ID A0A2I2G0Q2_9EURO Unreviewed; 2458 AA.
AC A0A2I2G0Q2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:PLB46464.1};
GN ORFNames=P170DRAFT_511231 {ECO:0000313|EMBL:PLB46464.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB46464.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB46464.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB46464.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLB46464.1}.
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DR EMBL; MSFO01000006; PLB46464.1; -; Genomic_DNA.
DR STRING; 1392250.A0A2I2G0Q2; -.
DR VEuPathDB; FungiDB:P170DRAFT_511231; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000234275; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase 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:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
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; 3.40.366.10; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR011032; GroES-like_sf.
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; IPR013217; Methyltransf_12.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF08242; Methyltransf_12; 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; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 31..449
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2378..2455
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2458 AA; 270063 MW; CB143488F4B70E4A CRC64;
MWLFGRKDSQ PEPNIQELEE TTHAATSDDD PDPIAVVGMS MRLPGGIKTG EEFWDLLVRG
KDTYGPVPPS RYNAESYYCE SGRPGTMPTK HGYFLDDDIA AFDAPFFGIN SAEAASLDPK
LRFLLEVVWE CLENGGQVGC QGKDIGCFVG NFGDDWSEIL WRDTQSIRRY EATGAQSFTI
ANRVSYEYDF HGPSMTIETA CSSTLIALHQ ACQSLRNNEC SGAVVGGGSM LICPSCTIAM
GAAGALCGDG KCKTFDASAD GYGRAEAITS IFVKKLSDAI RDGDPIRATI RSTATNFDGR
MPVFVAPNPE AHEEMIKTAY RSANIENIGE TAFYECHGTG TQLGDTTELS AVGNIFKNSG
VYIGSVKANV GHSEGSSGLT GLIKTILSME HDTIPPHVNF STPNPNIPFD SNNLWVSTKP
TPWPKDRLKR ASVSSFGIGG SNAHAVIEGH ERPKKPPAER STLPTLIVHS AKSHSSLERK
VRSMQDYVSK HSDRLIDIAC TLCQRREHLQ HRAFTVHGPG AVENHPQLIK APEKRPQLNF
VFTGQGAQWR GMAQGLMELE PFRDEVLRMS ETLKSIPNGP SWDLANLVLS EDIDYPIHDP
EYAQTLCTAL QVGIVKVLSS WQIKPDTALG HSSGEVAAAY AVGAISSSDA IKIAYYRGYT
AKQYPHNGAM AAVAISKETA EKYLKPSVIV ACENAPQSIT LSGDANDLHA ILDSIKLDIP
SVRSKVLNIP IAYHTHFLNK AGDSYEKLLS ESASPGQTPI AVFQSTSKIG ETACAEGFDP
SYWRNNLVSP VQFHSAVVNV LEKQEDDDKA VFLEIGPHSA LSSPLRDIWR AQSKGPEAVY
IPTIIRDTSP VIGLFHTAGR LHQQAVDIDF LAVNGKGNVL TDLPLYPWDH DQKYWTEPRI
SKEWRQQKFR HHEILGSRVV ESTDSNPSWR NVLSGRNAGW IIDHQLRGKI IFPGAGFVCA
AGEAIRQISG LEDYTIRHMR IAEPLILREE SDVEVITSLG VIPLTNAENS KRYRFTISST
TGDEWVNHCT GEVQGGADCD TSDKRQLLVD DDSHLWNRNV EADRFYSSLR AIGHGYGPYF
QLLSSVQSSS GSCAAKANVR LDKDLRRTSY YAQHPVVIDH CLQLSIVAAI KGLTYRLDHL
VVPAAVDHIY VAPSRGEGVD YSLKAFADKV GKGALCQTVG GSNGGMQIAI SGCSMVPIIK
DIKPIEIQEL HWHPMHSSMS SSELITATHK PIDSDMLVEE IAVLCTLESA RTAQSHKPTT
AHIRKYARWL QSQADMLRKQ GLALVPQAKK WANEDSSNWL DMIEKRASLA KEILEPWQYH
LMLRVFENLP SILSGDQQPL EILYDDAGLR DFYLGLHTPF DCSLFLSSLG HELPGLKALE
VGGGTGGFTT HVLGSLKGAS KVPLYSKYVF IDISAGFFPE AQKHLQSFAG IEYSVLDISS
DPTTQGFPEQ EYDLVVAANV LHATPLLSKT IQNVHKLLKP GGKLLMPEIF PEGLYMNYMM
GTLPGWWLGE QDDRPNSPYV SPERWDQELK AGGFTGLDVI VPDQQFPFHK GGILASTKKE
TLKALDDVTL IYHHEGSPVV QMIKHEFSRV GHQVHLTPFG SHKKHQGGIV CLLEAEDAFF
SDMTQDRWHA FQEFLRDIDQ ASVLWVARET HVQCQNPDYA LTLGVARTIR SELAVEMATF
ETQSFDNGFA DALRIAYNSF RGKYGGTNDR EYEYLYRDGK LHIGRYHSVP AENAVSAKKL
QSMDARMLSI GVPGSLSTMF WKPVACCPPQ DDRVVVDIQY TGLNFRDLLQ ALGAFGEKVE
FGIEATGIVS QVGPSSNLNV GQRVVVMAPH GLLATRAAVS CNSCVPIPDS ISLEDGAALS
CVYSTVILAL LHQGNLRKGQ TILIHSACGG VGLAAISLAL MQGAEIYATV GSEAKAQYLH
ERFGIPRCRI FNSRDSSFQS GVMRETDGKG VDMVLNSLAG ELLHASWECV AKFGKMIEIG
KKDIMGNGSL RLAPFLHNRS FVCVSMDEIM SDRPELNREI LSETFRYIEE GLIEPIRPIR
TFPASQAEEA FRHMQGGQHI GKVLVQMPAN IDDLPHSTKA DAPKFSPEAA YLLIGGLGGV
GRFVCRWMAD NGARELVCLS RSSPSLYTDF VSEMKGQGCL LTLVQGNVAI ENEVKMALRS
CKKPLKGVIH MAMVLEDRPI LQMTLDEWNV PQEPKTSGTW SLHRALQGTD LDFLILFSSI
SSVCGQPTQA SYSAASSFLG AFVRYRHSLG LPAAVIDLGI VGDIGRLTGA DRRLLETTLR
GYITIGEKEI FRAIEVAMMR QEPGSVSEGF RNSQFAVGLT PLPKDSPHHM NSLLHGDKRI
DLLRPALTHA QPVQDEASRV QRLFSAMSQD ATFCESDEAS TLTQQEVIHR LSCLSGSNEQ
DVGLQQPFSQ LGLDSLVVVE LRIWVQRTFH IQASVPEIMG TGHVEGLTQL ILSRVKPR
//
