ID   PKS2_METBS              Reviewed;        2157 AA.
AC   A0A0B4H8J1;
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 2 {ECO:0000303|PubMed:29958281};
DE            EC=2.3.1.- {ECO:0000305|PubMed:29958281};
GN   Name=Pks2 {ECO:0000303|PubMed:29958281}; ORFNames=MBR_03974;
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, 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; AZNG01000004; KID76039.1; -; Genomic_DNA.
DR   RefSeq; XP_014545211.1; XM_014689725.1.
DR   AlphaFoldDB; A0A0B4H8J1; -.
DR   SMR; A0A0B4H8J1; -.
DR   EnsemblFungi; KID76039; KID76039; MBR_03974.
DR   GeneID; 26241244; -.
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; 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_0000445749"
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          1622..1655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1734..1762
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        1734..1752
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;  234458 MW;  CA1B765E221CDFB5 CRC64;
     MQPHRVFLFG DQTGGFATGL QQLLLDKTNP SLVYFVDHAN LALRQELSRL PSTDRETLPL
     IGSVQDILTL HKKGERNVVI DSILSTVYHL ACFIYKYGNA GCAYPNGQNI HVTGMCVGSL
     AAAAVSCSRS IGDVIVAGIV AIRAALRVGL RAHQAALLTS NRAAPHTHWS YAVSTESLRL
     DLIKDALEKF AQDMDTSPLS HPYISAIGLD SVTVSGPPSQ LHQFWRENTT FHKPIPIPIW
     APYHGPHIFG DIDVETIIES LHPIPKLSQQ APIISSGSGV MASQTLADLI RAALRDILLH
     RLDLPALVGH IKDIFRSSPN QDFSMTPIAT NAATGLVAAT AKAAGNTGSV DNEIMDAAAL
     AGSASRATSA KTHDSKIAII GMSGRFPEAA DLDSFWSLLE QGVDAYRPVP PDRFDAHAHH
     DETGRRKNTS KVLGGCWINQ PGLFDAKFFS ISPKEAEQSD PAQRLALQTA YEALEMAGVV
     PDRTQSTQRD RVGVFYGMVS DDWREINSGQ NIDTYFIPGG IRAFTPGRIN YHFKFSGPSI
     TVDTACSSSL AAIHVACNSL WRGDCDTAVA GGVNVLTNPD IFAGLDRGHF LSTTGNCKTF
     DDDADGYCRA DGVGTVVLKR LEDAVMDKDP ILAVLNSAYT NHSAEAVSIT RPHAGAQERI
     FSKLLRETGI NPHDVSYIEM HGTGTQAGDA TEMSSVLRTF APDSGRLSNQ TLHLGSAKSN
     VGHGESASGV TSLIKVLLMM KHNMIPPHCG IKGRINHRFP TDLRERNVFI ASQPVAWNRP
     HAGSGKRRVF INNFSAAGGN SALLLEDAPA GEHPETKDPR STHVVAVSAK SATSLANNLK
     RLRDFVQDNI HDLDSLSKLS YTTTARRIHY PFRAAMTASS GDQLLQGIES VLLRDEMPKP
     RKSQKNIGFV FSGQGAQYAG MGRHLFQNNH TFRTQILACN QICLSQGFPS ILEIFKQDVD
     MNSLEPLVVQ LATTCLQMSL VSFWKSLGVT PDFCIGHSLG EYAALQAAGV LSVSDTIYLT
     GIRARMLQEK CSAGSHAMLA VRAPLARVNA LLDPAIHEVT CLNGPQDVVI GGRVADVEEL
     ERELAKQDIK AVKVSVPFAF HSTQVEPILG EFCDAARGVP FQTQTIPVIS TLLGEVVHPE
     TTGVFGPGYL KRHCREPVNF AAAVQAARDA NLIHAGTVFV EIGPHPVCSA LLKSNMGPDA
     VTLASLHRKD DGWKVLADTL AALYQAGLKI NWDELHRDFA SCQEVLPLPS YSWDNKNYWI
     QYVHNWTLTK GDEPAAMAEA TALQAPDGLT SSVQKIIRQT DGPGSLVTIV VQSDFGSARL
     ADVAQGHKVN GEMLCTSSLY AEIGMTLGRQ LLEKYRPDLQ GYSTEIQDMS VDKPLILKDE
     NKQTLFRAEV VHDKSTHTAS MSIYSVDSAG NKTVDHARCL LRFADPNSWL EEWERTYYLI
     DRSVHWLEER AEQGTDSLLS RGIVYKLFSS LVDYSPSFKG LQEVILNSGD REAAAKVRLQ
     AEKGDFDCNP MWIDSFGQLT GFLMNGHDFT GKDEVFINHG WRSMRCAKPF RKDAVYRTYI
     RMQHVEKTKY RGDLYIIEDG VIIAVFGGMT FLGMSRSLLN KVLPPRRGAE AINTPHPVAA
     APQGMAASAK DTERRPLDIP TRAQRQPSSP QTGTMGRILA ILSEEVGLSM EILTDDLVFA
     DYGVDSLLSL TITGRIREEL GLDMDSSIFT HYSTLGELKA FLGADQLPDD AVACESSNGQ
     HTPQTSDKGS GTLAAQKPDD DIGPDTTLNR VCAIIAEEVG ISVQELSSSQ DFQELGIDSL
     SSLTILSRVR EELQLDLESD FFDTHPSFYS LQKALCGTGA ASNGATEANE TTPSSHRLES
     DLRSITWQSG QNIVASPPHA TSILVSGSPS TARMILVLFP DGSGSAASYG ALAPKIRRDI
     AVYALNCPWR TNGEEILRLG VTLDTMVAKH LVEVGRILDS HRHGRPGSGN SSVGLALGGW
     SAGGILALEA VRQLGEAGVA VQKMVLLDAP NPIGLQNPPP RMFHFLDELG ILGAGKGKAP
     AWVLRHFDAM VNLLKSYRPR RLEAEDAPKC LIVYARDGIC KDPDGPRMDT KPDDAREMLW
     LLYNRVDFSA EGWKTLVGQQ NLAVGVVEDV NHFSMMNPGP KMVEMGNLIG EFLLGPS