PKS27_ASPFN
ID PKS27_ASPFN Reviewed; 2045 AA.
AC B8MYS6;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Non-reducing polyketide synthase pks27 {ECO:0000305};
DE Short=NRPKS {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:24412484};
DE AltName: Full=Asparasone A synthesis protein pks27 {ECO:0000305};
DE AltName: Full=Cluster 27 polyketide synthase {ECO:0000303|PubMed:24412484};
GN Name=pks27 {ECO:0000303|PubMed:24412484}; ORFNames=AFLA_082150;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=24405210; DOI=10.1080/19440049.2013.859743;
RA Malysheva S.V., Arroyo-Manzanares N., Cary J.W., Ehrlich K.C.,
RA Vanden Bussche J., Vanhaecke L., Bhatnagar D., Di Mavungu J.D.,
RA De Saeger S.;
RT "Identification of novel metabolites from Aspergillus flavus by high
RT resolution and multiple stage mass spectrometry.";
RL Food Addit. Contam. Part A Chem. Anal. Control Expo. Risk Assess.
RL 31:111-120(2014).
RN [3]
RP INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24412484; DOI=10.1016/j.fgb.2014.01.001;
RA Cary J.W., Harris-Coward P.Y., Ehrlich K.C., Di Mavungu J.D.,
RA Malysheva S.V., De Saeger S., Dowd P.F., Shantappa S., Martens S.L.,
RA Calvo A.M.;
RT "Functional characterization of a veA-dependent polyketide synthase gene in
RT Aspergillus flavus necessary for the synthesis of asparasone, a sclerotium-
RT specific pigment.";
RL Fungal Genet. Biol. 64:25-35(2014).
CC -!- FUNCTION: Non-reducing polyketide synthase (NRPKS); part of the gene
CC cluster 27 that mediates the biosynthesis of asparasone A, a
CC sclerotium-specific anthraquinone pigment important for sclerotial
CC survival (PubMed:24405210, PubMed:24412484). Catalyzes the formation of
CC the aromatic polyketide from acetyl coenzyme A and seven malonyl
CC coenzyme A molecules (PubMed:24405210). Through its product template
CC (PT) domain, catalyzes the cyclization of polyketide backbone via C6-
CC C11 aldolcondensation (By similarity). {ECO:0000250|UniProtKB:Q5B0D0,
CC ECO:0000269|PubMed:24405210, ECO:0000269|PubMed:24412484}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:24412484}.
CC -!- INDUCTION: Expression is induced by the developmental and secondary
CC metabolism regulator veA, as well as by the cluster 27 transcription
CC factor znf27 (PubMed:24412484). {ECO:0000269|PubMed:24412484}.
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:0000250|UniProtKB:Q5B0D0}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of asparasone A and
CC causess the formation of greyish-yellow sclerotia rather than the dark
CC brown sclerotia normally produced (PubMed:24405210, PubMed:24412484).
CC Leads to a significant decrease of resistance to insect predation and
CC increased susceptibility to the deleterious effects of ultraviolet
CC light and heat (PubMed:24412484). {ECO:0000269|PubMed:24405210,
CC ECO:0000269|PubMed:24412484}.
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DR EMBL; EQ963472; EED57518.1; -; Genomic_DNA.
DR RefSeq; XP_002373130.1; XM_002373089.1.
DR AlphaFoldDB; B8MYS6; -.
DR SMR; B8MYS6; -.
DR STRING; 5059.CADAFLAP00000995; -.
DR EnsemblFungi; EED57518; EED57518; AFLA_082150.
DR VEuPathDB; FungiDB:AFLA_082150; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OMA; MQYVNDW; -.
DR Proteomes; UP000001875; 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 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; 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; IPR001031; Thioesterase.
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 Pfam; PF00975; Thioesterase; 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; 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; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..2045
FT /note="Non-reducing polyketide synthase pks27"
FT /id="PRO_0000436110"
FT DOMAIN 1635..1712
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 10..247
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 380..756
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 913..1213
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1612..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1640..1709
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1735..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1798..2039
FT /note="Thioesterase"
FT /evidence="ECO:0000255"
FT COMPBIAS 1615..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1672
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2045 AA; 223487 MW; 93638F36620BFC7B CRC64;
MVVEERKQTI VFGDLTCDSV AGLRTLVTVK DNPLLISFFE RVTTGLREEI GLLPFSQRQR
FIRFTTFEEL LARVQRSTCP HPALEKALAC TYQLACFIRQ YTSPGHKYPS TQQTCLVGLC
TGLLSAAAVG CCQSITDLLP LATHTVLIAF RAGLFVADVR DRLEPQTGAP LAWSVLIPGL
DGDTASLTLQ KYNEEKGLPA TSAPYISTYA NTGVTLSGLP SALNDLLDSS CLPKNRALTI
PIYAPYHASH LYGQKDIESI LRKASATEFA SYQCQFSILS SITGQSIQVD TFGALIDYAL
NAILREPLRL DRIVSSLGEA LLSDSPIRGC TIFPIATVIG QSLAAALRKH GAPDITVDPC
MNSSIAVRDD RTSTTGHLGH SKLAIIGYSG RFPDANNNEE LWQLLHEGRD VASITPSNRW
DVKTHVDPTL KKKNTMGTPY GCWLKEPGLF DAKFFALSPR EAPQVDPAQR LALMTAYEAM
EFAGLVPDST PSSQSDRIGV FYGTTSNDWG ETNSSQNVDT YYIPGSCRAF IPGRQNFFYK
FSGPSYSVDT ACSSGLAALH LACNSLLKGD IDTAICGGTN VLTNPDITAG LDRGHFLSRT
GNCKTFDDDA DGYCRGEGVC TMVIKRLEDA KADNDPIIAV ILGAYTNHSA EAESITRPHI
GAQKAIFEKV LTSAGVDPYS VGYVEMHGTG TQAGDAREMK SVLSVFAPET ERPRTDAERL
FLGSAKANVG HGESVSGPIA LIKSLMMLER NEIPPHCGIK TKINSGFPTD LMDRNVHIAK
QPIPWERPEG GVRRIMINNF SAAGGNSSVL IEDAPVFEPK SKEAEPRSTH VVAVSAKSST
ALIANIKSLL SYMNATKPEL PSLSYTTTAR RTHHPFRVMV SGPDLPEIHA LLENKLASPT
VQNRARAAQR AAFAFTGQGS QYIGMGESLL NFSTFRSDIE RFNGIAETLG FPSFLPLLES
GNGDISELPP LVVQVGTVCT QIAMARLWRS WGIEPCAVVG HSLGEYAALN IAGVLSEADT
IFLAGKRAQL LQEDISANTH AMLAIGTSVE ETRSLCDGLE YDIACINTPK ETVLSGTNKQ
IDRILDILSS TSLKKTRLRV PFAFHSSQME PVLEKFKAAA RGVKFYEPKV PVISPLFGEV
LTSKEPFGPE YLARHCRETV NFATALESAK ADGVISSALW VEIGAHPIVS GLLRNNLDST
LKTVPTLQRN KDTWKVLTSS LSTLYESGVD IRWSEYHRDF IPGLSVLRLP SYNWDLKEYW
MQYVNDWSLY KGDAQFLKGT PGLSTTCVHK LVEEKKDGNK ITVVGEVDVL RDDVDPFVRG
HRVNNLPLVT PSVYAEMALV IGEYLRKQQT KLSGTLVDLQ HMDVQRPFAT KSKGKGPQLL
QCHVVLDCET FQGSVEFWSV TPEGKKLVRH ALASITFPDA KAAQEEVQQR AQGIMKEMDD
MAARLNTDDR VQKFTGKTGY NLVSSLASYD PEYMGVSSVL LDSGRLEAVA TVKFNNPRTD
GVYHVNPYLI DNLGQPALFV MNANDQADLS KEVFVNHGWK SLHFYKPLSI QKTYRSHVRM
SGPDADGLYG GDMVVFEDKE VVAVYKGIKA QGVPRRLMDY IVHMRDDTKA GAPAGGTLNA
SQSAAANPAA DPSAQADSDN WQAALKIISE ESGVPIAELS PEAAFDDLGV DSLLALLCAS
RFREELGLHY ESSIFLDHPT IKELEAFWKQ GAPETGAVTV SGRDAVLNSM FTEAEAEVDQ
DKNSSDEDRS SLGTSSYEVI SPNTTETTPE ITKTSSPKIS ATSLLLQGNP ALPSTVKTLF
LLPDGSGSCS SYAGLPRIHP SIAVVGVNCP FMKTPESYTC GIDEVTQMYI TEIRRRQPHG
PYALGGWSVG GIFSYHIAQQ LAAQGEQVSE LILIDCPVPK GLDHLPRRYY EYCDTIGLLG
DVNGVKRDPP PWLISHFEAC VNSLHTYHAT PFRPNNAPRT QIIWACDAID KHCEPKFDRR
PDDPEGLKFL TSTRTDFGPC GWETLLPEED MTLDRMTGAN HFSMMKGEFA KRLSEMIEGF
LMIGN
