ID A2QW90_ASPNC Unreviewed; 2341 AA.
AC A2QW90;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Contig An11c0160, genomic contig {ECO:0000313|EMBL:CAK40660.1};
GN ORFNames=An11g04280 {ECO:0000313|EMBL:CAK40660.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK40660.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK40660.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM270233; CAK40660.1; -; Genomic_DNA.
DR EnsemblFungi; CAK40660; CAK40660; An11g04280.
DR VEuPathDB; FungiDB:An11g04280; -.
DR HOGENOM; CLU_000022_31_5_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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 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; 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; 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; 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; 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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2257..2335
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2341 AA; 254505 MW; 2829B1D68FA5475C CRC64;
MEEQARGSSG PEPIAIIGMG CRFAGEASSV EGFWDMLRLG RREHGRVPAS RYQASAWEHP
SHERKGAINH DSGFFLAEDP SRFDAPFFSI TSKEAAGMDP VQRILLEVAY EAFENGGVPM
ETLPGSATGV YSGCMTNDYE LLSTRDIMDM PHNSATGNGR TMLANRLSWF FDLRGPSIMM
DTACSSSLTA LHLATQALRA GECSQALVTG ASLILHPNFT QRLSYMHMLS ADGISHSFDS
KANGYGRGEG FGAILLKPLS KAMADGDTIR AIVRATGSNQ DGRTPGITMP NATAQADLIR
STYSRAGLSM GDTSYFEAHG TGTAIGDPTE LSAIGASFGA ARTPGGEPVY VGSVKSNLGH
TEGAAGVASI IKVVLCLEKG MLVPNAGFSN LNPKIRLEEW GLRLSNSTTP WPSHLPQRAS
INSFGFGGAN AHAILESTAQ YLGKTQAPSD STIEGIPQVV VVSTHDQSGL DRTADKWTSF
LNPCVDGKRK DIALLDVAHT MATRRSQLPF RSFAVVNSLA ELRNVMAAGL PAFPRASRKN
QTHLAFVFTG QGAQWPRMGV QLLANPVFAA SMERSQQVLQ SLDCSWELLE EIRAGATTSR
INRPDRSQPS CCALQVALVD MLRSWGVTPK AVVGHSSGEV GAAYAAGYLT HEDAIRITYF
RGVLSQRIAE SESRGGMLAA GISAVDAQQY LQTLPPESVV VACVNSPSSV TLSGNIEEIN
LLEKRLQADG CFARKLCVDT AYHSPHMRAL ADDYKAAIES IQPVDKYKGS ISMFSSVTKE
LLQATDVDAS YWVRNLVSPV EFSAAVTKVV TMTEAGRGRG RRRVVPVKWA GFLEIGPHEA
LKGPFNQTLQ EANADLASTP YRSLVLRRQD SRQTALQVAG LLWCLGYAIN LDTANQSFLE
SRRPQVSRDL PSYAWNHQST FWHEPLESAR LRQRKEPRHD LLGMPWDYQN ELEPRWRNFL
RVSELPWLAD HVVAGSIVYP AAGMVSMVAE AARQLADTTK WLEGIEFYDL DFFRGVVIPP
DERGLEIVLH VAPHHGMNGW YEFGIFSLPE NSSWVQHAKG AFAPQYADED GVGCAADWQC
TVQRVRQTQA LAKKAEIEAV YEWLSETGGV TLGPTFRSMA GVAFDSESRL YVTGVAPNTK
QTMPYERESP CLVHPTSLDS LFQAAVVSCS DALSNHNANI PVGVERLYLS TAFSLQPGDR
FDVHVETRYE NGVSFTESIA SDPSWQQPGV VLQGVRLGRV PTRSGISTKE EIQQSRFSTL
HWAEHVDSFG GLEGRCSGDL QCWLGRVCHT HGDACVLVVT TKDIGQVVEA LKKYAPKRSH
RPRLQKLTIV LSDPDTEAST NQVKVIKESL DGCQVLPVAS LKDIGTDLLG ETAYDAIIVD
HPDVWSGDNA KAFFNTLLSI TRPDSWIAAR ATAENHDAAI RNAGHADWEV QGSIEQPGYL
LIRRQLAPIE LDPTIYILSS AAAESVGSLL YELDGVVSKL GSKIELVDVD KAPDLKEKMI
ISLLELDRPW TVNWTPDEIS RFQSLLQAKC LLWISQCPGH EASGYAGFGA TTGLLRTVRN
ENPHTVLPQL LVSGKDKDPH NLARSIAHVL QLTLKPRSRP HDWEFYMQDN CLLVPRAITA
RAVDESMDAL LHGPRPTLAE LAQDSRPLRL CTKSQDISDA RWELDEPLNS ALPDDLVEVQ
LHKVSITEPA SKSGLSPEAR IAAIEAVGIV RQVGSSIGSE FQVGDEVLCA IPSDAWPSAL
TTHQSQTQSV SMPVAFAGAY TSLFGSSGAS ASSVLIVGSV SQTLRATVDC ALAAGMQVYV
AIDGENGVNE MRSKYVGLHE RIIPIHRELD TTVKRLTGGK GVELSVCCLG GSVSRLAARC
LAYSGRLVDL SEELNLAALP QTFVDRGCTV SSVRLSKMLR EAPRQLQANF HRAVDLLGSD
ALASVQAYQS FPVSQVRDAV AHARDSGTRA IVDLQAPGQV PIVPALPDPA SLPAKNTYIL
VGGLGTLGIA LANTLVDCGA RHFVFLSRSG AVRETQQTAL KELQDRGART DVVRCDATCQ
EDVESLLTRA EKSRWRVRGI VQCATVLKDG MFEHMDFDAW KQSTEPKIQG TWNLHEAFYS
TPLDFFVTLS SISSIIGNIG QANYAAGNGY MDALMTWRRK HHLPGHSINI GLVPDASGVG
DVAETPEQRR QRYRHIEGTE ILQHEVQTLL RVIVQKITPV PAQIIAGLTD TLPRTDGAAS
WQFDRKFDHR IQVVADEDAG AGVVKTSTLL KKAESVDEAV RVVNQALQEY LARAMASSAE
AIDLELPFSA LGVDSLKAAE VQNWVSREMG AELSSFEFIG AQPVRVLAEK IATLSSFVVA
T
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