ID A0A117E2N2_ASPNG Unreviewed; 2580 AA.
AC A0A117E2N2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:GAQ45892.1};
GN ORFNames=ABL_08553 {ECO:0000313|EMBL:GAQ45892.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ45892.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ45892.1}.
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DR EMBL; BCMY01000018; GAQ45892.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:An09g02100; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1079931; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1087173; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1123159; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1163045; -.
DR VEuPathDB; FungiDB:ATCC64974_41180; -.
DR VEuPathDB; FungiDB:ATCC64974_43040; -.
DR VEuPathDB; FungiDB:ATCC64974_63190; -.
DR VEuPathDB; FungiDB:ATCC64974_7510; -.
DR VEuPathDB; FungiDB:M747DRAFT_353924; -.
DR OMA; CASDYND; -.
DR Proteomes; UP000068243; 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: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; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 2.
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; 3.40.50.720; 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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 471..889
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1708..1782
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1809..1886
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2580 AA; 281190 MW; E78F7F0288A0C061 CRC64;
MANDELIHKL TWSPAALSKE PLSIAHVVFV VAEKESESLS AYQAQLANEG ITTVVTDDAM
KINPLITPKT IVVYIPPTAK SKEEIYAAAT QACTSLINVA QQLYHRSISA KSKTVKLFSI
VPKDWGIGDL VYAPLHGLSR VLKTEIPEIM AALKYAQGFD VVRICEGEAQ VAYLQPFTDE
LSDKKELQLH ANSSYLITGG TGGIGLATAA WLAQRGARNI VLVSRRGLPP SSDSKAVEAN
SADLISRIAK LKAVGVSVHV LAVDISKPNA DVTLSQTIND LDIPPIKGVI HAAGTAGYHT
LTRCTPTDIA DNLAPKVIGS LNLDALFPPG TLDFFVFTSS VGQLVGFPGQ LAYAPSNAFL
DALAAHRRRQ GDNSMAILWA GWQGTGVWDQ SKSAMRRLNK ASISRGVADI SPDEAFAAWD
HIASLKTDHA VVVRVLELDA DEPVRHPMLK YVTPRKQAYQ PTTMDYKDLP EHAIAVIGMA
CRTAAGNTEN DLWQAILEGK SIVREVDEKR FPGVVRDGKM WGSFMSDIDS FDHQFFQRSK
REAAASDPHQ QVLLETAYHA LESAGYFGPG QQQGETHDPG SHTTGCFIGM SAPDHILHLA
SNPHSPYTGL GLMRSFVAGR LSHYFGWTGP SHTIDTACSS AMVAIHQACR AIQVGECTQA
VAGGVHLLLN MESSDALRAS GFTNETGTCK ALDSRADGYC RGEGVGVVIL KHLARALQDG
DNIQGVLLAT GNNQNINNTS ITNPVLASQV ALYKDVLGRA GVKPADVSYV EAHGTGTRAG
DPVEIQGIRE VFGGKDRPSI LNIGAVKANV SHAEGASGVV SLIKVLLMMK HGKIPGQAEL
HALNPNIPAL EPDRMAIPTS PREWRDSMRL AVVNNYGASG NNASAVVAPP PLQQYSASPT
LPSASTWPVF ISAASRASLL AYCNTLSRKI IEESPAPELF PHLSFALATR QNRQLRHLFC
TSATSLSDIH SHLSDPEKHI VLSPQLKPVV LLFSGQNGDT VPSVGPLYES SLLFRKHLHR
CEDVMQSLRL PSLFPVILQG IQGGADLILR HISMFAIQYS CGMSWINWSR AAVIQEFWDD
DPGSMVAIEA DLVGSNTTPE RHLEPFYKIH PDIKLDIACY NGPNNYVIAG PTKYIDHLES
YLVEKKASGE KIRFKVLRGM YAYHSSMADT IVDQCAKLSA SIEFQEPKFP FESCHETAWP
GPGPNVVARN TRQPVYFGQA MTRIVDRLGA CTFLEAGVNG PIVAMARSAL PQAPAQGNHT
FLGINGRDLV RSLADATVTL WKTGQTNVQY WLFHQCQRTS YRPVALPPYH FEKHRHWLDY
HGLSGDRDKK TGENGPEHPA VCPHCQRDTA DRPFIKQDKS HTQKAGESVF TIDMHSRRYQ
DLVKGHVVVG TAICPASVYL ELAAHSVALL LNNKITSSIV VDDIHFKAPL SLDTQRSVKL
TLTNKQQYRW GFEFTSTRNE RSILHAIGSI SLRDKSSGKA EEEQEKKDKW TRMINLLDND
PDTDALRGAM VYKVFGNMVK HASAYRGLRH LVGKGTEGAA DISIPVNELG TVARTPNDNV
VDALVLNNFL EVPGAYINCL HIFGSEDDSK AYICTSLGSV GPLNKLPDGR YYRVYAQIVR
QSSNEAILEV LAFDAQTMEL VLSAKDIKFS GISTSTLTKL LAGADPNPTV NGNTDPLQVA
EAPGFSQPTK PKPDTHSNMP NGIKTGSPDV LKIVQGTLSQ TLDVPVAEVT KGASLEELGV
DSLISSEILA SIHDALQIDI SVEDFAAATD VASLCELISA RVGSDATNTG GQDDEVLLGP
EHVSESAGDG HSDWQKTAIE ILGQSLDVPV AEIQMDSQLE ELGADSLIAA EIASNINDAL
NLTISSTDFG SLSDVRSLCD LIAHVSGRAS MQGAAVLPSD SMSAVNKGVT PNGHPITQDE
DMNQTPTEDN AELTHTVFQK VRRGFDSHAK EVKLAGFWDN VYPRQLSVVT AYILQAFEKL
GCPFKKFSQG EKLPSLQVTL PKYQRQVSRL WEILEVAGLV EKHGGTFIRG PVPHVQDKSP
KELSTELISN YPQYTSTHDL LDLLGPQLAE CLTGKADAAS ILCDNDKGKK LLESFYANDP
GLLAASRVLS DFFSTTMKAR TSGEPFRVLE IGAGFGSAAR HLLPQLQASG LRLTYTLSDS
SVTLLERSKA ASQDIEGLEF RQYDIEEDPP VDLLGRCHVV ISNSYVYATR NLQNSLLNMR
KLVRPNDGCV ALIEPTQKLA WHDLVWGLLD GWWQFEDDRT HALQSPWAWR SALQNAGFAH
VDWSESSSRE SRTVRVICGM TAEPERKCPA EATSMLMHRG TSASGKRNLF LAPDGFGSGA
VFGGLGPLLG SVKDISVYAL NSPFMHSKPD PDEPLTIEEL AAIYVGEIKR RQPEGPYLLG
GYSVGGVLAF EAVRQLLEDG NHVEKLFLID TACPTFVRYF PDALVKFLDS IEQVRVGNGS
EFRPNRRGRL VANDHFFLAR QQMRAYQMRR LPGRKMPQVV LISAKEGADK QEGVPRPAFL
PEDEKAVDWF LNDRTNDGCF GWNEVLDNIK VVRADGNHFS MMLPSMISGW GAELARMLDE
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