PKS1_METAQ
ID PKS1_METAQ Reviewed; 2148 AA.
AC A0A2U8NEV6; E9E687;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 25-MAY-2022, entry version 17.
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=MAC_05385;
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC
RP ACTIVITY, INDUCTION, AND DOMAIN.
RC STRAIN=CQMa 102;
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). Expression is also up-
CC regulated in appressoria-forming germlings on locust cuticle
CC (PubMed:29958281). {ECO:0000250|UniProtKB:E9F646,
CC 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=EFY88620.1; 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; MG385100; AWL82990.1; -; mRNA.
DR EMBL; GL698509; EFY88620.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_007811725.1; XM_007813534.1.
DR AlphaFoldDB; A0A2U8NEV6; -.
DR SMR; A0A2U8NEV6; -.
DR STRING; 92637.XP_007811725.1; -.
DR EnsemblFungi; EFY88620; EFY88620; MAC_05385.
DR GeneID; 19249696; -.
DR KEGG; maw:MAC_05385; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OrthoDB; 68112at2759; -.
DR Proteomes; UP000002499; 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; 1.
PE 1: Evidence at protein level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..2148
FT /note="Polyketide synthase 1"
FT /id="PRO_0000445741"
FT DOMAIN 1678..1752
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29958281"
FT DOMAIN 1793..1870
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29958281"
FT REGION 19..261
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT REGION 397..832
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT REGION 929..1233
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT REGION 1310..1624
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT REGION 1619..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1756..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..2146
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT COMPBIAS 1622..1647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 566
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1018
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1973
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1712
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1830
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2148 AA; 235786 MW; 44CFEB438F78A990 CRC64;
MEHVTIKQSG TRADPFRVFI FGDQSSCNLS NLQLLLLKKS NIYLASFVDQ VNFTLRHEIA
RLTTAERQSF PAFSSIQNLV TRALKKDKSV ALESTLATIY HLCCFLNYFG DGQEAYPTGP
NTHISGLCIG ALAAAAVSSS KSLAELVQAG IDAVRVSLKV GLLVARTAAL FSHQEPNGTS
SSPWSYAVPD SQLPLAFAEE AIESYQVKTK IPPLSLPYIS AKGQNSWTVS GPPEIVQHFL
ESSKFEKTLR LTPLAVHAPY HAPHIFSARD VEHIIHAVGP VSNISSKLSF ISSSSSCNLP
NGVKFQDLLY RAVEDILILS LDLREAAENI RLVLEATDDV QQCVLFPIST TVCPSLKQSF
SPVLASRVSI VDCIMESVAA NAGPKSTSGP KPSDSKIAII GMSGRFPESA DVEAFWDLLY
QGLDVHRPVP PDRFNGESYY DVTGKRKNTC KVMHGCWINE PGLFDAKFFN ISPKEAEQSD
PGQRLALATA YEALESAGVV ADRTPSTQRD RVGVFYGMTS DDYREVSCGQ NVDTYFIPGG
NRAFTPGKIN YFFKYCGPSV SVDTACSSSL AAIHLACNSI WLNECDTAIA GGTNVMTNPD
SFVGLDRGYF LSRTGNCHTF DDEADGYCRA DAVGTVILKR LEDAIADHDP ILGIISGAYT
NHSADSVSIT RPHSGAQEEI FSKLLTESGV HPHQVSYIEM HGTGTQAGDA TEMTSVLNCF
APSTHPRRLP HESLHLGSTK ANVGHAESAS GVSALIKVLL MMEKNIIPPH CGIKGKINQK
FPTDLDERNV HIAKTATQWN RRDEFNNIRR AFVNNFSAAG GNTALLVEDY PLPTVDSSQE
DSRTAHVVAV SAKCVKSLKG NLENLKKFVQ KQSSIEGFLP KLSYTTTARR MHHPFRVAIP
AASSDQLLSA LDQELKHESY RCTSESPVAF VFSGQGSQYS AIGRHLLHFT IFRDEVNSYD
ILAQRHGFPS IMPLIDGSVD IEDLEPLVVQ LGTVCVQMAL ASLWIAFGMR PAYVVGHSLG
HYAALKVAGV LTASDTIYLV AMRARLLQNK CSRGSHTMLA IRSSADEMQA YLDEDIYDIA
CINGPQDTVV SGCIDDIDRL SQKLMDNRIK VTRVNVPFAF HSAQVDPILD ELEAIASQVE
FHTPRVAIGC PLLGKTFVAG ETSSLGADHI KRHCRETVNF RDILRSAKGD GLISEKTAWI
EIGPHTVCST LLRANINQDI VAVPSLMRNK DGWQVLASSV ATLYRHGLPV DWDEYHHDFE
ACKQVLRLPA YSWDNKVYWI HYVYDWLLTR GDPPVQAAAS LPAPPSSFST ASVHRIVHES
VDKGKLTLTA ECEFTSEQLR EVVYGHVVNG NRVCSSSLYT DFGVTLGLYI LETYRPDLKD
HSVDVQDMVV NKALVHKEGS TMLLRINVIL DMTDGKAASM SIYSVNSKGD KTADHAQSSL
HFEQPKVWLR NWDSTQYYVE RSIEWLKEKA DQGLNSRMSS GVIYKLFSSL VDYSTAYKGM
QEAIVNTEDF EATALVRFQV DEGNFRCNPM WVDSCGQLAG FLMNGHAKTP KDQVFINHGW
QSFRTVRKLS KDKTYRTYVR MRCIEGTTYA GDVYIFDNEG IVGVCGGITF QGIPRKVLNT
AMPPPKSQNE AQVHSSPAKS RPKPPGSASS VHSGRLARHT NIEPLKLDAA LKSATAARDP
MQALFKIVSE EIGIPSASVQ NDLVFADYGV DSLLSLSISG RLREELDLDV ESSVFETCAT
LADLATHLGF DTFSSDQSSG QSSSCGGLSP RSDSTGEITS NATTPPSLSP RGSVSGSQCK
DVCAILAEEI GVSMSEITND TDLGELGMDS LMSLAVLSRL REELELDLEG DFFVSHPKFS
SFKHMFQQGH EDEIEPEPSA ELKQYRATST LLQGNPKSAL YTLFLLPDGS GSSFSYAPIN
AVRKDVCVYG LNCPWLKSAE KLVQFGLKGL ATLYVEEIRR RAPHGPYNLG GWSAGGICAY
EAAIQFTREG ETVERLILLD SPNPIGLEKL PARLFDFVNG LGLFGDGKAP DWLLAHFLAF
IDALDEWKPV PWDKALGSNT PPPMTYILWA EDGICKGTDA RPEYRDDDPR EMKWLLENRT
NFGGNNWDVL LGEPALSIER IQDANHFTML RKGKNTERVA AFIRSTFG
