ID   PKS2_METAF              Reviewed;        2155 AA.
AC   A0A0B4FLB2;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   25-MAY-2022, entry version 32.
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=MAN_00842;
OS   Metarhizium anisopliae (strain ARSEF 549).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1276135;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 549;
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; AZNF01000001; KID71243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B4FLB2; -.
DR   SMR; A0A0B4FLB2; -.
DR   EnsemblFungi; KID71243; KID71243; MAN_00842.
DR   HOGENOM; CLU_000022_6_0_1; -.
DR   Proteomes; UP000031186; 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..2155
FT                   /note="Polyketide synthase 2"
FT                   /id="PRO_0000445747"
FT   DOMAIN          1649..1726
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:29958281"
FT   DOMAIN          1764..1838
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          1626..1654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1735..1765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1873..2149
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   COMPBIAS        1736..1764
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        1979
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         1798
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2155 AA;  234222 MW;  8F042E9663477939 CRC64;
     MQPHRVFIFG DQTGGFATGL QQLLLDKTNP SLVYFVDHAN LALRQELSRL PSTDREALPL
     IGSVQDILTL HKKGERNVVI DSILSTVYHL ACFIYKYGNA GCAYPNGQDI HVTGMCVGSL
     AAAAVSCSRS IGDVIVAGIV AIRAALRVGL RAHQAALLIS NRAAPHTHWS YAVSTESLRL
     DLIKDALEEF AQDMDTSPLS HPYISAIGLD SVTVSGPPSQ LQQFWRENTT FHKPIPIPIW
     APYHGPHIFG DSDVETIIES LHPIPKLSQQ APIISSGSGV MASQTLADLI RAALRDILLH
     RLDLPALVGH IKDIVRSSPN QDFSMTPIAT NAATGLVAAT AKAAGNKGSV DNEIMDAAAL
     AGSASRATSA KTHDSKIAII GMSGRFPEAA DLDSFWSLLE QGVDAYRPVP PDRFDAHAHH
     DETGRRKNTS KVLGGCWINQ PGLFDPKFFS ISPKEAEQSD PAQRLALQTA YEALEMAGVV
     PDRTQSTQRD RVGVFYGMVS DDWREINSGQ NIDTYFIPGG IRAFTPGRIN YHFKFSGPSI
     TVDTACSSSL AAIHVACNSL WRGDCDTAVA GGVNVLTNPD IFAGLDRGHF LSTTGNCKTF
     DDDADGYCRA DGVGTVILKR LEDAVMDKDP ILAILNSAYT NHSAEAVSIT RPHAGAQELI
     FSKLLRETGI HPHDVSYIEM HGTGTQAGDA TEMSSVLRTF APDTRRLSSQ TLHLGSAKSN
     VGHGEAASGV TSLIKVLLMM KHNTIPPHCG IKGRINHRFP TDLRERNVFI ASQPVAWNKP
     HTGSGKRRVF INNFSAAGGN SALLLEDAPA GENPETKDPR STHVVAVSAK SSTSLANNLK
     RLRDFVQDNI HDLDSLSKLS YTTTARRIHY PFRTAVTASS RDQLLQGIES VLLRDEMPKP
     CKSQKNIGFV FSGQGAQYAG MGRHLFQNNH TFRTQILACN QICLSQGFPS ILEIFKQDVD
     MNSLEPLLVQ LATTCLQMSL VSFWKSLGVT PDFCIGHSLG EYAALQAAGV LSVSDTIYLT
     GIRARMLQEK CSAGSHAMLA VRAPLARVNA LLDPAIHEVT CLNGPQDVVI GGRVADVEAL
     EKELAKQDIK AVKVSVPFAF HSTQVEPILG EFCDAARGVP FQTQTIPVVS TLLGEVVQPE
     AAGVFGPGYL KRHCREPVNF AAAVQAARDA NVIHAGTVFV EIGPHPVCLA LLKSNMGPDA
     VTLASLHRKD DGWKVLADTL AALYQSGLKI NWDEVHRDFA SCQEVLPLPS YSWDNKNYWI
     QYVHNWTLTK GDEPAAMAET TALQAQDGLT SSVQRIIRQT DGPGSLVTIV VQSDFGSARL
     ADVAQGHKVN GEMLCTSSLY AEIGMTLGRH LLEKYRPDLD GYSTEIKDMS VDKPLILKDE
     NKQTLFRAEV VHDKTTHTAT MSIYSVDSAG NKTVDHARCL LRFADPTSWL DEWERTYYLI
     DRSVRWLEER AEQGTDSLLS KGIVYKLFSS LVDYSPSFKG LQEVILNSGD REAAAKVRLQ
     AEKGDFDCNP MWIDSFGQLT GFLMNGHDFT GKDEVFINHG WRSMRCAKPF RKDAVYRTYI
     RMQHVEKTKY RGDLYIIEDG VIVAVFGGMT FLGMSRSLLN KVLPPRRGAE AINTPHPVAA
     AQQGMAASAK DTERRPLDIP TRAQRQPSSP QTGTMGRILA ILSKEVGLSM ETLTDDLVFT
     DYGVDSLLSL TITGRIREEL GLDMDSSIFT HYSTLGELKA FLGADQPDDA VACESSIGQH
     TPQTSDKGSG TLASQKTDGD TGPDTTLNRV CAIIAEEVGI SVQELSSSQD FQELGIDSLS
     SLTILSRVRE ELQLDLESDF FDTHPSFYAL QKALCGSEAS NGAPEANETT PSSDRLESDL
     RSITWQSGQN IVASPPHATS ILVSGSPSTA RMILVLFPDG SGSAASYGAL APKIRRDIAV
     YALNCPWRTN GEEILRLGVT LDQMVAKHLV EVGRILDSHQ RGRPGSSNAS VGLALGGWSA
     GGILALEAVR QLREAGVAVQ KMVLLDAPNP IGLQNPPPRM FHFLDELGIL GAGKGKAPAW
     VLRHFDAMVT LLKSYRPRRL GAEDAPKCLI VYAKDGICKD PNGPRMDTKP DDAREMLWLL
     YNRVDFSAEG WKTLVGPQNL AVGVVEDVNH FSMMNPGPKM VEMGNLIGDF LLGPS