION 383..808
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26305932"
FT REGION 910..1228
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26305932"
FT REGION 1334..1573
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26305932"
FT REGION 1755..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1937..2204
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26305932"
FT COMPBIAS 1760..1786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 549
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1006
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1715
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1824
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2211 AA; 237462 MW; ED327AD168F62FA7 CRC64;
MPSFFPVFSG LGSGSVFSEE NVGRAEENAL SPECAVLLQS CHRTFREQVS DAIARNILPE
DSIDLDDFAE PASLIRPLSK YSRNVVMQHA ALYLHQILAY MTSQKELGNL IGSAGFCTGL
LPAAVAAASQ TSVITLISQS HHFFQVALWI GIRSEQYRVD HLTNDTQDAD GESMLPCSYV
LEGVSEAAAQ DLLHKTNMGN EVFVSAILSP TRVTISGIPT KLSTFISKHL PANCRTTVAV
VHSLYHHESL LEVRNLVMAD LERQDTLLQA RVELSAPILS TKTGKPLALS SVTTLEQVAC
AILDLIFIEK VDWLNLQQSI VSHTSQDALD RPINIVNYGP GLGMAPSAFA QAQEKDVCIM
DAAKISKGSF QNSGASRLAW DDIAIVGMAV ELPGASDADT LWQNLVDGYQ ACSEIPPSRF
NVNDYNNGKG SRTLNTKYGN FLENPFLFDA EHFGISRREA KSMDPQQRIL LQTAYRALED
AGYVPDTTTS SARDTFGCWI GNATLDYVDN LRSDIDVYYS TGTLRAFLSA RISYVFGWSG
PSITLDTACS SSIVALHQAA RSILAGDCRS ALVGAANTIT SPDMYLGLDR AHFLSPSGQC
KAFDASADGY CRAEGCGVFV IKRLSDALAE GDRIHGVIKA IEINQSGNTH SITHPHVPTQ
EALFDKMFRE SRINPHEISV VEMHGTGTQA GDPNEVESVR RALCKARSPL NPVYLTSLKA
NIGHAEAVSG IAGLAKLILM TRNGYIPPQV SLKTLNPRIR PLGVDGAAID ANGTEWPRAG
PKKARMSMLN NFGAGGSNAA VIIGEHLSQD ESEAQQPACG ATIFVCGVSA KNDRALVKLQ
ETVADYLTSA GQSRKPPSLA DVCATLTSRR QMYNHRVAVV ASSLEELAEN LRSASSHNVS
KSICEAPEAV FIFSGQGSQY LGMGRELIEQ YEDFAHTVNV CDGWLVKNNY PSCLAVITGE
QRESEDDKVD AHTWQSFQSA IYVIEVALAK LLESWGIRPQ AVAGHSLGEY AALVTAGVIR
LMDGLKLVAH RAKLMMEQCD LGQTSMLAVN CSAAVITSII EASTDFEGLA ISCNNSETDC
VVGGPVPQLV LLKKHLTDRA QVRSKLLDVP MAFHTAAMDP ILEEFTAFAA REVRVFPPTL
PVVSNVLGRT VAVGEQAFSP EYFAKQCRGT VAFDDGIKHF LALGDCESTP YRWIEIGPHP
SVQPMLRGRL GKAATSHIQL TTLKKNVPPA STLSQLLSHF YQTSSGVNWR SVFSRNAHRR
FKLIQLPGMP FFPSEFHVPY REMAGEPAST SQSSGDAASN VVPNSFAVHA IQKLSHGASN
SCAIYETPAV LLKEFIEGHL VCGYALCPAS VYHEMVLAAL NDCQSAAGSS VVWGLSKVSY
CAPMVYDGNS NQVLRVVITP RLTLPDRYDF AVMSYVAGTD PNERSTVHCR GVVKQSNMAS
AELKYSRLQA SMKGSMDGLK HVGQLGAPAA SCVQVFSKRA MYEKIFTRVV EYSDPYQKVE
TIRIREDTGE ALATCVSPAP YLARDSSIPA SHAIFMDVLL HVAGFVSNLN LPNDVMGICK
EVGGATTLRA PVVRDGACAP FDVYCSTFDT QDSDGRSFTI SNAYAVDSSG VMAVFKGMVF
QHVKIPLIEQ ALKRATRSSP NAAVSASHPA QPKRRNDVTS FVNAQSVERM ALPRAAAPVR
AAPEVSVPEL VAKVCGLDAG QLGVDSRLDA HGVDSLMGIE IAAALSSALG VDVLPDTLGS
CDTVGDIERL CEALSPTPVG NDVDNDSPTP GSERGSDSAI STPASVSTVD ASSIDMVQIV
AELCGARAEA VSPDSELRAL GVDSLMFLEL ADRLQDLDRG IALSSNDLAD CQTIGDIERL
IVKRPGTPAY QSGISTKIYP EAVHASSEAV RLSAQQPATQ ISLLASEEAV LPQIERLLHL
SQQPEEIQVG SLDRKFSGKS PLFLIHDGSG ICTHYRGLRP LGRRVLALHD PKFLIQSSKQ
RSWASLTTMA NEYASSISST MGMTGGEDCI LGGWSFGGVV AFEAARILMS RGHRVKGVVL
IDSPPPIGHI PLSESIISAV TAQPAEKDAA AGSTTASKCV SPVASAIRKL VQQSFRICAG
LIGDFGTSAE LQQRGLSNKP VGPVPRVILL RSAVGWTPPR GYTGAAVEEM ENPWLQDRRD
RSLATAGWEI LTGGPIQCLD IPGNHFQVFD APNIAAVSAA LVDACSEFEL K
