ID   PKS2_METAQ              Reviewed;        1861 AA.
AC   E9EHG2;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=MAC_09310;
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   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 (PubMed:29958281). Expression is also up-regulated
CC       during conidiation (PubMed:29958281). {ECO:0000269|PubMed:29958281}.
CC   -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC       catalyzes repeated decarboxylative condensation to elongate the
CC       polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC       and transfers the extender unit malonyl-CoA; a product template (PT)
CC       domain 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. Lacks the starter unit:ACP transacylase (SAT)
CC       that selects the starter unit. {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; GL698613; EFY84645.1; -; Genomic_DNA.
DR   RefSeq; XP_007815650.1; XM_007817459.1.
DR   AlphaFoldDB; E9EHG2; -.
DR   SMR; E9EHG2; -.
DR   STRING; 92637.XP_007815650.1; -.
DR   EnsemblFungi; EFY84645; EFY84645; MAC_09310.
DR   GeneID; 19253621; -.
DR   KEGG; maw:MAC_09310; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_6_0_1; -.
DR   InParanoid; E9EHG2; -.
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; -; 1.
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; 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; 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; 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   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;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..1861
FT                   /note="Polyketide synthase 2"
FT                   /id="PRO_0000445748"
FT   DOMAIN          1356..1433
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:29958281"
FT   DOMAIN          1472..1546
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:29958281"
FT   REGION          112..528
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   REGION          626..931
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   REGION          1008..1312
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   REGION          1441..1470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1582..1855
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   COMPBIAS        1441..1464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        264
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        716
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1685
FT                   /note="For thioesterase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q03149"
FT   MOD_RES         1393
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1506
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1861 AA;  202972 MW;  2C0351B35326BAC0 CRC64;
     MPKLSQQAPL VSSGSGVIAS QTFADLIRAA LRDILLHRLD LPALVGHLTG IFGLSSNESF
     VITPVSTNVA TGLVAATAKA VGKTGSVDNE IMEAVALAGS RGTSARTHDS KIAIIGMSGR
     FPEAADLDSF WSLLVQGVDA YRPVAPDRFD AHAHYDETGR RKNTSKVLGG CWINQPGLFD
     PKFFSISPKE AEQSDPAQRL ALQTAYEALE MAGMVPDRTQ STQRERVGVF YGMFTQGGIR
     AFTPGRINYH FKFSGPSITV DTACSSSLAA IHVACNSLWR GDCDTAVAGG VNVLTNPDIF
     AGLDRGHFLS TTGNCKTFDD DADGYCRADG VGTVILKRLE DAIMDKDPIL AVLNSAYTNH
     SAEAVSITRP HAGAQELIFS KLLRETGIHP HDVSYIEMHG TGTQAGDATE MSSVLRTFAP
     DTGRLSNQTL HLGSAKSNVG HGESASGVTS LIKVLLMMKH NTIPPHCGIK GRINHRFPTD
     LRERNVFIAS QPVAWDKPHS GSGKRRVFIN NFSAAGGNSA LLLEDAPTRQ HPETKDPRST
     HIVAVSAKSS TALVNNLKRL KVFVQDNIHN LDLLAKLSYT TTARRIHYPF RAAITASSSD
     QLLQGIESIL LRDESTKPAT SQKNIGFVFS GQGAQYAGMG RHLFQNNETF RTQVLACNQI
     CLSQGFPSIL DIFNQGVEMN NLEPLVVQLG TTCLQMSLVS FWKSLGVTPD FCIGHSLGEY
     AALQAAGVLS VSDTIYLTGI RARLLQKKCS AGSHAMLAVR APLAQVHGFF NPSIHEVTCL
     NSPHDVAIGG LVADIEDLER ELAENNIEAV KVSVPFAFHS TQVEPILDEF CAAAESVQFQ
     TQRIPVISTL LGEVVLPEAK AVFGPEYLKR HCREPVNFTA AAQAGKDANI INSASVFIEI
     GPHTVCSALL KSNIGPNAVT LPSLHRKDDG WKVLADTLAG LYHSGLRINW DEFHRDFESC
     QEVLQLPSYC WDNKNYWIQY VHNWTLTKGD PPATTAQTPA LELPENSTSS VQKVIQQTDG
     PGPFVTIVVQ SDFGSPRLAE VAEGHKVNGE MLCTSSLYAE IGMTLGRQLL EKYRPDLQGY
     STEIEDMSVD KPLILKEKNK ETLFRAEVVH DKSTLTAAMS IYSVDSAGKK TVDHAHCILR
     FADPKSWLDE WERTYYSIER SVRWLEARVE QGTDSLLSKG IVYKLFSSLV DYSPSFKGLQ
     EVILNSSDRE ATAKVRLQAE KEDFDYNPMW IDSFGQLTGF LMNGHDFTEK DQVFINHGWR
     SMRCAKQFRK DAVYRTYICM QNVDKTKYCG DLYIIEDGVI IAVFGGMTVL PPRRGADAIH
     TPNPVAAAPA GLVASTKAHV RRPLDIPTRA QRQASSPQSG AIHRILVILA EEVGLSLETL
     TDDLVFADYG VDSLLSLTIT GRIREELDLD VDSSTFTNCS TLGELRLFLA ADQKLDDAVA
     CESSNGQHTP QTSDKGSGTL TAQKPDHDTD SEMTLNRVCA IIAEEVGISV EELSSSQDFQ
     ELGIDSLSAL TILSRVREEL QLDLESDFFD THPSFYSLQK TLRGTEGASN RTLEPNGAIP
     SRHDLKSDLG NIEWQSGQNI VASAPHATSI LVSGSPSTAR MILVLFPDGS GSAASYGALA
     PKIRKDIAVY ALNCPWRTNG EEILRLGVSL DQMVAKHLIE VRRILDNHQQ SRLNGSIDLA
     LGGWSAGGIL AIEGVRQLRQ TGIVVQKLVL LDAPNPIGLQ NPPPRMFHFL DELGILGAGT
     GKAPTWVLQH FDAMVNLLKS YRPRPLSAES APKSLIVYAK DGVCKDPKGP QMDTKPDDAR
     EMLWLLYDRV DFSAEGWKSL VGQQNLVVGV VEDVNHFSMM NPGPKIIEMS NLIGDFLLGL
     N