ID Q2UA48_ASPOR Unreviewed; 2141 AA.
AC Q2UA48;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Polyketide synthase module {ECO:0008006|Google:ProtNLM};
GN ORFNames=AO090102000545 {ECO:0000313|EMBL:BAE61567.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE61567.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE61567.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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DR EMBL; AP007162; BAE61567.1; -; Genomic_DNA.
DR RefSeq; XP_001822700.1; XM_001822648.1.
DR STRING; 510516.Q2UA48; -.
DR ESTHER; aspor-q2ua48; Thioesterase.
DR EnsemblFungi; BAE61567; BAE61567; AO090102000545.
DR GeneID; 5994745; -.
DR KEGG; aor:AO090102000545; -.
DR VEuPathDB; FungiDB:AO090102000545; -.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OMA; FRATMQH; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000006564; Chromosome 4.
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:0046148; P:pigment biosynthetic process; IMP:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; 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; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 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; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 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 Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 376..807
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1646..1722
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1764..1841
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1608..1645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1721..1764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2141 AA; 234167 MW; AB6964F2CE9E5DE3 CRC64;
MEGPRGVYLF GDQTSDFDAG LRRLLQVKNN TIVASFFQRC FHALRQEIAR LSPSERKIFP
RFTSIVDLLA RHRESDPNPA LESALTCIYQ LGCFINYYGD LGNVYPSASD CHIVGLCAGL
LSSAAVSCSN NVGELLPAAV EAVVVALRLG LCVLKVRELV SSDQASSTSW SVLISGISEK
DASQLIGEFT AERAIPPSSK PYISAVGYNS ITISAPPKVL DDLIDSRLSK SHKPVRAQIH
GPYHAAHLYY GRDVDRIIES CHNEVVSNYT PRIPVLSSTT GQPIEAKHMK DLLKAALEEI
LLRQLCWEKV TDACYSILKT ARHQPCKLFP ISSTATQSLF TALTKAGITD IEVENGLGDV
PTNPKDNLNI SGRADCSKIA IIGMSGRFPE ADGTESFWDL LYNGLDVHRK VPAERWDVDA
HVDPTGTKRN TSKVPYGCWI NEPGLFDPRF FNMSPREALQ ADPAQRLALL TAYEALEMAG
FIPDSTPSTQ RDRVGLFYGM TSDDYREINS GQDIDTYFIP GGNRAFTPGR INYYFKFSGP
SVSVDTACSS SLAAIHMACN SIWRNDCDAA IAGGVNILTN PDNHAGLDRG HFLSRTGNCN
TFDDGADGYC RADGVGTIIL KRLEDAQADN DPILGVINGA YTNHSAEAVS ITRPHVGAQA
FIFNKLLNDA NIDPKDVSYV EMHGTGTQAG DAVEMQSVLD TFAPDYRRGP GQSLHLGSAK
ANVGHGESAS GVTALVKVLL MMKKNTIPPH CGIKTKINHN FPTDLAQRNV HIAFQPTPWN
RPASGKRQCF INNFSAAGGN TALLMEDAPI AEVKGQDTRP VHVVSVSARS QSALKNNINS
LVKYIDEQGR SFNVNEADFI PSLAYTTTAR RIHHPFRVTA IGSSLQELRD SLNNSSRLES
FTPVPATAPG VGFVFAGQGA QHTGMGRQLY EKCSQFRATM QHFDCISQNQ GFPSILPLVD
GSVPVEELGP IVTQLGTTCL QMALVNYWGS LGIKPAFVLG HSLGEFAALN TAGVLSTSDT
IYLCGRRATL LTEYCQVGTH AMLAVKASYP QVKQLLKEGV DEVACVNSPS ETVVSGLTAD
IDDLAQRCST EGWKSTKLRV PFAFHSAQVT PILERFQEEA QGVTFRKPSL PFVSSLLGEV
ITESNYDVLG AQYMVKQCRK SVNFLGALEA TRYAKLMTDK TVWLEVGAHT ICSGMIKATF
GPQVTTVASL RREENAWKVL SNSLSALHLA GIDINWKEYH QDFSSSHQVL PLPSYKWDLK
NYWIPYTNNF CLTKGAPQTA IQAAPQTTFL TTAAQKVVES RDDGTTATVV VQNDIADPEL
NRVIQGHKVN GAALCPSSLY ADIAQTLGEY LIEKYKPEFK DLGLDVCDMV VPKPLIAKGG
EQLFRVSAIA NWAEKKASVQ VYAVNADGKK TVDHAYCTVK FFDTNASELE WKRISYLVKR
SIDSLHQNAE TGEAHRIQRG MVYKLFSALV DYDENFKSIR EVILDSDNNE ATARVKFQAP
PGNFHRNPFW IDSFGHLSGF IMNASDATDS KNQVFVNHGW DSMRCLKKFS PDVTYRTYVR
MQPWQNNIWA GDVYIFEGDD IIAVFGGVKF QALARKILDT VLPPVGGSKA PITAKSPPPA
RTQKANTGAK TRPKAPVPSK SFTKSSGPSV VVRALSILAS EVGLAESEIS DDMVFADYGV
DSLLSLTVTG RYREELNLDL DSSVFTDHPT VNDFKRLIAQ VSPSESHDGS SSEQESNFSF
NGGESSSAST PDITSPPNEK VAQVEQNGTM KEIRNIMAEE IGVPAEEIDP DENLGEMGMD
SLLSLTVLGR IRETLDMDLP GEFFIENQTL NDIEVALDLK PKTTSAPIPM PEPVKFPEAI
HDLQPKLAQH PKATSILLQG NPRTATKTLF LFPDGSGSAT SYATIPGLSP DVCVYGLNCP
YMKTPEKLKC SLDELTAPYV AEIRRRQPKG PYSFGGWSAG GICAYDAARH LMFEEGEQVD
RLLLLDTPFP IGLEKLPQRL YGFFNSIGLF GEGKTAPPSW LLPHFLAFID ALDAYKAAPL
PFKDEKWAKK LPKTYIIWAK DGVCGKPGDP RPDPPTDGSK DPKEMVWLLN DRTDLGPNKW
DTLVGPENIG GITVMEDANH FTMTKGEKAK ELSTFMANAM A
//
