ID B0XVQ6_ASPFC Unreviewed; 2146 AA.
AC B0XVQ6;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE SubName: Full=Polyketide synthetase PksP {ECO:0000313|EMBL:EDP55264.1};
GN ORFNames=AFUB_033290 {ECO:0000313|EMBL:EDP55264.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP55264.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP55264.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS499595; EDP55264.1; -; Genomic_DNA.
DR ESTHER; aspfu-PKSP; Thioesterase.
DR EnsemblFungi; EDP55264; EDP55264; AFUB_033290.
DR VEuPathDB; FungiDB:AFUB_033290; -.
DR HOGENOM; CLU_000022_6_0_1; -.
DR PhylomeDB; B0XVQ6; -.
DR PHI-base; PHI:7335; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase 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:0008295; P:spermidine biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; 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; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
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; 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; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 375..806
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1647..1721
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1768..1845
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1611..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1724..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1636
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2146 AA; 234495 MW; 03D724B868C9DA75 CRC64;
MEDLHRLYLF GDQTISCDEG LRNLLQAKNH TIVASFIERC FHALRQEITR LPPSQRTLFP
RFTSIADLLA QHRESGTNPA LGSALTCIYQ LGCFIDYHGD RGHPYPSSDD GLLGSCTGML
SCTAVSSCKN VGELLPLAVE IVRLTIHLGL CVMRVREMVD STESSSGSWS ILVSEINEAD
ATSLIGDFVK KRGIPPSSQP YISAVGSKGL TISAPPEILD NFIEEGLPKE YKHFKAPGVS
GPYHAPHLYN DREIRNILSF CSEDVILRHT PRVPLVSSNT GKLVQVKSMR DLLKVALEEI
LLRKICWDKV TESCLSIVQA TNDKPWRILP IASNATQGLV TALQRMGNCQ IEVDTGVGAP
QMDPAAPNAT GNASRSKIAI IGMSGRFPEA DGIEAFWDLL YKGLDVHKKV PPERWDVDAH
VDLTGTKRNT SKVPYGCWIN EPGLFDARFF NMSPREALQA DPAQRLALLS AYEALEMAGF
VPNSSPSTQR DRVGIFMGMT SDDYREINSG QDIDTYFIPG GNRAFTPGRI NYYFKFSGPS
VSVDTACSSS LAAIHLACNA IWRNDCDTAI SGGVNLLTNP DNHAGLDRGH FLSRTGNCNT
FDDGADGYCR ADGVGTIVLK RLEDAEADND PILGVINAAY TNHSAEAVSI TRPHVGAQAF
IFNKLLNDTN TNPHEIGYVE MHGTGTQAGD AVEMQSVLDV FAPDYRRGPA NSLYLGSAKS
NIGHGESASG VTSLVKVLLM LKQNMIPPHC GIKTKINHNF PTDLAQRNVH IAFKPTPWNR
PVSGKRKMFI NNFSAAGGNT ALLMEDAPLR EITGQDPRNV HVVSVTARSQ TALKRNINAL
IKYINTHAPS SPANERRFLA SLAYTTTARR MHHPFRVTAV GSSVKDIREV LRQRADQDVT
TPVPATAPKT GFVFTGQGAQ YTGMGKQLYE DCATFRSTIH RLDCIAQSQG FPSILPLIDG
SMPVEELSPV VTQLGTTCLQ MALVDYWKGL GVTPAFVLGH SLGDYAALNS AGVLSTSDTI
YLCGRRAQLL TQQCQMGTHA MLAVKAAVSE IQHLLDPDVH AVACINGPTE TVISGLSGRI
DELAQQCSSQ NLKSTKLKVP FAFHSAQVDP ILESFEESAQ GVIFHEPAVP FVSALNGEVI
TESNYSVLGP TYMVKHCREA VNFLGALEAT RHAKLMDDAT LWVEVGSHPI CSGMIKSTFG
PQATTVPSLR RDDDPWKILS NSLSTLHLAG VELNWKEFHQ DFSSAHEVLE LPRYGWDLKN
YWIPYTNNFC LTKGGPVTAE VSAPKSTFLT TAAQKIVECR EDGNTATLVV ENNIAEPELN
RVIQGHKVNG VALTPSSLYA DIAQTLVDHL ITKYKPEYQG LGLDVCDMTV PKPLIAKSGD
QFFRVSAVMS WAEQKASVQV WSVNGDGKKM AEHAHCTVKL FNCAERETEW KRNSYLIKRS
VSLLQDKAQT GEAHRMQRGM VYKLFAALVD YDENFKAIQE VILDSNEHEA TARVKFQAPP
GNFHRNPFWI DSFGHLSGFI MNASDATDSK NQVFVNHGWD SMRCLKKFSG DATYQTYVKM
QPWKDSIWAG DVYVFEGDDI IAVYGGVKFQ ALARKILDTV LPPIGGSKTV GAPAPAPARP
IGEKKAPPPI KVTGPPKPNP SNARAASPVV ARALEILAAE VGLSEAEMTD SLNFADYGVD
SLLSLTVTGR YREELNLDLE SSVFMDYPTI KDFKAYLAEK GFCDSSSPEP SSEPESKFSF
NSDASSEASS GLTTPGITSP VKHEAPKGGQ NKVWKSICSI IAEEIGVSVG DIDPSDNLPE
MGMDSLLSLT VLGRIRETLG MDLPAEFFLE NPTLDAVQAA LDLKPKMVPA ATPVSEPIRL
LETIDNTKPK TSRHPPATSI LLQGNPHTAT KKLFMFPDGS GSASSYATIP ALSPDVCVYG
LNCPYMKTPQ NLTCSLDELT EPYLAEIRRR QPKGPYSFGG WSAGGICAFD AARQLILEEG
EEVERLLLLD SPFPIGLEKL PPRLYKFFNS IGLFGDGKRA PPDWLLPHFL AFIDSLDAYK
AVPLPFNDSK WAKKMPKTYL IWAKDGVCGK PGDPRPEPAE DGSEDPREMQ WLLNDRTDLG
PNKWDTLVGP QNIGGIHVME DANHFTMTTG QKAKELSQFM ATAMSS
//
