ID A0A100IJM8_ASPNG Unreviewed; 3930 AA.
AC A0A100IJM8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:GAQ42439.1};
GN ORFNames=ABL_05100 {ECO:0000313|EMBL:GAQ42439.1};
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:GAQ42439.1, 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 -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:GAQ42439.1}.
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DR EMBL; BCMY01000007; GAQ42439.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:An11g06460; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1112058; -.
DR VEuPathDB; FungiDB:ATCC64974_92040; -.
DR VEuPathDB; FungiDB:M747DRAFT_361485; -.
DR OMA; HMFLEAI; -.
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:0043604; P:amide biosynthetic process; IEA:UniProt.
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:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
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; 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:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..439
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2344..2421
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3468..3545
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2453..2487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2455..2487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3930 AA; 430344 MW; 440C5FE64C07AF06 CRC64;
MAPEREPIAI IGSASRFPGN ATSPQKLWDL LIHPRNVGKV IPGDRFSVDG FWNADGSHHG
TSNVTQSYFI EDDTRHFDAN FFNINPREAA AIDPQHRLLL EVTYEALESA GLSIDILRGT
PTGVYVGLMC ADYLDVQLRD PEALAQYHAT GTARSILSNR VSYFYDWKGP SVTVDTACSS
SLVAVHQAVQ ALRQGECSTA MAAGVNLIFG PEMYIAESNL RMLSPTGKSR MWDARADGYA
RGEGVGVVIL KRLGDALRDG DPIESVIRET AVNSDGRTNG LTMPSSASQA DLIRQTYRRA
GLDPTQASDR CQYFEAHGTG TPVGDPLEAE AIHSAFFPES HDGCQVQESQ LYVGSIKTVV
GHTEGAAGIA GLLKASLALQ HEIIPPNLHF KRLNPNIVPF YDGLHVPIKP IPWPPAQVRR
ASVNSFGFGG TNAHCILEHY APSVHGGAKE GSEKPVNEPA VESPLISLPF SASSQSSLAR
LIQQYAGFIA THPSVDMQAV SLALQKRSNL PFKHYVTGLS HNSILQQLQD PQWKLGPSGG
GAEAHNSAIL GVFTGQGAQW PTMGRELLLR PGPFTATIDR LDDILRQLPE PPTWSLREEI
LADPDTSRCQ QSTYAQPLTT AVQVALVDLL YSVGIRFSVV VGHSSGEIGA AYAAGCITAE
AAITIAYYRG LYSPRADPGE GGPKRSMMAV GMGFNEATRF CTQPEYAGKI FPAASNAPSS
TTLAGDLFTL EFARDELTRQ QKFARILRVD KAYHSPFMEP CAEPYMQALQ AGNFAYRTSG
PSCTWISSVH GFEMDCSSDC VNDSYWLKNL LQPVLFSDAL SQAIRDHGPF NCVIEVGPHP
ALAGPAGQTF KALQQNVPTY LGALTRGEND VLRLSRCLGE VWKLCGPSSV NLRVFQSLIN
GEDGTLPAML PKILPSYPWD HERPYWRESR SSKEYRTRAP SHELLGVCVE QSEQFWRWRN
ILHPREIPWL QGHEFQGEML FPAAGYCIMA MEAALRFSYP QPVRLLELHD LDIRRGISID
GSADGIELHC HLGPSSTRES EKSSALKVVN LSFTCTAGHV DGSDALTTRF STRIRLEMGS
PDLTVLPRKQ QQSSGNSPVD IERFYGSMSQ LGLNYTGPFH SLLASERRLF QASATVAHVS
SSSSFMHPGV LDTCFQTLFV AFASPDDEYV LPNLRYPPIA LTYTSCRSLR TPHLPREIRS
IRFNPAAIAH PDHPRGSPFQ VESYVTKATP PTRKIPSDMV GDIDVYTAAG DCVLQIESLR
CVALAVTTEK DDRAMFHRTH WEIDIDAGMV VSFDKPNTEY STILEQFEAV ARQAIDGTPP
AIGDIVSPEL QLIQNAISLH FAHPSEVPEA QATFKAAQSQ YWKTSAGAQR MQEYVVRTVK
QVTHKYPRMR ILLLLGGNDD VSVARRILDA INGNYTSLIL TGSSLETLKT AKERLKPYGD
AVQVETLDLG TSPPEMLYDM VIVQIGVLGE GAASIPLEYC RRVLKTGGFL LFDSITGRGN
FAGCLQGRLM DEHRINSEPK RIWEALLQQS GFSGLESVAY DTGNPQLHCH SLILSRAMDA
SLQSLQHPLA YPDQTNEAAD KDHVLIIGGH TGIGSQGLQA LRSHLSKWKR GLTNVASLED
LGSYKSQNIP SHVLCLTDVD APLFRNLSAE QFAALQRLFQ EAHNVYWVTR GFKQGDSYSA
MTVGLGRVVQ TELQGLNLGF LDIDVVDENG ITQIATRFAQ FVSHGQHSHA VSAETSLWCQ
EREVSLENGL PYIPRVKHAQ DMNARFNSAF RAIEQPLGLD ASLSKQSDTA SELEVVASVV
ARSAHALTLT NEVDGYLCIV NINSTMGDRL GLVISSSAEE KVVVCKRDDI LDINLRQNHT
ISAPEILRML VALHISERVQ ASLCYSTTLV FTNDPWLLRV LAMSRESDQR ALILATSHEG
AMEWDKSIIY VHPHTPTRDL LSLVPQDVSK FINLDTEFQP LHNRLLAAIP RTCATHSAKD
YLSERASTGH VLSPSQSSRD ALDMLWTQWL ISSAALQSNM HPDTVVPHGL SACAVKSYTP
QESPHVTVHR LDPSIILRRD ATYLLVGMTG ELGQSLCRWL VANGAKHLVI ASRSVKPVPW
HEELQQSSGC QLMTLPLDVC DMQALRLAHQ NILQSMPPIA GVVNGAMVLA DAIFVNMAYE
DFTRVLEPKV RGSKNLDELF SGNELDFFIM LSSTASLIGN AGQSNYSAAN MYMKALAEQR
RQRGLAGSCF DIGMILGVGV VSRERVYEEP LRKAGLMPIA EPDFHCMFTE AMWLGRPGMS
ADSSPCFSTG LHVPPGTMRP AWYHDPRFSH FQVPEEDINR SAGAGKDAAV TLGEQLRCTS
ELTAAEGLIQ EAFVVRLQSL LQLTGPIDDV TRALSELGID SLLAIEIKTW FFQELGFQVS
VMKILNGISV RGVCREAAEH VFRARAAESD EGASTVESVK VLKTLEAPTP RLQEDEATET
VSTVARTQET PFSDTSSQTS HAVETPTSSQ ILPAAGLSIP TMVAMSTEQE KIWFMLQSVD
DPAMYNCTIQ YELNGQLDRV RFQVAVTEVA QRHESLRTAY VTDLHDQVPR RLILGQPQIT
WREVGMKSDD KDLIATEFEA LQTRAFDLAK GQTMAITILS HGPARHAIIF GYHHLIMDGV
SWQMVLREIA AAYQDRQSLP PVVAQYSAFC NQEDSTSEAT TPAWNKGPSS TDTDGQLPDD
LPLFPFARTG FRTRTRTSYE TIRVSSYLGK DDANRVRSIS SRTGATSFHI HLAAIQLLLQ
QTLEVDRFYL GIAHANRNDP RFERVVGLMV EVVPLMFEPQ QAQGFKDLVK DTRSRVLGAL
SQAHGSGKSS RPCDIVVNYI AGVTHDIMFD EAVLKYATSE DARQPHDLVI TVRDNPDGTT
VITFGALEYL YHAHDVRLLL DLYVRLLGSV SLNSDLKLEQ YRCLEPLCLK APIQPPTSQA
ELSAIQKEPD RLTQWIARIA ATYPNTVALK DTNGRELTYA GMESRVRSII DILLAVGVQP
RAFVVVACGP SVDTVCALLA IWRLGAVYVP ADLEHGVERL SLILKDCSPA ALLCRSKAGL
GHFMADHGPQ VVELKMHLPP PSPTTLDYDR STGQDPAILI YTSGTTGVPK GVLLSHDNLL
CHFAAVQQVF PVDQPVVLQQ SSHNFDASLF QVCVSLLHGG TLVMTSNRQD PIELAELMVR
EKVSLTLGVT SEYALWLGEA ASVLRKCTSW QYALCGGEKM SSGTLQGFSG LDIAGLRLIN
AYGPCEASVA CTMGEIDYKR NDLYGSHDPI PVGQTLLTYA IHILDNQMQP VAAGWPGEIC
ISGGAVSSSG YWNREDETSA RFRVFNGIRI YRTGDYGRIL PNGDLEYRGR LKGDSQIKLR
GMRLELEEIS SVLVQASQGV LREAAVIVKG HPEPYLVAFV VFSTSESPAS VGSFLNTLRS
GLPLPAYAKP TVITAIDRIP LTTSGKVDRT ALARLEIHQQ QSVSPTSGAL NIIEMKLKEL
WQELLPATGL PITPQSNFFD LGGNSLQILR LQGRIRAITK VSVPVVHLFR CSTLNEMAQL
IGAATSAHRA SAPTPPAPAL SITIDWEAET AIPSSFDNLI TILDPHIHQP SNSPREVILT
GATGFYGTAL LTHLLSLPSI TRIHCLAIRP NADGSPRRLE HLTSPKVHLY SGDLSHPTLG
LKEAEITHLA STVDCIIHNG ADVSFLKPYS ALRAANVEST KFLFSLCTSR GIPFHYISTA
SVTSLSGKDE FLESSVASYS PPMDGSPSGH TVGYTASKWA SEVFLEKAST RYTNVPVCIH
RPTAITGDKD MAIAATSGGV IESVLDLSRR MRAIPETGSW RGYIDLIGVK KAADMVVRKV
VGGDDTSGVE VQYSHVCGEK RFKASDLRMF LEKEEGVEFQ QLGWKEWLDM AAEYGIDDGV
AAYLEGLKGD NGGSRDLFFL PLLGGGLSGY
//
