PKS2_METRA
ID PKS2_METRA Reviewed; 2157 AA.
AC E9ET39;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 25-MAY-2022, entry version 57.
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=MAA_03239;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
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 GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
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 [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=25445307; DOI=10.1016/j.fgb.2014.10.018;
RA Chen Y., Feng P., Shang Y., Xu Y.J., Wang C.;
RT "Biosynthesis of non-melanin pigment by a divergent polyketide synthase in
RT Metarhizium robertsii.";
RL Fungal Genet. Biol. 81:142-149(2015).
RN [4]
RP INDUCTION.
RX PubMed=26714892; DOI=10.1111/1462-2920.13198;
RA Chen X., Xu C., Qian Y., Liu R., Zhang Q., Zeng G., Zhang X., Zhao H.,
RA Fang W.;
RT "MAPK cascade-mediated regulation of pathogenicity, conidiation and
RT tolerance to abiotic stresses in the entomopathogenic fungus Metarhizium
RT robertsii.";
RL Environ. Microbiol. 18:1048-1062(2016).
RN [5]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, 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 (PubMed:29958281). The product of
CC the Pks2 gene cluster is different from the one of Pks1 and has still
CC not been identified (PubMed:29958281). {ECO:0000269|PubMed:29958281}.
CC -!- INDUCTION: Expression is up-regulated in appressoria-forming germlings
CC on locust cuticle (PubMed:26714892, PubMed:29958281). Expression is
CC positively regulated by the Fus3 MAPK and negatively regulated by Opy2
CC (PubMed:29958281). {ECO:0000269|PubMed:26714892,
CC 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}.
CC -!- DISRUPTION PHENOTYPE: Does not affect conidial pigmentation.
CC {ECO:0000269|PubMed:25445307}.
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DR EMBL; ADNJ02000004; EFZ02010.2; -; Genomic_DNA.
DR RefSeq; XP_007819428.2; XM_007821237.2.
DR AlphaFoldDB; E9ET39; -.
DR SMR; E9ET39; -.
DR EnsemblFungi; EFZ02010; EFZ02010; MAA_03239.
DR GeneID; 19257525; -.
DR KEGG; maj:MAA_03239; -.
DR HOGENOM; CLU_000022_6_0_1; -.
DR Proteomes; UP000002498; 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_0000445752"
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 1626..1652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1859
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 1844..1859
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; 234630 MW; CA58DA5338F8B7FA CRC64;
MQPHRVFIFG DQTGGFATGL QQLLLDKTNP SLVYFVDHAN LALRQELSRL PSTDRETLPL
IGSVQDILTL HKKGERNVVI DSILSTVYHL ACFIYKYGNA GCAYPNRQDV HVTGMCVGSL
AAAAVSCSRS IGDVIVAGIV AIRAALRVGL RAHQAALLIS NRAAPHTHWS YAVSTESLRL
DLIKDALEKF AQDMDTSPLS HPYISAIGLD SVTVSGPPSH LHQFWRENTT FHKPIPIPIW
APYHGPHIFG DSDVETIIES LHPIPKLSQQ APIISSGSGV MASQTLADLI RAALRDILLH
RLDLPALVGH IKDIFRSSPN QDFAMTPIAT NAATSLVATT AKAAGNTGSV 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 ILAVLNSAYT NHSAEAVSIT RPHAGAQELI
FSKLLRETGI HPHDVSYIEM HGTGTQAGDA TEMSSVLRTF APDTGRLSSQ TLHLGSAKSN
VGHGEAASGV TSLIKVLLMM KHNTIPPHCG IKGRINHRFP TDLRERNVFI ASQPVAWNKP
HAGSGKRRVF INNFSAAGGN SALLLEDAPT DEHPETKDPR STHIVAVSAK SSTSLANNLK
RLRDFVQDNI HDLDSLSKLS YTTTARRIHY PFRAAMAVSS RDQLLQGIES VLLRDEMPKP
GKSQKNIGFV FSGQGAQYAG MGRHLFHNNH TFRTQILACN QICLSHGFPS ILEIFKQDVD
MNSLEPLLVQ LGTTCLQMSL VAFWKSLGVT PDFCIGHSLG EYAALQAAGV LSVSDTIYLT
GIRARMLQEK CSAGSHAMLA VRAPLARVNA LLDPAIHEVT CLNGPQDVVI GGRVADVEEL
EKELAKQDIK AVKVSVPFAF HSTQVEPILG EFCDAARGVP FQTQNIPVIS TLLGEVVQPE
ATGVFGPGYL KRHCREPVNF AAAVEAARDA NVIHAGTVFV EIGPHPVCLA LLKSNMGPDA
VTLASLHRKD DGWKVLADTL AALYQAGLKI NWDEVHRDFA SCQEVLPLPS YSWDNKNYWI
QYVHNWTLTK GDEPAATAET TALQALDGLT SSVQKIIRQT DGPGSLVTIV VQSDFGSARL
AEVAQGHKVN GEMLCTSSLY AEIGMTLGRQ LLEKYRPDLD GYSTEIKDMS VDKPLILKDE
NKRTLFRAEV VHDKSTHTAT MSIYSVDSAG NKTVDHARCL LRFADPTSWL DEWERTHYLI
DRSVRWLEER AEQGTDSLLS RGIVYKLFSS LVDYSPSFKG LQEVILNSGD REAAAKVRLQ
AKKGDFDCNP MWIDSFGQLT GFLMNGHDFT GKDEVFINHG WRSMRCAKPF RKDAVYRTYI
RMQHVEKTKY RGDLYIIEDG VIVAVFGGMT FLGMSRSLLN KVLPPRRGTD AINTAHPVAA
AQQGMAASAK DTERRPLDIP TRAQRQPSSA QTGTMGRILA ILSKEVGLSM ETLTDDLVFA
DYGVDSLLSL TITGRIREEL GLDMDSSIFT HYSTLGELKA FLGADQLPDD AVACESSNGQ
HTPQTSDKGS GTLAVQKTDD DTSPDMTLNR VCAIIAEEVG ISVQELSSSQ DFQELGIDSL
SSLTILSRVR EELQLDLESD FFDTHPSFYS LQKALCGSEA ASNGAPEANE TTPSSHRLES
DLRSITWQSG QNIVASPPHA TSILVSGSPS TARMILVLFP DGSGSAASYG ALAPKIRRDI
AVYALNCPWR TNGEEILRLG VTLDQMVAKH LVEVGRILDS HRHGRPGSAN ASVGLALGGW
SAGGILALEA VRQLGEAGVA VQKMVLLDAP NPIGLQNPPP RMFHFLDELG ILGAGKGKAP
AWVLRHFDAM VNLLKSYRPR RLGAEDAPKC LIVYAKDGIC KDPDGPRMDT KPDDAREMLW
LLYNRVDFSA EGWKTLVGQQ NLAVGVVDDV NHFSMMNPGP KMIEMGNLIG EFLLGPS
