ID A0A093UNS8_TALMA Unreviewed; 2362 AA.
AC A0A093UNS8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Lovastatin nonaketide synthase {ECO:0000313|EMBL:KFX41560.1};
GN ORFNames=GQ26_0570130 {ECO:0000313|EMBL:KFX41560.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX41560.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX41560.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX41560.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX41560.1}.
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DR EMBL; JPOX01000057; KFX41560.1; -; Genomic_DNA.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 2.
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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 2.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..431
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2274..2351
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2362 AA; 257637 MW; A7E577DCA41BB64D CRC64;
MAQLREGQET VAITGLACRF PGGHNLESFW QFLCEGKSAW SEMDSSRFHA DAFWSEEKRR
NKSITGGAHF LKQDFASFDA NFFGISATEA GSMDPQHRIM IEVAYEALET AGYTLEDLAG
TRTGVFMGHF TSDWKDTMYR DADAAPQYSA TGPLASSFAN RISWLWNLRG PSFCVDTACS
SSLVALHLAC QSLHTRESDI AIVGGSNLLI NPDMFLFLSG QNFLSPDGKC KPFDASANGY
GRGDGFAAII LKRAGDAIAA SDPVRAMIRG TGVNQDGHTK ALFLPSADAQ AELISEVYRS
AGLDFRETMY AEAHGTGTQA GDAEEALALS RTLSAPGVRN QKLLLGSVKG NIGHTEAAAG
IASVIKGVLM LEHGIIPPTI NHINPNPKID FDTYQLRVQT KLTPWPTDGV RRLSINACGY
GGTNAHAVLE DAYHYLQSRG KITPHFTKEG LVHRLKSSSY NERAKPTPRL IPISAQDRDG
LKRVKSSLAN YVRLKTPNLD DLAYTISSKR SRLQWKTFVT ADSLEELASS LEVEDSGTVE
YLSSRKPRIG FIFTGQGAQW PGMGAQLMDF PVFRSSVEAA DEYLRTQLSC KWSAVEELKH
MLNHWSIKPV AVAGHSSGEI GAAYCAGYLT REDAWKVAYE RGIVSGSLKT IVPELQGAMM
AVGTSPEKAE SFIERACQNG EVGVACVNSP SSVTLSGDAE SIDKLETMFS EAGIFARKLR
VDTAYHSHHM HRVARDYLER IADIRPITQS LRDITMHSSV IPGIVSPGEL GAGYWVRNLI
SPVQFAQAVQ NLVRPMVDGK HSTENAVDVL VEIGPHPALQ GPSTQSLKGI GVTNMDYLST
LVRNANGIDL AISLAGNLVA RGSPVDLVQV NAQDSSTYNP HLLVDLPAYP WSHTRRFWTE
SRMARGYRLR EGSHKRLLGS RMSAVAAEEH VWRGHIRLSE EPWVSDHKIH GSILYPAAGF
LAMAIEAALE SADTTRQVTG LYLREIQFVA AMIVAPDSDG VEYTIILRPH LSGTRGTTSA
WMEFSVASSP DGSSLTQNCL GLIQVKYDVS NQREDVTREL RLKDEKTVEQ YQDAVSACKV
VRHTKDFYTK LDSLGLNYGE AFRNVTELHS RMGQSLGTVT IPDAGLNPNK RQRRPHVVHP
TTLDAVFHLA FAATTANELR QPMVPRFLAE LFVAVDMPFT AHAQLKGFST SAKHGLKELR
ADINILDETQ TRPVLTVTGL TCAEVVGPTS LKPINVSKKL CSKIVWRPAV DILTPEEINR
AITSASCKDK IDANAEMQIA EYIKLLHHIN PQLSILEFAQ SESLWASLEL DDIIDTAEYT
VLCDTEHAAD AVRETLPDRG VTCRASKIDE GILDYEKGRS DIIIASTMTV TSPQTDEKVK
PLLKPGGKLC LLGDVKNTRT IEERLHSVGF STLVSNKTAS TKSYLILESP KEAGINGDKF
SSDDEVMIIQ VPQPSRAVQE VAMQFSIELA GMGYTTKLHT WGIDSISNIR RKPCVSLLEL
EKPILQDLEE VNFEGIKKLI LDAGSVLWVV GVDAAAGAMI NGLMRVVRNE VPGINLRTVN
SPFSSASDSL IAAKRLAGLL ARVFVSESTD NEFCIQDDVV KVSRIIEDLV INDELNRVSN
DSKETDVVYR KALKDVPGPV KLAIGQMGIL DSLRFEHDPL ASTELKDDEI EVQVKATSLN
FREVMVVMGQ IPDTLLGFDA AGVVKRVGSS VDKFKVGDRV VMCEHGAHRT IHRAKASFCA
HIPARLSFEQ AASVPTVQAT AWYGLVSLAR VHRGQSILIH AAAGGVGQSA IQVAQHFGLE
VFVTVGSKAK RELVRNEYGI PDDHIFNSRD LSFADGIRRM TGGKGVDVVL NSLTGEALRE
TWHCIAPFGY FIEIGLKDIQ ANTRIDMAPF ARNVTFSFFN LNLIAREQPE LFAAIIENTF
DFLERGITRP VTPVITYSIG DIEGAFRLMQ TGKHVGKISI SYEDDAVVPV VRSTSHPQSL
KLDSNASYVL VGGLGGLGRS LASLLVENGA RKLCFLSRSG AKTLEAQRLM QELSASGVQA
LALECDVSVA VSLREALAKC VKDLGPVNGV IQCAMVLRDT LFTNMTYMQW VECTRPKVQG
TWNLHVELPD VNFFIVLSSF AGIFGNRGQS NYAAAGAFQD ALAHLRRSQN KKGLSLDLGI
MRDIGVLAEN GITESLREWE EPYGIRESEF SQFLKLAIAG DIAGTLDAQV VTGLATGGSV
VSNNITEPFY LSDAKFAIMA RMGLREQQQN STMRANSVTD SVGGLVAKST SVAEAAEHVK
TALIQRVAKM LQTQTSEIDT SRPLHSYGID SLVAIEVVNW AFKELKATLT VFDIMAAVPI
MTTAAKMAAG SAWLSKEVAA AS
//
