ID A0A074XGB7_AURPU Unreviewed; 2163 AA.
AC A0A074XGB7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KEQ82754.1};
GN ORFNames=M438DRAFT_46967 {ECO:0000313|EMBL:KEQ82754.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ82754.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ82754.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ82754.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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DR EMBL; KL584986; KEQ82754.1; -; Genomic_DNA.
DR STRING; 1043002.A0A074XGB7; -.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000030706; 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 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 373..805
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1664..1738
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1794..1871
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1630..1661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1735..1798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1758
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2163 AA; 234279 MW; CF6220099F187475 CRC64;
MSNVLLFGDQ TAEQYPLLRK VVLRTKNALV LNFLERTVVA LRGEIAQLSR PQRDAIPDFM
TLNNLVDLYY EKGLKLPHLE SCMVTIAQLG HYIGYFSENT NELPPAANTR ILALCTGSLA
AAAVASARTL DELVTLGVET VRIAFRTGVR VNNARSALGQ DLMSKESWST IVTGINEQSA
KEALTAFHEA AGIPTTSHAY ISAVSTMAIT ISGPPTTTKR FFEESEAVRK NNRVKIPVYA
PYHAEHLYSS ADIEAIIGEE SAKFLQAYQP RSLVHSGSSG MCHVAENTYE LFKLSLNDML
RAPVSWNSLL EESVSQITAN TNASAKVFCI GVSNVSNSLV SAIKAGGQSS VSLVDHSAWE
SAVTDATHGR TQNDKIAIVG MSGRFPSAAS TEALWELLEK GLDVHRKIPS DRFDADAHCD
PSGKGKNKSH TPFGCFIDEP GLFDPRFFNM SPREAAQTDP MGRLALVTAY EALEQSGYVP
NRTPSTKLHR IGTFYGQTSD DWREINASEN VDTYFITGGV RAFAPGRINY YFKFSGPSYS
IDTACSSSLA AIQLACTSLW AGDCDTACAG GLNVLTNPDI FSGLSKGQFL SKTGSCKTYD
NAADGYCRGD GVGTVVLKRY EDALNDKDNI LGCILGAATN HSAEAVSITH PHAGAQEFLY
KKVLANAGVD AHEISYVEMH GTGTQAGDGI EMTSVTNVFA PRHRQRKPEQ KLHLGAIKAN
IGHGEAASGI NSLCKVLMMM KKNAIPANVG IKGEINKTFP KDLKDRNVNI PQQNTPFPRN
GAEKRKIFLN NFSAAGGNTA ILLEDGPLRE APKAVDPRGT LPVTVTARSI AALKSNILRL
QGYLSENPDT TLADLSYTST ARRIQHNYRI AFPIGDIAKV SDALQAQTKE TYSPVPMVPT
KTAFCFTGQG SQYTALGQKL YQDLKPFRDD INQLDNMATI QGLPSFIELL DGTDVATLSP
VKVQLGMACI QVALARMWAS WGITPTAVIG HSLGEYAALH VAGVISASDM IMLVGRRAEL
LVKDCTPHTH GMLAVKGGAE AIRGVLGSKM TEIACINGPE ETVLCGSGEV VGAANDALSA
RGFKATKLNV PFAFHSAQVD PILESFKKVA SSVTFNKPAV PVLSPLSGDV IREAGVIGPD
YLARHARETV NFWTALTSGQ KEKIFDEKTA WLEVGAHPVC SGMVKASVSA TTTAPSLRRN
EDPWKTIATS VCTLFNAGVQ INFDEYHREF NDAQSLLPLP TYAFDNKKYW LDYHNNWTLT
KGEVREVQKT IEAAPVAAPV AEKPAKRLST SCQKVVFEEF EANSGTVIIQ SNVAEPKLFQ
AVIGHQVNDT ALCPSSLYAD MALTVSDYLY KQLRPSAPKI GMNVCDMEVP KPFIAKMEQP
AEGQHIQLEA KADLDEGVAH LKFRSVTPDG KLIQDHAHCL VKFEDISSWT EDWERINFMV
KSQVDLLKAK TKTQEAHVMQ RGMAYKLFKC FVNYNEKYRG MEEVIVNSQT TEATASIKFQ
NGPADGDWYQ APYQIDSMCH ISGFIVNATD LIDSDNNVCI SHGWGSMRIA KQMTPEGNYR
SYVRMLPKPG NVYQGDVYIM EGDEIVAVCG GLKFQQIPRR VLNVFLPPQK AGAPAKAAAP
AAAAHAPKAI AAPKASAPKA QAPKPVVKAA KAPKKAAAKK PQGATITSRV MQIIATETDV
EQSELVEEAA FENLGVDSLM SLTISAKFRE DLDMEISSTL FTDYPTVGEM KKHFSQYDGN
VGPVEDDSED ESEPSDIATP YEDDLSTPAS SAPSTAPSDA GKPDIDSPSR EIPDSEVGEV
SLARHIIVQE MGIDSSELTD EADLSELGMD SLMSLTILSE LREKTGVDLP STFLSTNSTI
LDIENALGMR PKPKAKAASA PKAAKQTSPQ LDKVNAKLTD LSKFPAATSV LLQGNAKIAT
KKIFFLPDGS GSATSYVSIP NIGPDTAAFG LNCPFMKNPT EWTCGIETVS LLYLAEIKRR
QPQGPYIIGG WSAGGVIAYA VAQALLANGE EVDRLLLLDS PCPVNLAPLP QRLHVFFNEI
GLLGTGDPSK TPKWLLPHFT AAIRSLSDYE PQPSLKPIKT YAIWCRDGVA GNPGDPRPPP
AEEEDPAPMT WLLNHRTDFT DNGWAQLCGN NMKYGVMGGN HFTMMKEPHA QELGKLIQEG
LQI
//
