PKS1_METAS
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 25-MAY-2022, entry version 15.
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};
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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 EnsemblFungi; KHN93908; KHN93908; MAM_08215.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OrthoDB; 68112at2759; -.
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 Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
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; 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; 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 Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..2162
FT /note="Polyketide synthase 1"
FT /id="PRO_0000445742"
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 400..844
FT /note="Ketosynthase (KS) domain"
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:PRU10022"
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
