ID PKS1_METAS Reviewed; 2162 AA. AC A0A2U8NET4; A0A0B2WJ51; DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot. DT 12-SEP-2018, sequence version 1. DT 22-FEB-2023, entry version 18. DE RecName: Full=Polyketide synthase 1 {ECO:0000303|PubMed:29958281}; DE EC=2.3.1.- {ECO:0000269|PubMed:29958281}; DE AltName: Full=Conidial pigment biosynthesis polyketide synthase {ECO:0000303|PubMed:29958281}; GN Name=Pks1 {ECO:0000303|PubMed:29958281}; ORFNames=MAM_08215; OS Metarhizium album (strain ARSEF 1941). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium. OX NCBI_TaxID=1081103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ARSEF 1941; RX PubMed=25368161; DOI=10.1073/pnas.1412662111; RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S., RA St Leger R.J., Wang C.; RT "Trajectory and genomic determinants of fungal-pathogen speciation and host RT adaptation."; RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC RP ACTIVITY, INDUCTION, AND DOMAIN. RC STRAIN=ARSEF 1941; RX PubMed=29958281; DOI=10.1371/journal.pgen.1007472; RA Zeng G., Zhang P., Zhang Q., Zhao H., Li Z., Zhang X., Wang C., Yin W.B., RA Fang W.; RT "Duplication of a Pks gene cluster and subsequent functional RT diversification facilitate environmental adaptation in Metarhizium RT species."; RL PLoS Genet. 14:E1007472-E1007472(2018). CC -!- FUNCTION: Polyketide synthase; part of the Pks1 gene cluster that CC mediates the biosynthesis of an anthraquinone derivative pigment that CC contributes to conidial pigmentation that provides protection from UV CC radiation, heat and cold stress (PubMed:29958281). The polyketide CC synthase Pks1 produces 1-acetyl-2,4,6,8-tetrahydroxy-9,10-anthraquinone CC though condensation of acetyl-CoA with malonyl-CoA (By similarity). The CC dehydratase EthD and the laccase Mlac1 further convert the CC anthraquinone derivative into the final conidial pigment (By CC similarity). {ECO:0000250|UniProtKB:E9F646, CC ECO:0000269|PubMed:29958281}. CC -!- INDUCTION: Highly expressed during conidiation (PubMed:29958281). A CC conserved conidiation regulatory pathway containing BrlA, AbaA and WetA CC regulates expression. During conidiation BlrA up-regulates AbaA, which CC in turn controls WetA. Moreover, the Hog1 MAPK regulates fungal CC conidiation by controlling the conidiation regulatory pathway, and that CC all three pigmentation genes Pks1, EthD and Mlac1 exercise feedback CC regulation of conidiation (By similarity). CC {ECO:0000250|UniProtKB:E9F646, ECO:0000269|PubMed:29958281}. 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. {ECO:0000305|PubMed:29958281}. 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. {ECO:0000305|PubMed:29958281}. CC -!- DISRUPTION PHENOTYPE: Results in red conidia. CC {ECO:0000269|PubMed:29958281}. CC -!- SEQUENCE CAUTION: CC Sequence=KHN93908.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; MG385101; AWL82991.1; -; mRNA. DR EMBL; AZHE01000047; KHN93908.1; ALT_SEQ; Genomic_DNA. DR AlphaFoldDB; A0A2U8NET4; -. DR SMR; A0A2U8NET4; -. DR STRING; 1081103.A0A2U8NET4; -. DR ESTHER; metas-pks1; Thioesterase. DR HOGENOM; CLU_000022_6_0_1; -. DR OrthoDB; 5396558at2759; -. DR Proteomes; UP000030816; Unassembled WGS sequence. 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 CDD; cd00833; PKS; 1. DR Gene3D; 3.30.70.3290; -; 1. DR Gene3D; 3.40.47.10; -; 1. DR Gene3D; 1.10.1200.10; ACP-like; 2. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2. DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; 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; IPR042104; PKS_dehydratase_sf. DR InterPro; IPR020807; PKS_DH. DR InterPro; IPR020806; PKS_PP-bd. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR006162; Ppantetheine_attach_site. DR InterPro; IPR030918; PT_fungal_PKS. DR InterPro; IPR032088; SAT. DR InterPro; IPR001031; Thioesterase. DR InterPro; IPR016039; Thiolase-like. DR PANTHER; PTHR43775:SF45; CONIDIAL PIGMENT POLYKETIDE SYNTHASE ALB1; 1. DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1. 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 SMART; SM00827; PKS_AT; 1. DR SMART; SM00825; PKS_KS; 1. DR SMART; SM00823; PKS_PP; 2. DR SUPFAM; SSF47336; ACP-like; 2. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1. DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1. DR SUPFAM; SSF53901; Thiolase-like; 1. DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1. DR PROSITE; PS50075; CARRIER; 2. DR PROSITE; PS00606; KS3_1; 1. DR PROSITE; PS52004; KS3_2; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2. PE 1: Evidence at protein level; KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; KW Reference proteome; Repeat; Transferase. FT CHAIN 1..2162 FT /note="Polyketide synthase 1" FT /id="PRO_0000445742" FT DOMAIN 397..841 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348, FT ECO:0000305|PubMed:29958281" FT DOMAIN 1692..1766 FT /note="Carrier 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258, FT ECO:0000305|PubMed:29958281" FT DOMAIN 1807..1884 FT /note="Carrier 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258, FT ECO:0000305|PubMed:29958281" FT REGION 19..264 FT /note="N-terminal acylcarrier protein transacylase domain FT (SAT)" FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281" FT REGION 941..1245 FT /note="Malonyl-CoA:ACP transacylase (MAT) domain" FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281" FT REGION 1322..1636 FT /note="Product template (PT) domain" FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281" FT REGION 1633..1669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1772..1809 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1896..2160 FT /note="Thioesterase (TE) domain" FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281" FT COMPBIAS 1643..1669 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 578 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 713 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 757 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 1030 FT /note="For acyl/malonyl transferase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022" FT ACT_SITE 1987 FT /note="For thioesterase activity" FT /evidence="ECO:0000250|UniProtKB:Q03149" FT MOD_RES 1726 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" FT MOD_RES 1844 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" SQ SEQUENCE 2162 AA; 235429 MW; 812C6E52C12537BA CRC64; MEHVIIKQPD TGGDSVRIFV FGDQTSCNLS NLQPLLLKRS NIYLVSFVDQ VNCALRHEIA RLTTAERRSF PAFSSIQNLV TRGLQKERSV ALESTLATIY QLCCFFNYFG DGQKSYPTGP NTHVSGLCIG ALSAAAVSSS RSLDELVQAG IEAVLVSLKV GLLVSRTAAL FSHQASANSS CSSSASWSYT VPDSQLPLAL AEEAIASYTD KTNIPPLSSP YISARGQNSW TVSGPPAVLQ GFLRSSQVVE APRLTPLAVH APYHAPHIFS VSDVENVIQA VGPVSSLSSK LPFISTSSCG SLSSGTRFQD LLFRAVEGIL ILPLDLRAAA ENMRQVFEAV EDVSRCALIP ISTGVCTSLK MSFSPVLADC VSIVDSIMEG TAADGGSKSA PATNPGDSKI AIIGMSGRFP EAADVEAFWA VLYKGLDVHR PVPKDRYDGE LYYDPTGKKK NTCKVMHGCW INEPGLFDAK FFNISPKEAE QSDPGQRLAL TTAYEALESA GVVAGRTPST QRDRVGVFYG MTSDDYREVR ASVCKPQCKP FPYTKANLTT GGNRAFTPGK INYFFKYCGP SVSVDTACSS SLAAIHLACN SIWRNECDTA VAGGTNVMSN PDSFVGLDRG HFLSRKGNCN NFDDEADGYC RADAVATVVL KRLEDAMADH DPILGVISGA HTNHSAESVS ITRPHSGAQE EIFSKLLCES GVHPHQVSYV EMHGTGTQAG DATEMTSVLN CFAPSTGPRR LPHESLHLGS AKANVGHSES ASGVTSLIKV LLMMEKNMIP PHCGIKSKIN HRFPTDLEQR NVHIAKTATR WGRRREFDNI RRVFVNNFSA AGGNTALLVE DYPPLAAASS QRDSRTAHVV TTSAKCIQSL RGNLEKLKAF VQKTSSSESF MSKLSYTTTA RRMHHPFRVA IPAAKPEELL SALDTELRRD SCRCSSESAV AFVFSGQGSQ YGAMGKHLLH YTIFRGEIDS YDILAQRHGF PSIMPLVDGS VAIEHLEPLV VQLGTVCVQM ALASLWIAFG MQPSYVVGHS LGHFAALKVS GALTASDTIY LVGMRARLLQ NKCSIGSHAM LAVRSSAEDV QAYLDADVHD IACINSPQDT VVSGRVDDID RLSERLLDKG IKATRVNVPF AFHSSQVEPI LDELGAIASQ VKFHSPCVPI GCPLQGKSLL PGETLTSEAS HVKRHCRQTV NFRGILQSAK SDGLVSEKTA WIEIGPHTVC SMLVKANINH DVTAVPSLMR SHDGWQVLAS SLATLYSKGL SVAWDEYHHD FECCKEVLRL PAYSWDNKRY WIEYVHDWLL TRGDPPVPAA APSPAPVSSF STASVHRIVR ESVDRETVAL TAECEFTSEQ LREVVYGHVV NGNRVCTSSL YADFGVTLGT YILDKYRADL KDHSVDVQEM VVNKPLVHKE GLPMLLRIDV VHDMTASKSA TMSIYSINAK GNKTVDHAKS SLCFGESRAW LRSWDSTQYY VERSIEWLKE KADQGLNSRL SSGVIYKLFS SLVEYSSAYK GMKEAIVNTE DFEATALVQF QVDEGNFRCN PMWVDSCGQL AGFLMNGHSK TPLDQVFINH GWQSFRTVRK FCKDKTYRTY VRMRCIEGTT YAGDVYIFDD EGIVGVCGSI TFQGVPRRVL DAAMPAPKSP NKTRDHASPN ATISRAKPPQ GSSPASSAQL AQHSSIEPLK LDAALKSATT AIDPMHAVLR ILSEEIGIPL TSLQYDLVFA DYGVDSLLSL TISGRLREEL DLDIESSVFE TCATVGDFAV HLGLDTLASY QSSGESNVSG GVSPRSDSVA AMSSDVTTPP AQSPLGSMSS SPCEDLCAII AEEIGVSMSV IKSDANLGEL GMDSLMSLTV LSRLREELDL DLEGDFFVAH PTYSSFKHVF EQEIEPEIGL GESADLKKYH ATSTLLQGSP KSALYTLFLL PDGSGSATSY ATISAVGRDI CVYGLNCPWL KSAEKLVQFG LKGLASLYVG EIRRRAPHGP YNLGGWSAGG ICAYEAAIQF TREGEAVERL ILLDSPNPIG LEKLPPRLFD FVNGLGLFGE GKAPDWLLAH FLAFIDALDQ WKPVPWDKAL DSTTPPPMTY ILWAEDGLCK GIDARPEYRD DDPREMRWLL ENRTNFGGNS WDILLGEGRL LTERIQDANH FTMLRRGKNA ERVAAFIRSA FK //