ID I8I802_ASPO3 Unreviewed; 2456 AA.
AC I8I802;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Polyketide synthase module {ECO:0000313|EMBL:EIT73076.1};
GN ORFNames=Ao3042_11114 {ECO:0000313|EMBL:EIT73076.1};
OS Aspergillus oryzae (strain 3.042) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1160506 {ECO:0000313|EMBL:EIT73076.1, ECO:0000313|Proteomes:UP000002812};
RN [1] {ECO:0000313|EMBL:EIT73076.1, ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|EMBL:EIT73076.1,
RC ECO:0000313|Proteomes:UP000002812};
RX PubMed=22933657; DOI=10.1128/EC.00160-12;
RA Zhao G., Yao Y., Qi W., Wang C., Hou L., Zeng B., Cao X.;
RT "Draft genome sequence of Aspergillus oryzae strain 3.042.";
RL Eukaryot. Cell 11:1178-1178(2012).
RN [2] {ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|Proteomes:UP000002812};
RA Zhao G., Hou L., Wang C., Cao X.;
RT "Comparative genomic analyses of Aspergillus oryzae 3.042 and A. oryzae
RT RIB40 for soy-sauce fermentation.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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:EIT73076.1}.
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DR EMBL; AKHY01000202; EIT73076.1; -; Genomic_DNA.
DR HOGENOM; CLU_000022_6_2_1; -.
DR Proteomes; UP000002812; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; 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; 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; 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; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013120; Far_NAD-bd.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF14; ITERATIVE POLYKETIDE SYNTHASE AFOE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 388..805
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1655..1732
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1635..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1640..1655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2456 AA; 267664 MW; 9628D53D773460F5 CRC64;
MVNSGSNIKS ESLTLVFGPQ DPNLDNTFLQ SLRTTLLETP ELQWILETLT QLPQEWQKIS
DAHSELAAFQ GQRYLQLLNE WVRRGTLPSN LFPLPNILVT PLVVTTQLAQ YTKFITQLNP
GITSNDSLQG ALKLDTETAG LCTGLISSAA VAISGTLAEL QKHGAAAIRI ATAIGALVDA
GDSEHEDGDK WESLAVGWTA HGTESKLESI VDGSPEAYVS VISEARLATL TVLKADTLEL
LEKLKAAGVI FTKTALRGPF HCGKRKDQAA SLLQLFDSDP SFQFPHASQL AFSTRSADSG
KFRIEDKLHH EAARAMLTDK ADWHKLFTAL HESTSTRPSL TICFGSQRFV PQWFLRKLGP
KLAYAADLDA NPGQLPPALG ALLGPIEDDA IAVVGMACHF PGGSDLNEFW DTICAAESQC
TEVPSDRINF DYAAWRENDE KRKWFGNFVR DYDAFDHKFF QKSPRETVSS DPQHRMMLQV
AYQAVQQSGY FSKAAIDQHV GCYVGIGVVD YENNVACHAP TAYTATGNLK SFAAGKISHF
FGWSGPGVTI DTACSSSALA VHHACNAILN GECNAALAGG VNVMTSPEWY QNLDGASFLS
PTGQCKPFDE AADGYCRGEG AGAVFLKKLS AAMEDGDQVL GVIRGSSVNQ NANCSAITAP
SVQSLTGVFN AVLRKARLDP KQISVVEAHG TGTQVGDRAE YDSVRRVLGG PGRAEPLSLG
SVKGLIGHLE CASGVAALIK VLLMIQNGAI PPQSSFRTIS SKLDASPLDN IEISTCLRPW
ATGSRAALIN NYGASGSNAS LVITQADHAE VQSEAPRVVE AFAGKRPFWF SGIDDQSLRS
YAAKMVRFLQ TRKPNDNRFT IDNLSYQLAR QSNRSLGQSL IFSCASVAEL EAKLASFADG
WSELKSTQRQ QSSRPVILCF GGQKSNFVGL DREAYDHFKV LRTHLDQCHE ICLSLGLGGI
IPAIFERTPR SSIVELQTMQ FALQYSCAKS WIDSGVQVAA LVGHSFGELT AMCVCGTLSV
RDTLKMIVGR ARLLEEKWGP DRGSMMAVDG ELESIQRLLR ETNAAHTTEP PVNIACFNGP
RQFTLAGTSK AMAVVKQTLS SNPFFSSIKA KQLDTTHAFH SVLVDPLVPE LEKLGEDLIF
RSPVIPHERA TQEAIRDPPA FNVFASHMRD PVYFDQAVQR LAQKYPSSIW LEAGSGSGVT
ALASRAAGSC GMVFQSINIT GSGAVQNVAD ATSNLWKEGL NVSFWGHVGQ TVNSLLLLPP
YQFAKTRHWL VRRKPEVKQA APVAPWPKSP KGLWTFMGFQ DSGNTYARFQ IHSTSDEFKK
YVGAHLVAQT APICPSMFQH VMAREALVSL LEDSDMIPEL ENMENDAPLC LDESRFVWLD
AHRTDSESTS WEFRITSVDK GNAASNATQH VSGRLLFRSL GDSTSVFTTF ERLVNRRRPL
DLLDGQEAED VIQGSRNIYK VFAPVVQYND DSYKGLQKLA ASGNESAGRI VKQDAEQTIL
SVGLADTFCQ VAGIYLNCMA ECEDGKMYLS NRVERWIRSP NVPLDSRPNQ WEVHAIHNRP
SPKAYVSDLF VFDSANGKLV WVIIGLHFVE VSIAGMSRLL GRCTGVQSTQ QVAALAPEPT
PVLPGIASPA AVPVTKAPAN KPKTKTSTSS PTKKAPGRDV LNGVRELFCN LLGLEPEDIR
PGSDLVELGI DSLLAMEVAR EVEKAFSIKF ELEELMQMTD VRSLVNCIQA SMGASDSSTT
DGDLSDGFDE ASAAGIQTPP SEPAEDVKIP SIGSAPITGH LSADSIIEAF TETKLLTDRF
IEQNGLSGYS NYVQPKLTEL VVAHTLDAFD QLGCSLRSVQ EGQIIKRLPY LPKHDKVIAV
LTGLLEKARL IDLDGSTMIR TAVPLPTKSA PQLLQELLHE YPEHAYDHKL TSLTGSRLAD
CLGGKTEAIQ LLFGSAEGRE LAAGMYGKSP INVAWLRQLQ HFWQRFLAHL PQQQQEPINI
LEMGAGTGGT TAALLPLLAS SGVPVRYTAT DISPSLVAGL RKRFKDYPWM RFEVIDIEEE
PPTKLLETQH VVLATNCVHA THSLAVTTKN IHRILRPDGF LVMLEMTEAV PWVDSVFGLV
EGWWLFNDGR THALAQPDFW KRTLHANGYG HVNWSDGQLP ENSIQRIIIA LASSESQNLV
SICPPAPSIT TADFAARQAV VDSLVQKHTH DFAVPTSLPI SQTNNDSFRC VLVTGATGSL
GSHLVAHFAA QPDVRKVICL NRVSGSDATT RQLEALQSRG LQFNQNILLK IEAIETNSSA
PMLGLSGNEY QHLVNCVTDV AHNAWAMSMT RPARGFEAQF KALRNLIDLC RDAACHRRAG
MEKIGFQFVS SVSVVGCHPF LTNEAWVPEQ RVNVASALPM GYADAKLICE KMLDETLHRY
PDHFRTMAVR VGQISGSKVN GYWNPVEHLV HLIKSSQSLG VLPDLDGVCP SIDLIS
//
