PKS81_PSEFD
ID PKS81_PSEFD Reviewed; 1762 AA.
AC M3A326;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Non-reducing polyketide synthase PKS8-1 {ECO:0000303|PubMed:27388157};
DE EC=2.3.1.- {ECO:0000305|PubMed:27388157};
DE AltName: Full=PKS8-1 gene cluster protein PKS8-1 {ECO:0000303|PubMed:30735556};
GN Name=PKS8-1; Synonyms=PksIII {ECO:0000303|PubMed:27513322};
GN ORFNames=MYCFIDRAFT_34361;
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2]
RP IDENTIFICATION.
RX PubMed=27513322; DOI=10.1371/journal.pgen.1005904;
RA Chang T.C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL PLoS Genet. 12:e1005904-e1005904(2016).
RN [3]
RP IDENTIFICATION, FUNCTION, AND DOMAIN.
RX PubMed=27388157; DOI=10.1371/journal.pone.0158471;
RA Noar R.D., Daub M.E.;
RT "Bioinformatics prediction of polyketide synthase gene clusters from
RT Mycosphaerella fijiensis.";
RL PLoS ONE 11:e0158471-e0158471(2016).
RN [4]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=30735556; DOI=10.1371/journal.pone.0212229;
RA Noar R.D., Thomas E., Daub M.E.;
RT "A novel polyketide synthase gene cluster in the plant pathogenic fungus
RT Pseudocercospora fijiensis.";
RL PLoS ONE 14:e0212229-e0212229(2019).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of an emodin derivative that may be
CC involved in black Sigatoka disease of banana (PubMed:27513322,
CC PubMed:27388157, PubMed:30735556). The pathway begins with the
CC synthesis of atrochrysone thioester by the polyketide synthase PKS8-1
CC (Probable). The atrochrysone carboxyl ACP thioesterase
CC MYCFIDRAFT_190111 then breaks the thioester bond and releases the
CC atrochrysone carboxylic acid from PKS8-1 (Probable). The decarboxylase
CC MYCFIDRAFT_34057 then catalyzes the concerted decarboxylation-
CC elimination required to convert atochrysone carboxylic acid into emodin
CC anthrone, which is further oxidized to emodin by the anthrone oxygenase
CC MYCFIDRAFT_34418 (Probable). The functions of the other tailoring
CC enzymes as well as the final product of the cluster have still to be
CC identified (Probable). {ECO:0000269|PubMed:27388157,
CC ECO:0000269|PubMed:27513322, ECO:0000269|PubMed:30735556,
CC ECO:0000305|PubMed:30735556}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8 H(+) + holo-[ACP] + 8 malonyl-CoA = atrochrysone carboxyl-
CC [ACP] + 8 CO2 + 8 CoA + 2 H2O; Xref=Rhea:RHEA:64232, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:149712;
CC Evidence={ECO:0000305|PubMed:30735556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64233;
CC Evidence={ECO:0000305|PubMed:30735556};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30735556}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor MYCFIDRAFT_198930 and is up-regulated as early as
CC 2 weeks post-inoculation and remains high through 9 weeks.
CC {ECO:0000269|PubMed:30735556}.
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:27388157}.
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DR EMBL; KB446562; EME79056.1; -; Genomic_DNA.
DR RefSeq; XP_007929626.1; XM_007931435.1.
DR AlphaFoldDB; M3A326; -.
DR SMR; M3A326; -.
DR STRING; 83344.XP_007929626.1; -.
DR EnsemblFungi; EME79056; EME79056; MYCFIDRAFT_34361.
DR GeneID; 19338987; -.
DR KEGG; pfj:MYCFIDRAFT_34361; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_1_1; -.
DR OrthoDB; 68112at2759; -.
DR Proteomes; UP000016932; 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 GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
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; IPR032821; PKS_assoc.
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; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 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; 1.
PE 2: Evidence at transcript level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..1762
FT /note="Non-reducing polyketide synthase PKS8-1"
FT /id="PRO_0000451117"
FT DOMAIN 1685..1762
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:27388157"
FT REGION 17..247
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27388157"
FT REGION 388..822
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27388157"
FT REGION 920..1240
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27388157"
FT REGION 1308..1622
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27388157"
FT REGION 1632..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1722
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1762 AA; 192445 MW; 85DA164D5B80289B CRC64;
MEFVYFSNEF PKDDLHDIYR GLHNHSKHRD FPLLARFLNE ATAAVKDEVR RLPTELKRLI
PPFDNLLSWV ENKELREGLL CGAIDGVLLI VAQVASYIGY VESHPEELRN MSEASLAGLG
IGLLASTAIS LSTEQADLPL AGADAVRLAF RMGVHVFGVS ENLEARDLSE KPETWACVVH
NVDPAVAQKE LDAMQPAGEV PETGKVFISA ISRTSVTVSA PPQKLKALLN KCEFFRKARY
IELPVYGGLC HAPHIYSAQD TESIVRGASL NARRKGLEPV VPVYSTSSGQ PYAAKTATEL
FECVVSELLR QAICWDKVIA GIVDSAKRTA TTEATLHCFG NSIPLNDLDK AFKSDMPELR
VSTNNLVPWI FQNEPRDTAP RGPAQSKLAI TGISCRFPGG ATTTEKFWEI LEKGLDVSRK
IPADRFDIET HYDPTGKALN KSMTQYMCPI DEPGLFDAPF FNMSPREAQV VDPQMRLALV
TAYEALERAG YVGNRTASTK LERIGTYYGQ AADDYREVNQ GQEVSTYYIP GGCRAFGPGR
INYFFKFAGP SYSIDTACSS GLAAIEIACR ALWNGDVDTA VTGGMNILTN PDGFAGLNQG
HFLSKGHNAC KTWDATADGY CRADGIGSLV IKRLEDAEAD NDNILGVILG AGTNHSAEAV
SITHPHAGHQ AYLSRQVLRQ AGVDPLDVSY VELHGTGTQA GDFEEMSGIM DVYAPLTKRR
SKDQPLHIGA VKSNVGHGES VAGTTALIKV LMMLQKNAIP KHIGIKTEIN PKFPKDFKQR
NLHIAFEQTA WPQIPGKKRL AAINNFGAAG GNTTMVLEEG PVREKQQADP RQSHVVAVSA
KTKASLTGNI ERLIAYLEAN PATDLADLAY TSTARRYQHT HRVAMATSDV AELTKKLTSS
LSKVDSIGPV GKSGPPQVAF SFTGQGASHK SMNLELYRDV PTFREHIHHL DTIAQNQGFP
SCIPALDGSF PQDHEHSPVI TQLALVCTEM ALAKYWASLG VKPDVVIGHS LGEYAAMHVA
GVITASDAIF MVGRRAQMLQ EKCKIRSHTM MAVRASVAQI SESSGGKRHT IACVNGPSDT
VLSGTKEQMN EIQVPLEAAG YRCIKLDVAF AFHSEQTDPI LDDLEAVLES GVVFQEPKMP
YISPLLGKTI FDGKTLNANY VRRATREAVN FLPAMQNAID IEAVSEETVW VEIGPHPVCA
GFIKSIVPST QLAIPSIRRN EDNWTTMSSS MAALHLTGVA LSWNEFHRPF ESSLRLLDLP
TYAFTEKNYW LQYNGDWCLT KGNTFYSAEK EAARAAEPQP SVGSDLQTST VQQVIALEVE
GNAGVVVMKS DLMQGDLLVA AHGHRMNGCG VVTSSIHADI AYTLGNYLYR KIKPKDKVPA
MNMTDLLVTK GLVAQNKTKY PQEFRVTAAT PDITSGQIMM SWQNVDDNEP FATATLILGD
ANDWLSSWES MSHLICSRID SLERMAAEGK ASRFTRNMAY TLFASNLVDY ADKYRGMQSV
VMSGLEAFAD VELTTKESGT WTIAPYFIDS VAHLAGFVMN CSDAMDAAKN YCVTPGWKSM
RFAKPLTAGA KYRSYVRMIP TKDDPTVYLG DVYIMQDDEI MGMVGGIQFR SYPRILLNRF
FSAPDKAMTE ARAGNAATVT PQVTIPKPPS SLKTPAPANP SRRDSGVESK PLPPPQPKQA
PPSTDSENST ISKALTLIAT EGGLEISDLG DDVSFADLGI DSLLSLVISE KFRSELGVQV
SGSLVLDYPR IGDMRRWLEE HY
