PKS1_METBS
ID PKS1_METBS Reviewed; 2148 AA.
AC A0A0B4ESU9;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 25-MAY-2022, entry version 34.
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=MBR_10250;
OS Metarhizium brunneum (strain ARSEF 3297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1276141;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 3297;
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 IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY,
RP INDUCTION, AND DOMAIN.
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}.
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DR EMBL; AZNG01000033; KID61218.1; -; Genomic_DNA.
DR RefSeq; XP_014539689.1; XM_014684203.1.
DR AlphaFoldDB; A0A0B4ESU9; -.
DR SMR; A0A0B4ESU9; -.
DR EnsemblFungi; KID61218; KID61218; MBR_10250.
DR GeneID; 26247520; -.
DR HOGENOM; CLU_000022_6_0_1; -.
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_0000445743"
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 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; 234471 MW; C8EB500E4E7E5480 CRC64;
MNHVTIKQSD TRADPFRVFI FGDQSSCNLS NLQLLLFKKS NVYLASFIDQ VNLTLRHEVA
RLTAAERQSF PAFSSVQNLV ARALKKDTSV ALESTLATIY HLCCFINYFG DGQEAYPTGP
TTHVSGLCIG ALAAAAVSSS KSLAELVQAG IDAVRVSLKV GLLVARTAAL FSHQESNGTS
SPPWSYAVPD SQLPLALAEE AIESYQAKTN IPPLSLPYIS AKGQNSWTAS GPPAIVQHFL
ETSQFEKTLR LTPLAVHAPY HAPHIFSAID VQHIIRAVGP VSSFSSKLSF ISSSSSRNLA
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 DDEADGYCRA DAVGTVILKR LEDAIADHDP ILGVISGALT
NHSADAVSIT RPHSGAQEEI FSKLLTESGV HPHQVSYIEM HGTGTQAGDA TEMTSVLNCF
APSTSTRRLP HESLHLGSTK ANVGHSESAS GVSALIKVLL MMEKNIIPPH CGIKGKINHK
FPTDLDERNV HIAKTATQWN RRNELNNIRR AFVNNFSAAG GNTALLVEDY PLLIADSSQP
DGRTAHVVTV SAKSIKSLKG NLENLKKFVQ KQASTEGFLP KLSYTTTARR MHHPFRVAIP
AANSEQLLSA LNEELTHDSY TCCSESPVAF VFSGQGSQYS AMGQHLLHFT IFRDEVHAYD
ILAQRHGFPS IMPLIDGSVD IEDLEPLVVQ LGTVCVQMAL ASLWMALGMR PAYVVGHSLG
HYAALKVAGV LTASDTIYLV ATRARLLQNK CSRGSHAMLA IRSSAAEIQA HLDEGIHDIA
CINGPQDTVV SGCIDDIDRL SQKLMDKGIK ATRVNVPFAF HSAQVDPILD ELEAVASQVE
FHAPRVAIGC PLLSKTFKAG ETPSLEAKHI RRHCRETVNF LDVLRSAKDD GLVSEKTAWI
EIGPHTVCSN LVKANINQDI TAVPSLMRNK DGWQVLASSV ATLYRQGSSV AWDEYHHDFE
ACKQVLRLPA YSWDNKLYWI DYVHDWLLTR GDPPVQAAAS LPAPPSSFST ASVHRIVHES
VEKGKLTLTA ECEFTNEQLH EVVYGHLVNG NRVCSSSLYT DFGVTLGSYI LEKYRPDLQG
HAVDVQDMVV NKALVHKEGP TMLLRIDVVL DTTDSKAASM SIYSVNSKGN KTADHAQSSL
HFEQPKVWLK SWDSTQYYVE RSIEWLKEKA DQGLNSRMSS GVIYKLFSSL VDYSTAYKGM
QEAIVNTEDF EATALVRFQV DEGNFRCNPM WVDSCGQLAG FLMNGHAKTP KDQVFINHGW
QYFRTVRKFS RDKTYRTYVR MRCVEGTTYA GDVYIFDDDG IVGVCGSITF QGIPRKVLNT
AMPPPKSQNE APVRSGPAKP AVKPPRSASS EHSGHFARHA NIEPLKLDAA LKSATTARNP
MLPVFKIVAE EIGIPSAGVD NGLVFADYGV DSLLSLSISG RLREELDLDV ESSAFETCAT
LADLAAHLGM DTFSADQSSG QSSSSGGLSP RSDSIGEMTS SATTPPSMSP RGSVSGSQCK
DVCAILAEEI GVSMGEITND TDLGALGMDS LMSLAVLSRL REELELDLEG DFFVSHPNFS
SFKHMFQQGH GDEAEPETSA ELKQYRATST LLQGSPKSAL YTLFLLPDGS GSSFSYAPIN
AVRKDVCVFG LNCPWLKSAE KLVQFGLKGL ATLYVEEIRR RAPHGPYNLG GWSAGGICAY
EAAIQFTREG ETVERLILLD SPNPIGLEKL PARLFDFVNG LGLFGDGKAP DWLLAHFLAF
IDALDEWKPV PWDKALGGSS PPPMTYILWA EDGICKGTDA RPEYRDDDPR EMKWLLENRT
NFGGNNWDVL LGQQSLSIER IQDANHFTML RKGKNTERVA AFIRSIFG
