PKS2_METMF
ID PKS2_METMF Reviewed; 2158 AA.
AC A0A0B4I1J8;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Polyketide synthase 2 {ECO:0000303|PubMed:29958281};
DE EC=2.3.1.- {ECO:0000305|PubMed:29958281};
GN Name=Pks2 {ECO:0000303|PubMed:29958281}; ORFNames=MAJ_07522;
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297;
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, FUNCTION, 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 Pks2 gene cluster that
CC mediates the formation of infectious structures (appressoria), enabling
CC these fungi to kill insects faster (Probable). The product of the Pks2
CC gene cluster is different from the one of Pks1 and has still not been
CC identified (Probable). {ECO:0000305|PubMed:29958281}.
CC -!- INDUCTION: Expression is up-regulated in appressoria-forming germlings
CC on locust cuticle. {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}.
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DR EMBL; AZNE01000049; KID96466.1; -; Genomic_DNA.
DR RefSeq; XP_014575460.1; XM_014719974.1.
DR AlphaFoldDB; A0A0B4I1J8; -.
DR SMR; A0A0B4I1J8; -.
DR EnsemblFungi; KID96466; KID96466; MAJ_07522.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OrthoDB; 68112at2759; -.
DR Proteomes; UP000031176; 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 2: Evidence at transcript level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat;
KW Transferase.
FT CHAIN 1..2158
FT /note="Polyketide synthase 2"
FT /id="PRO_0000445751"
FT DOMAIN 1649..1727
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29958281"
FT DOMAIN 1766..1840
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29958281"
FT REGION 7..244
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT REGION 377..810
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT REGION 908..1213
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT REGION 1290..1605
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT REGION 1734..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..2152
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT COMPBIAS 1734..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 546
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 998
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1982
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1687
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1800
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2158 AA; 234196 MW; 52B5C69B23D15374 CRC64;
MQPHRVFIFG DQTGGFATGL QQLLLDKTNP SLVYFVDHAN LALRQELSRL PSTDRETLPL
IGSVQDILTL HKKGERNVVI DSILSTVYHL ACFIYKYGNA GCPYPNGQDI HVTGMCVGSL
AAAAVSCSRS IGDVIVAGIV AIRAALRVGL RAHQAALLIS NRAAPHVHWS YAVPTESLRL
DLIKDGLAKF AQDMDTSPLS HPYISAVGLD SVTVSGPPSQ LHQFWRENTA FHKPMPIPIW
APYHGPHIFG DGDVETILES LRPIPKLSQQ APLISSGSGV MASQTLAGLI RAALRDILLH
RLDLPGLVGH IQAIFKSSPN QDFSMTPIAT NAATSLVAAT AKDAGNTGSV DNEIMDAVAL
AGSASQATSA KTHDSKIAII GMSGRFPEAA DLDSFWSLLE QGVDAYRQVP PDRFDAHAHH
DETGRRKNTS RVLGGCWINQ PGLFDAKFFS ISPKEAEQSD PAQRLALQTA YEALEMAGVV
PDRTQSTQRD RVGVFYGMVS DDWREINSGQ NIDTYFIPGG IRAFTPGRIN YHFKFSGPSI
TVDTACSSSL AAIHVACNSL WRGDCDTAVA GGVNVLTNPD IFAGLDRGHF LSTTGNCKTF
DDDADGYCRA DGVGTVILKR LEDAVMDKDP ILAVLNSAYT NHSAEAVSIT RPHAGAQELI
FSKLLRETGI HPHDVGYIEM HGTGTQAGDA TEMSSVLRTF APGTGRLSSQ PLHLGSAKSN
IGHGESASGV TSLIKVLLMM KHNTIPPHCG IKGRINHRFP TDLRERNVFI ASQPVPWNKP
LAGSGKRRVF INNFSAAGGN SALLLEDAPA GELPETKDPR STHIVAVSAK SSTSLANNLK
RLRDFVQDNI HSLDSLSKLS YTTTARRIHY PFRAAVTASS RDQLLQGIES VLLRDEMPKP
RKSQKNIGFV FSGQGAQYAG MGRHLFQNNH AFRTQILACN QICRSQGFPS ILEIFEQDVD
VNSLEPLLVQ LGTTCLQMSL VSFWKSLGVT PDFCIGHSLG EYAALQAAGV LSVSDAIYLT
GTRARMLQEK CSAGSHAMLA VRAPLARVNA LLDPAIHEVT CLNGPRDVVV GGRVADVEEL
EKELAKQDVK AAKVSVPFAF HSTQVDPILG EFCAAARGVP FQTQSMPVIS TLLGEVVQPE
TTGVFGPEYL KRHCREPVDF AAAVRAGRDA NLIHAGTVFV EIGPHPVCLA LLKSNMGPDA
VTLASLHRKD DGWKVLADTL AALYLSGLKI NWDELHRDFA SCQEVLPLPS YCWDNKNYWI
QYVHNWTLTK GDEPAAMAET PALQAPESLT SSVQKIIRQT DGPGSLVTIV AQSDFGSARL
AEVARGHKVN GEMLCTSSLY AEIGMTLGRQ LLEKYRPDLQ GSSTEIQDMS VDRPLILKDE
NKQTLFRAEV VHDKSTPTAT MSIYSVDSAG NKTVDHARCL LRFADPTSWL DEWERTYYLI
DRSVRWLEAR AEQGTDSLLS KGIVYKLFSS LVDYSPSFKG LQEVILNSGD REATAKVRLQ
AERGDFDCNP MWIDSFGQLT GFLMNGHDFT GKDEVFINHG WRSMRCAKPF RKDAVYRTYI
RMQHVEKTKY RGDLYIIEDG VVIAVFGGMT FLGMSRGLLN KVLPPRRGAE AINTPHSVAA
AQEGMAASAK DAERRPVDIP TRVQRQPSSS SPTGTMGRIL VMLAEEVGLS LETLTDDLVF
ADYGVDSLLS LTITGRIREE LGLDMDSSIF THYSTLGELK AFLGADQHPD DAVACESSNG
QHTPQTSDKG SGTLAASKPD DDTGSDTTLH RVCAIIAEEV GISVQELSSS QDFQELGIDS
LSSLTILSRV REELQLDLES DFFDTHPSFC SLQKALCGTE AASNGAPEAN ETTPSSHRLE
SDLRTITWQS GQNIVASPPH ATSILVSGSP STARMILVLF PDGSGSAASY GALAPKIRRD
TAVYALNCPW RTNGEEILRL GVSLDQMVAK HLVEVGRILD SHQHGRPGSG NASVGLALGG
WSAGGILALE AVRQLREAGV AVQKMVLLDA PNPIGLQNPP PRMFHFLDEL GILGAGKGKA
PAWVLRHFDA MVTLLKSYRP RRLGAEYAPK CLIVYARDGI CKDPDGPRMD TKPDDAREML
WLLYNRVDFS AEGWKSLVGQ QNLAVGVVED VNHFSMMNPG PRMAEMGDLI GEFLLGPS
