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 05-DEC-2018, entry version 4. 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; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae; OC 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 RT host 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., RA Yin W.B., 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 CC that contributes to conidial pigmentation that provides protection CC from UV radiation, heat and cold stress (PubMed:29958281). The CC polyketide synthase Pks1 produces 1-acetyl-2,4,6,8-tetrahydroxy- CC 9,10-anthraquinone though condensation of acetyl-CoA with malonyl- CC CoA (By similarity). The dehydratase EthD and the laccase Mlac1 CC further convert the anthraquinone derivative into the final CC conidial pigment (By similarity). {ECO:0000250|UniProtKB:E9F646, CC ECO:0000269|PubMed:29958281}. CC -!- INDUCTION: Highly expressed during conidiation (PubMed:29958281). CC A conserved conidiation regulatory pathway containing BrlA, AbaA CC and WetA regulates expression. During conidiation BlrA up- CC regulates AbaA, which in turn controls WetA. Moreover, the Hog1 CC MAPK regulates fungal conidiation by controlling the conidiation CC regulatory pathway, and that all three pigmentation genes Pks1, CC EthD and Mlac1 exercise feedback regulation of conidiation (By CC similarity). {ECO:0000250|UniProtKB:E9F646, CC ECO:0000269|PubMed:29958281}. CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP CC transacylase (SAT) that selects the starter unit; a ketosynthase CC (KS) that catalyzes repeated decarboxylative condensation to CC elongate the polyketide backbone; a malonyl-CoA:ACP transacylase CC (MAT) that selects and transfers the extender unit malonyl-CoA; a CC product template (PT) domain that controls the immediate CC cyclization regioselectivity of the reactive polyketide backbone; CC and an acyl-carrier protein (ACP) that serves as the tether of the CC growing and completed polyketide via its phosphopantetheinyl arm. CC {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. CC {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 EnsemblFungi; KHN93908; KHN93908; MAM_08215. DR Proteomes; UP000030816; Unassembled WGS sequence. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.1200.10; -; 2. DR Gene3D; 3.40.366.10; -; 1. 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; 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; IPR020801; PKS_acyl_transferase. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR020807; PKS_dehydratase. 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 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; SSF47336; 2. DR SUPFAM; SSF52151; SSF52151; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR SUPFAM; SSF53901; SSF53901; 1. DR SUPFAM; SSF55048; SSF55048; 1. DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. DR PROSITE; PS50075; CARRIER; 2. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2. PE 1: Evidence at protein level; KW Complete proteome; Multifunctional enzyme; Phosphopantetheine; KW Phosphoprotein; Reference proteome; Repeat; Transferase. FT CHAIN 1 2162 Polyketide synthase 1. FT /FTId=PRO_0000445742. FT DOMAIN 1692 1766 Carrier 1. {ECO:0000255|PROSITE- FT ProRule:PRU00258, FT ECO:0000305|PubMed:29958281}. FT DOMAIN 1807 1884 Carrier 2. {ECO:0000255|PROSITE- FT ProRule:PRU00258, FT ECO:0000305|PubMed:29958281}. FT REGION 19 264 N-terminal acylcarrier protein FT transacylase domain (SAT). {ECO:0000255, FT ECO:0000305|PubMed:29958281}. FT REGION 400 844 Ketosynthase (KS) domain. {ECO:0000255, FT ECO:0000305|PubMed:29958281}. FT REGION 941 1245 Malonyl-CoA:ACP transacylase (MAT) FT domain. {ECO:0000255, FT ECO:0000305|PubMed:29958281}. FT REGION 1322 1636 Product template (PT) domain. FT {ECO:0000255, FT ECO:0000305|PubMed:29958281}. FT REGION 1896 2160 Thioesterase (TE) domain. {ECO:0000255, FT ECO:0000305|PubMed:29958281}. FT ACT_SITE 578 578 For beta-ketoacyl synthase activity. FT {ECO:0000255|PROSITE-ProRule:PRU10022}. FT ACT_SITE 1030 1030 For acyl/malonyl transferase activity. FT {ECO:0000255|PROSITE-ProRule:PRU10022}. FT ACT_SITE 1987 1987 For thioesterase activity. FT {ECO:0000250|UniProtKB:Q03149}. FT MOD_RES 1726 1726 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000255|PROSITE-ProRule:PRU00258}. FT MOD_RES 1844 1844 O-(pantetheine 4'-phosphoryl)serine. FT {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 //