ID   PKS2_METGA              Reviewed;        2157 AA.
AC   A0A0B4I1L1;
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=MGU_06677;
OS   Metarhizium guizhouense (strain ARSEF 977).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1276136;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 977;
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; AZNH01000023; KID86244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B4I1L1; -.
DR   SMR; A0A0B4I1L1; -.
DR   EnsemblFungi; KID86244; KID86244; MGU_06677.
DR   HOGENOM; CLU_000022_6_0_1; -.
DR   Proteomes; UP000031192; 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..2157
FT                   /note="Polyketide synthase 2"
FT                   /id="PRO_0000445750"
FT   DOMAIN          1649..1726
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:29958281"
FT   DOMAIN          1765..1839
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          1629..1653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1729..1765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1875..2151
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   COMPBIAS        1731..1761
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        1981
FT                   /note="For thioesterase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q03149"
FT   MOD_RES         1686
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1799
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2157 AA;  234311 MW;  4396D4AEFCB26974 CRC64;
     MQPHRVFIFG DQTGGFATGL QQLLLDKTNP SLVYFVDHAN LALRQELSRL PSTDRETLPL
     IGSVQDILTL HKKGERNVVI DSILSTVYHL TCFIYKYGNA GCPYPNGQDI HVTGICVGSL
     AAAAVSCSRS IGDVIVAGIV AIQAALRVGL RAHQAALLIN NRAAPHTHWS YAVSTESLRL
     DLIKDALAKF AQDMDTSPLS HPYISAIGLD SVTVSGPPSQ LHQFWRENTP SHKPIPIPIW
     APYHGPHIFG DSDVETIIES LHPIPKLSQQ APLISSGSGV MASQTLADLI RAALQDILLH
     RLDLPALVGH IKDIFRSSPN QDFAMTPIAT NAAAGLVAAT AKAAGNTGSV DNEIMDAAAL
     AGSASRATSA KTHDAKIAII GMSGRFPEAA DLDSFWSLLE QGVDAYRPVP PDRFDAHAHH
     DETGRRKNTS RVLGGCWINQ PGLFDPKFFS ISPKEAEQSD PAQRLALQTA YEALEMAGVV
     PDRTQSTQRD RVGVFYGMVS DDWREINSGQ NIDTYFIPGG IRAFTPGRIN YHFKFSGPSI
     TVDTACSSSL AAIHVACNSL WRGDCDTAVA GGVNVLTNPD IFAGLDRGHF LSTTGNCKTF
     DDDADGYCRA DGVGTVILKR LEDAVMDKDP ILAVLNSAYT NHSAEAVSIT RPHAGAQELI
     FSKLLRETGI HPHDVSYIEM HGTGTQAGDA TEMSSVLRTF ASDTSRLSNQ TLHLGSAKSN
     VGHGESASGV TSLIKVLLMM KHNTIPPHCG IKGRINHRFP TDLRERNVFI ASQPVAWNRP
     HAGSGKRRVF INNFSAAGGN SALLLEDAPA GEHPETKDPR STHIVAVSAK SSTSLANNLK
     RLKDFVQDNI YNLDSLSKLS YTTTARRIHY PFRAAMTASS RDQLLQGIES VLLRDEMPKP
     CKGQKNIGFV FSGQGAQYAG MGRHLFQNNH TFRTQILACN RICLSQGFPS ILEIFTQDVD
     MNSLEPLVFQ LGTTCLQTSL VSFWKSLGVT PDFCIGHSLG EYAALQAAGV LSVSDTIYLT
     GIRARMLQEK CSAGSHAMLA VRAPLARVNA LLDPGIHEVT CLNGPHDVVI GGRVADVEDL
     EKELAKEDIK AVKVSVPFAF HSTQVDPILG EFCAAARGVP FQTQNIPVIS TLLGEVVQPE
     TTGVFGPEYL KRHCREPVNF AAAVQAGRDA NLIHAGTVFV EIGPHPVCLA LLKSNMGPDA
     VTLASLHRKD DGWKVLADTL AALYRSGLKI NWDELHRDFA SCQEVLPLPS YSWDNKNYWI
     QYVHNWTLTK GDEPAAVAEA TALQAPDICT SSVQKIIQQT DGPGSLVTIV AQSDFGSARL
     AEVAQGHKVN GEMLCTSSLY AEIGMTLGRQ LLEKHRPDLQ GYSTEIQDMS VDKPLILKDQ
     NKQTLFRAEV VHDKSTHTAA MSIYSVDSAG NKTVDHARCL LCFADPNSWL DEWERTYYLI
     DRSVRWLEAR AEQGTDSLLS KGIVYKLFSS LVDYSPSFKG LQEVILNSGD REATAKVRLQ
     AEKGDFGCNP MWIDSFGQLT GFLMNGHDFT GKDEVFINHG WRSMRCAKPF RKDAVYRTYI
     RMQHVEKTKY RGDLYIIEDG VIIGVFGGMT FLGMSRSLLN KVLPPRRGAE AINTPHPVAA
     AQEGMAASAK DTERRPLDIP TRAQRQPNSP PTGTLGRILA ILSEEVGLSL ETLTDDLVFA
     DYGVDSLLSL TITGRIREEL DLDMDSSIFT HYSTLGELKE FLGADQNPDD AVACESSNGQ
     HTPQTSDKGS GTLAAQKPDD DTGSDTTLHR VCAIIAEEVG ISVQELSSSQ DFQELGIDSL
     SSLTILSRVR EELQLDLESD FFDTHPSFCS LQKALCGTEA ASNGAPEANE TTPSSHRLES
     DLRTITWHSG QNIVASPPHA TSILVSGSPS TARMILVLFP DGSGSAASYG ALAPKIRRDI
     AVYALNCPWR TNGEEILRLG VSLDQMVAKH LVEVGRILDR HQHCRAGSGN ASVGLALGGW
     SAGGILALEA VRQLREAGVA VQKMVLLDAP NPIGLQNPPP RMFHFLDELG ILGAGKGKAP
     AWVLRHFDAM VTLLKSYRPR RLGAEDAPKC LIVYARDGIC KDPDGPRMDT KPDDAREMLW
     LLYNRVDFSA EGWKSLVGQQ NLAVGVVEDV NHFSMMNPGP KMAEMGDLIG EFLLGPS