ID G7XNL1_ASPKW Unreviewed; 1745 AA.
AC G7XNL1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:GAA88581.1};
GN ORFNames=AKAW_06695 {ECO:0000313|EMBL:GAA88581.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA88581.1};
RN [1] {ECO:0000313|EMBL:GAA88581.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA88581.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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DR EMBL; DF126463; GAA88581.1; -; Genomic_DNA.
DR STRING; 1033177.G7XNL1; -.
DR VEuPathDB; FungiDB:AKAW_06695; -.
DR eggNOG; KOG1202; Eukaryota.
DR InParanoid; G7XNL1; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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; 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; IPR049551; PKS_DH_C.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775:SF53; ATROCHRYSONE CARBOXYLIC ACID SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43775; 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; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 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; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 383..813
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1669..1745
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1612..1666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1745 AA; 192285 MW; 9FF54699B5A74964 CRC64;
MRVVFFSNKF PGVDLRDLSQ RLRFVSRSRS HGLLRRFLEE ATMVAHEEIR RLPPELKTLI
PPFQSILDLV DSFDWHGGPL TGVFECAFTC LFHISLFLGS YERNPQEFNF SNSTFTGLGL
GLLAATGIVA SQTLLDVPQT SAEAVRIAMR TGYLLYQKQQ EIEPQEPDAP PKSWSVILKN
MDQATVQETL DHFNASIDVS ITGKLYISVI EPDGSLFVNG PPSILAKIFG KTGKLASARH
AALPVYGGPC HAAHLYDRAD SAHVAETVSP KIANRRVPSN VCLLSMVDGK PLGSQTVLEL
FESAIYCLLT GTIQWGNVAE AIFSSPDWNE EAHVRLESIF QPCPVVNTLI SRAQATYPHC
TVDTREHMQW VFMEENKPTN PSSTDIAVVG MSCRLPGGAN DLTQFWELLV DGRDVHKKIP
ADRYDVETHT DTTGKRQNTS HTPFGCFIDD PGLFDNGFFG MSPREAGQTD PAHRLALLTA
YEALEQSGFV PNRTPSTMAT RVGTYYGHCS DDYREANAGQ DIDTYFIPGN YRAFAPGRIS
YFFKFSGPSY SIDTACSASL AAIQIACSAL IREETDTVVA GGLNLLTGSD SFAGLSRGYF
LSKTGSCKVF DDGADGYCRA DGIVSIVMKR LADAQNDNDN ILGIIRASAT NHAGNASSIT
HPHAPTQEHL FSQILKEANV NALDVDVIEM HGTGTQAGDT TEMESVTNVF CPGLKRRLHP
LYVSSVKANV GHGEAAAGIT ALVKALLMFQ KSAIPKHVGI KTAINKQFRD LGTLNVKIPM
ETVSWAHDNN RRRFALVNNF SAAGGSTCLL LQEPPVRSTP QACPHPTLPV AVSAKSKVSL
KNNIRSLITY LQQNPSSDLP SLSYTTTARR MHYRYRVVVN GGSTQELIRR LQTCLNDVEM
RRPIPKRPSV AFVFSGQGSF YTSIGRQLFE EYPPYREKIQ RLDKLCLLHG FPSIIPLILS
QEQDTAAVMP LMTQLLTTCV QIALTDLWRM LGVKPDVVIG ASLGEYAALH AAGVLSASDA
IFLVGRRALL LQELCTIGTH GMVTVRASVD EICECLPHRK EYEVACINAQ RNVTIAGPVE
HMDDIQASLE SNGYSTTKLN VPFAFHSAHV EPILRRFGEI SRTVTFHSPK ASVLSPLLAD
NVTSRDILAD SYLERATRAP VRFAAALERA QEMGIIHSNT AFIEIGVHQT YSNAVRATVR
DMTCMVPSMR SDQSNWSTFA ASMSALHEVG VEIDWNEWYR PFEPNLRLLT LPSYQWDMKK
HWIQYNGNWL LLKDKGLKTQ DGGALAPVTS AFQTPLLHQI LEESSSENGH TVLMQSNIME
DQLLKIISGH KMCGRPVMSV FAYPDMALSL ANYIYTKHQP QVELPSLDFG NVQIFQGLVA
RKSQANPQWL RVRADADLKH RSVRMSFEHA LEDGHGSHET LATGVVTCGD SQIWSDEWGT
QTDLLISRIE VLYRLAQEGQ ASRLSGNLVY SFFKTLVDYS EKYRGIQSVV LHHLEGVAEV
LLPPGEGGWT AAPNYIDSVS HVAGFILNGS NALDDHDTVY VMDGWKSMRF SQPLVPGARY
QSYTSLKPAK EKPGFYISDV FVIRDGQIVG QIRGMTMRPL PRILLRRFFD PPEESPMSHK
DLSVSSTISD SLTRTHSPIS VSPGRPIESI ERDTPPSTPD DAEISPVARN DSGLVKQAMG
IIASETSICP EELTDDVEFA NIGVDSLLSL VLVEKFALGL HLNLRASVFQ DCPSVGSFKE
HLVAA
//
