PKS1_METRA
ID PKS1_METRA Reviewed; 2148 AA.
AC E9F646;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Polyketide synthase 1 {ECO:0000303|PubMed:25445307};
DE EC=2.3.1.- {ECO:0000269|PubMed:29958281};
DE AltName: Full=Conidial pigment biosynthesis polyketide synthase {ECO:0000303|PubMed:25445307};
GN Name=Pks1 {ECO:0000303|PubMed:29958281}; ORFNames=MAA_07745;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
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 GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
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 [3]
RP FUNCTION.
RX PubMed=20382249; DOI=10.1016/j.fgb.2010.03.011;
RA Fang W., Fernandes E.K., Roberts D.W., Bidochka M.J., St Leger R.J.;
RT "A laccase exclusively expressed by Metarhizium anisopliae during isotropic
RT growth is involved in pigmentation, tolerance to abiotic stresses and
RT virulence.";
RL Fungal Genet. Biol. 47:602-607(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25445307; DOI=10.1016/j.fgb.2014.10.018;
RA Chen Y., Feng P., Shang Y., Xu Y.J., Wang C.;
RT "Biosynthesis of non-melanin pigment by a divergent polyketide synthase in
RT Metarhizium robertsii.";
RL Fungal Genet. Biol. 81:142-149(2015).
RN [5]
RP IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=28447400; DOI=10.1111/1462-2920.13777;
RA Zeng G., Chen X., Zhang X., Zhang Q., Xu C., Mi W., Guo N., Zhao H.,
RA You Y., Dryburgh F.J., Bidochka M.J., St Leger R.J., Zhang L., Fang W.;
RT "Genome-wide identification of pathogenicity, conidiation and colony
RT sectorization genes in Metarhizium robertsii.";
RL Environ. Microbiol. 19:3896-3908(2017).
RN [6]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY,
RP INDUCTION, DOMAIN, AND PATHWAY.
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:25445307, PubMed:28447400,
CC PubMed:29958281). The polyketide synthase Pks1 produces 1-acetyl-
CC 2,4,6,8-tetrahydroxy-9,10-anthraquinone though condensation of acetyl-
CC CoA with malonyl-CoA (PubMed:29958281). The dehydratase EthD and the
CC laccase Mlac1 further convert the anthraquinone derivative into the
CC final conidial pigment (PubMed:20382249, PubMed:25445307,
CC PubMed:28447400). {ECO:0000269|PubMed:20382249,
CC ECO:0000269|PubMed:25445307, ECO:0000269|PubMed:28447400,
CC ECO:0000269|PubMed:29958281}.
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:25445307,
CC ECO:0000269|PubMed:28447400, ECO:0000269|PubMed:29958281}.
CC -!- INDUCTION: Highly expressed during conidiation (PubMed:28447400). 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 (PubMed:28447400). Expression is positively
CC regulated by Opy2 and the Slt2 MAPK (PubMed:29958281).
CC {ECO:0000269|PubMed:28447400, 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:25445307, ECO:0000269|PubMed:29958281}.
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DR EMBL; ADNJ02000010; EFY96684.2; -; Genomic_DNA.
DR RefSeq; XP_007823934.2; XM_007825743.2.
DR AlphaFoldDB; E9F646; -.
DR SMR; E9F646; -.
DR EnsemblFungi; EFY96684; EFY96684; MAA_07745.
DR GeneID; 19262031; -.
DR KEGG; maj:MAA_07745; -.
DR HOGENOM; CLU_000022_6_0_1; -.
DR Proteomes; UP000002498; 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; Repeat;
KW Transferase.
FT CHAIN 1..2148
FT /note="Polyketide synthase 1"
FT /id="PRO_0000445746"
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 930..1236
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 1755..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 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; 234854 MW; 176C4B1624236769 CRC64;
MNHVTIKQSD TRADPFRVFI FGDQSSCNLS NLQLLLFKKS NVYLASFIDQ VNLTLRHEIA
RLTAAERQSF PAFSSVQNLV ARALKKDTSV ALESTLATIY HLCCFINYFG DGQEAYPTGP
TTHVSGLCIG ALAAAAVSSS KSLAELVQAG IDAVRVSLKV GLLVARTAAL FSHQESNGTS
SSPWSYALPD SQLPLALAEE AIESYQAKTN IPPLSLPYIS AKGQNSWTVS GPPAIVQHFL
ETSQFEKTLR LTPLAVHAPY HAPHIFSAID VQHIIRAVGP VSSFSSKLSF ISSSSSRNLP
TGLKFQDLLY RAVEDILILP LDLREAAENI RLVLEATDNV QQCALFPIST GVGPSLKQSF
SPAMASRVSI VDCIMERVAA DAGPKSTSGP KPSESKIAII GMSGRFPESA DVEAFWDLLH
QGLDVHRPVP PDRFNGELYY DVTGKRKNTC KVMHGCWIND PGLFDAKFFN ISPKEAEQSD
PGQRLALATA YEALEAAGVV ADRTPSTQRD RVGVFYGMTS DDYREVSCGQ NVDTYFIPGG
NRAFTPGKIN YFFKYCGPSV SVDTACSSSL AAIHLACNSI WRNECDTAIA GGTNVMSNPD
SFVGLDRGYF LSRTGNCHTF DDDADGYCRA DAVGTVILKR LEDAIADHDP ILGVISGALT
NHSADAVSIT RPHSGAQEEI FSKLLTESGV HPHQVSYIEM HGTGTQAGDA TEMTSVLNCF
APSTSPRRLP HESLHLGSTK ANVGHSESAS GVSALIKVLL MMEKNIIPPH CGIKGKINHK
FPTDLDERNV HIAKTATQWN RRNELNNIRR AFVNNFSAAG GNTALLVEDY PLRIADSAQQ
DARTAHVVTV SAKSIKSLKG NLENLKKFVQ KQAFTEGFLP KLSYTTTSRR MHHPFRVAIP
AANSEQLLCA LDEELKHDSY TCSSESPVAF VFSGQGSQYS AMGQHLLHFT IFRDEVHAYD
ILAQRHGFPS IMPLIDGSVD IEDLEPLVVQ LGTVCVQMAL ASLWMALGMR PAYVVGHSLG
HYAALKVAGV LTASDTIYLV AMRARLLQNK CSRGSHAMLA IRSSAAEIQA HLDEGIHDIA
CINGPQDTVV SGCIDDIDRL SQKLMDKGIK ATRVNVPFAF HSAQVDPILD ELEAIASQVE
FHAPRVAIGC PLLGKTFTAG ETPSLEAKHI RRHCRETVNF LDVLRSAKDD GFVSEKTAWI
EIGPHTVCSN LVKANINQDI TAVPSLMRNK DGWQVLASSV ATLYRHGLSV AWDEYHHDFE
ACKQVLRLPA YSWDNKLYWI DYVHDWLLTR GDPPVQAAAP LPAPPSSFST ASVHRMVHES
VEKGKLTLTA ECEFTNEQLR EVVYGHVVNG NRVCSSSLYT DFGVTLGSYI LEKYRPDLQG
HAVDVQDMVV NKALVHKEGP TMLLRIDVVL DTTDSKAASM SIYSVNSKGN KTADHAQSSL
HFEQPKVWLK SWDSTQYYVE RSIEWLKEKA DQGLNSRMSS GVIYKLFSSL VDYSTAYKGM
QEAIVNTEDF EATALVRFQV DEGNFRCNPM WVDSCGQLAG FLMNGHAKTP KDQVFINHGW
QYFRTVRKFS RDKTYRTYVR MRCVEGTTYA GDVYIFDDEG IVGVCGSITF QGIPRKVLNT
AMPPPKSQNE APVRSGPAKP AAKPPRSASS EHSGHFARHA NIEPLKLDAA LKSATTARNP
MLPVFKIVAE EIGIPSASVD NGLVFADYGV DSLLSLSISG RLREELDLDV ESSAFETCAT
LADLAAQLGL DTFSSDQSSG QSSSSGGLSP RSDSIGEITS SVTTPPSLSP RGSVSGSQCK
DVCAILAEEI GVSMGEITND TDLGALGMDS LMSLAVLSRL REELELDLEG DFFVSHPNFS
SFKHMFQQGH GDEVEPEPSA ELKQYRATST LLQGNPKSAL YTLFLLPDGS GSSFSYAPIN
AVRKDVCVFG LNCPWLKSAE KLVQFGLKGL ATLYVEEIRR RAPHGPYNLG GWSAGGICAY
EAAIQFTREG ETVERLILLD SPNPIGLEKL PARLFDFVNG LGLFGDGKAP DWLLAHFLAF
IDALDEWKPV PWDKALGGNS PPPMTYILWA EDGICKGTDA RPEYRDDDPR EMKWLLENRT
NFGGNNWDVL LGQQSLSIER IQDANHFTML RKGKNTERVA AFIRSTFG
