ID BA17A_METAN Reviewed; 3068 AA.
AC P0DUT7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 27-NOV-2024, entry version 16.
DE RecName: Full=Highly reducing polyketide synthase 17 {ECO:0000303|PubMed:33991663};
DE Short=HR-PKS 17 {ECO:0000303|PubMed:33991663};
DE EC=2.3.1.- {ECO:0000269|PubMed:33991663};
DE AltName: Full=PKS17 biosynthesis gene cluster protein Ba17a {ECO:0000303|PubMed:27801295};
DE AltName: Full=Polyenoic acids biosynthesis gene cluster protein Ba17a {ECO:0000303|PubMed:33991663};
GN Name=Ba17a {ECO:0000303|PubMed:33991663};
GN Synonyms=PKS17 {ECO:0000303|PubMed:27801295}; ORFNames=MANI_025650;
OS Metarhizium anisopliae (Entomophthora anisopliae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=5530;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25263348; DOI=10.1186/1471-2164-15-822;
RA Staats C.C., Junges A., Guedes R.L., Thompson C.E., de Morais G.L.,
RA Boldo J.T., de Almeida L.G., Andreis F.C., Gerber A.L., Sbaraini N.,
RA da Paixao R.L., Broetto L., Landell M., Santi L., Beys-da-Silva W.O.,
RA Silveira C.P., Serrano T.R., de Oliveira E.S., Kmetzsch L., Vainstein M.H.,
RA de Vasconcelos A.T., Schrank A.;
RT "Comparative genome analysis of entomopathogenic fungi reveals a complex
RT set of secreted proteins.";
RL BMC Genomics 15:822-822(2014).
RN [2]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=27801295; DOI=10.1186/s12864-016-3067-6;
RA Sbaraini N., Guedes R.L., Andreis F.C., Junges A., de Morais G.L.,
RA Vainstein M.H., de Vasconcelos A.T., Schrank A.;
RT "Secondary metabolite gene clusters in the entomopathogen fungus
RT Metarhizium anisopliae: genome identification and patterns of expression in
RT a cuticle infection model.";
RL BMC Genomics 17:736-736(2016).
RN [3]
RP FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=33991663; DOI=10.1016/j.fgb.2021.103568;
RA Sbaraini N., Hu J., Roux I., Phan C.S., Motta H., Rezaee H., Schrank A.,
RA Chooi Y.H., Christian Staats C.;
RT "Polyketides produced by the entomopathogenic fungus Metarhizium anisopliae
RT induce Candida albicans growth.";
RL Fungal Genet. Biol. 152:103568-103568(2021).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of (2Z,4E,6E,10E)-9-hydroxydodeca-
CC 2,4,6,10-tetraenoic acid (BAA), (2E,4E,6E,10E)-9-hydroxydodeca-
CC 2,4,6,10-tetraenoic acid (BAB), and (2Z,4E,6E)-octa-2,4,6-trienedioic
CC acid (PBA) (PubMed:33991663). The highly reducing polyketide synthase
CC Ba17a is sufficent to produce PBA and BAA (PubMed:33991663). The still
CC to be characterized protein Ba17b leads to an increased production of
CC BAA as well as to the production of the new compound BAB
CC (PubMed:33991663). BAA does not possess insecticidal activity against
CC G.mellonella larvae, however, both BAA and BAB increase the growth of
CC Candida albicans and BAA can mitigate the fungicidal effects of
CC fluconazole over C.albicans, suggesting that generalist pathogens such
CC as M.anisopliae, can potentially manipulate the yeast microbiota found
CC in arthropods (and anywhere else) by the activity of compounds as BAA
CC and BAB (PubMed:33991663). {ECO:0000269|PubMed:33991663}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:33991663}.
CC -!- INDUCTION: Expression is induced under mimicked-infection conditions.
CC {ECO:0000269|PubMed:27801295}.
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 dehydratase (DH) domain that
CC reduces hydroxyl groups to enoyl groups; an enoylreductase (ER) domain
CC that reduces enoyl groups to alkyl groups; a ketoreductase (KR) domain
CC that catalyzes beta-ketoreduction steps; an acyl-carrier protein (ACP)
CC that serves as the tether of the growing and completed polyketide via
CC its phosphopantetheinyl arm; and a C-terminal choline/carnitine
CC acyltransferase (cAT) domain that acts like a thioesterase domain,
CC using water as a nucleophile to release the polyketide product.
CC {ECO:0000305|PubMed:33991663}.
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DR EMBL; JNNZ01000213; KFG78606.1; -; Genomic_DNA.
DR SMR; P0DUT7; -.
DR VEuPathDB; FungiDB:MAN_00012; -.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:TreeGrafter.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase_dom.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR049900; PKS_mFAS_DH.
DR InterPro; IPR050091; PKS_NRPS_Biosynth_Enz.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF22; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..3068
FT /note="Highly reducing polyketide synthase 17"
FT /id="PRO_0000453547"
FT DOMAIN 100..526
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348,
FT ECO:0000305|PubMed:33991663"
FT DOMAIN 1027..1334
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2345..2423
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:33991663"
FT REGION 627..938
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT REGION 1027..1311
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT REGION 1027..1160
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1179..1334
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1735..2037
FT /note="Enoylreductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT REGION 2062..2240
FT /note="Catalytic ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT REGION 2831..3062
FT /note="Choline/carnitine acyltransferase (cAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT ACT_SITE 274
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 410
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 449
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 721
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT ACT_SITE 1059
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1247
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 2383
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3068 AA; 334489 MW; B6054A700DE67DF9 CRC64;
MLQKSYHGVV SQASYDNTCG RGSQIRRDRS RAGVRFNTEY NPVLLTVSKQ IAQDGEGYHC
RANLINKITT KQQLAFISEL QPTQSTLKVL PVADGRKMPI EPIAIVGASC RLPGSSNSLD
SLWELLADGG EAWSSVPADR FNEAAFHHPN ASDPNGTNNH QGGHFIDGDI RDFDHAFFHL
SPQHAAAMDP QQRILLELVY EAFESAGWAR EACAGSRTAV FAAIFGTDYD RNLCKDLLDL
PVYHSVGTGI AILANRISHA FDLRGPSLTL DTGCSGGLVA LHEACQSLRN GESDAALVAA
ANLQLMPDHY IGMSSQHMVS STGRCYPFDL RGDGYGRGEG FAVVALKRLS DALRDQDPIR
SVILNSGINQ DGYTASGITH PNRVAQADLI RDTYDRVHLH PQDTVYVEAH GTGTVAGDNE
ELAAIAEVFA GPDRSLPLHV GSNKGSIGHT ESTSGLASLL KVILMLDHQV IPPVAGFTNP
KPGLPLDRIK IPTQRLPWPL TEGMVPRISI NSFGYGGTNA HAIMERGPRT YDASCNTTPT
YSPRLFVLSA NNKGSLRSLL ESYVNWIQKH PNIPLADISY TLCHRRSALP WRFSCVADSE
SSLLDTLERG VKLISTRPPP SKRQVIYVFT GQGAQWAGMG HELLLETTPS SVFRDSIRTS
RDILYELGAT WDLEAELLGQ DGGGRINKAE LAQPATTAVQ IGIVMLLRSQ GVRPWAVVGH
SSGEIAAAYA AGRLSHRMAL RVAFHRGFMA GVSKDRGLPP GAMLSIGLGQ GDAAPYLHDL
THGEAVIACI NSPNSVTVSG DAAAVDEVMA RIIARGDGTF CRKLHVDTAY HSHHMRAVAD
EYCIRLGDLD LGIDERISAP GGQRDKEEVK YFSSNSGLAW VSGFAASYWV DNLISPVRFS
DAIQTVAREH HKHNGGLALF VEIGPHAALA GPIRQCLAAS NVPKLEYNYL SALKRGAGAV
ETMLQVVGHL FERGVRVNFD EISALTPGFH TAAVRPDLPS YCWDYSSKHW HESRLSREYR
MRREPYHHLL GVRMTELAST EPRWRHMVGL ATLPWLAHHI IDGLIIFPGA CYVCMVIEAV
RQLAKEQYSD QALEAVSLRD VSFLRALVVP DAPSRVEMQL SLKHRADASP LGFTFSVTAL
SDGKWHVFCT GVVEGVMTLD KPETEPVMLD PRPKQDWLNR TMVIPEELYN EMTADGNTYG
PSFRGLSSLT MSTDGSMATA VIEVPDIAAS MPAQYQASHI LHPTTLDSMF HVGIPMMKRR
HGAGSVMPVH IGELLISTQT PALNSQGSKL DVSAKLTSSH FRASNIDMTI VSGGFPVMYA
SAIESRSLAA HVDGAHGTQD EHGICYELAW RCDLNFLRTS DLTRSSILAD LVSFLCFKTA
HLSIAELGES PGVLAPAFLA AVGVHRGTVT SYDVVERGNQ PIDEGCKRLT GYPIRRRALD
PDSSLESQGF APNTYDVVLA SDLGSLCYVS TLVKNDGVVV VVLKPGSDDN WQSTLRKTWP
SHDIQLTVVD SVNGNRIILA RNDKTKDSHS SSRVHILTHS ALQTTPSWAT ALIGKLHEMG
YEMSSGSLSQ DVIQRSSDAR NTCIMVIDDL AQPILSDRAC FNSAITLLRQ EHRIIWLSLD
SPSSMHQITG VARTAHAEND NLRLTVVHAA LEAIGSPPLV DLLCHCLTYA QNRDSLAPYE
REYRVSRDAA VLIPRLRSSD CLNRAIRASE KASEPSSNIE TEPHHYINTT RSLALGPVQS
SKGDGDIVFI DSHTVELAEG QVEVETEAFV LSKSQNLTSS QLGEYSGIVR RVGKGVRDFS
PGDAVVALAL DGVVGANHAR VPSSHVSRRP DSLSPAVAAA LFLPTIAASY AIHHLAQISK
GKSIVLIHGV LTDIGRASVA VARVLGATIT ATAISRQEAL EITQQLNIQL ENIIVSRPSL
LRPQLDELFQ LDAIIHISKD SVPVAAWSCL KPFGQVVVFN SSSSIAFPSP PPENATIHYC
HITNLVQAQP DRLADLVSLA APALERIPFK GIDLCIQDVA QVPEAIRLVR QGGKVILQAS
PSSLVRTVIP SSISMDWEAV DAAYVVAGGM GDLGRRLLLL MARRGAMHLV TLSRRSIEPE
DHRSFQGQLQ LVQPGCRLYC LVCDITSESS VQNAADTLTR TGVPPVRGVI QSAVTLHDRT
LETMTFDDFF AVAHAKVDGT LVLERVFASP HLHFFLMLSS AVNITGASGQ ANYNAGNAVQ
DAIAHDRGPG FLSMNIGWIE DAINTSNNKT ILQGLWRTGL RPILGQELSR YFDHLLGAAS
SHSRMRQAII GFNAASLSHT SASNSNVHSA MFCHIRGSLA AEESSSSTNN VRSFGEVVEG
GDLDTIIDFI SSAITRRLMT LISMDDDQIK DRNGSILDLG LDSLVAIELR NWITREFKSP
LQSSEILTDQ PIRDLAEKVA SRSSLLASGL DKEVPAGSLE NGDVEDRHSA GAIRPSTSAH
STVKYVSENL PPLPLPPLAD TLRLFEDSRR AIDTANHRRN TSDAVHDFLK GPGPRLYNSL
QETNSDVIAD AYDRQVYLER REPLPEQGPF IFIHSIQAPV HSQARRAAIL TIAAFDFIRL
LARGDIATDT LHGEPITTEG RNWLFYATRR PGIGIDRMER HVPNNTVAVL RRGHVFQLRL
PDVEQALDML AVTRVYDDIL AASCDAIPPI CTLTADERDS WALFRLDLER HPQNAAVLAC
IDTAAFVMCL DDESPTSSGE RYTQFMINGA HRPFANRWLD KTLQFAVTAN GISAEIYEHS
KLDGIDTNRL HAHIARAILA HPPSETADIS SFSSPYAVQE LMWEPSSATL QRIEHVRTQC
QVYGPLDHQV FDVASLGLRS LRGFRLQPNA TAHLTVLLAL YLVDGEIRPA WEKVSLGTFA
RGRVEWVQTI SPAARAFIEA AAASYTDSNN RTRVRALLHQ ATSTHSRSLV AAGRGLGAVR
ALYALRGAAQ EQEKELPELF RTHSWDATRR GGPGQDVKLG FMRLAPDDDA NGNVGATPGD
DDINGRWDEA GFLVCGERGV YVHCNVWEKH ARFAASGRPA YVTKLCKAMR RASCMITSLL
EDPSKRPT
//
