ID A0A0F4YWL7_TALEM Unreviewed; 2441 AA.
AC A0A0F4YWL7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Lovastatin nonaketide synthase {ECO:0000313|EMBL:KKA22033.1};
DE EC=2.3.1.161 {ECO:0000313|EMBL:KKA22033.1};
GN ORFNames=T310_3923 {ECO:0000313|EMBL:KKA22033.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA22033.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA22033.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA22033.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA22033.1}.
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DR EMBL; LASV01000160; KKA22033.1; -; Genomic_DNA.
DR RefSeq; XP_013328645.1; XM_013473191.1.
DR STRING; 1408163.A0A0F4YWL7; -.
DR GeneID; 25316272; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0050637; F:lovastatin nonaketide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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; IPR011032; GroES-like_sf.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF49; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF08242; Methyltransf_12; 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; 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:0000313|EMBL:KKA22033.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKA22033.1}.
FT DOMAIN 37..455
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2346..2422
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2441 AA; 268479 MW; 2FDF963E19C43105 CRC64;
MGDCGLNGVY TNATVNGISP LSSSSTSHGT RDREMTVEPI AITGIGLRLP GRIHDASSFW
KFLTSKGSGR CRVPPDRYNV DAFYRPGKAG HTCTDFGYFL DDVDLATMDT SFWSMSRREV
EVMDPQQRLM LEVVYECLES PGTTDYKGKA IGCYVGVFGE DWADLQAKDT LNSGPYRVPG
YGDFAISNRV SYEFGFVGPS MTIRTACSSS LTALYEACQA LYAGECSSAV VGGSNIILSP
HMTVAMTEQG VLSPTGLCKS FDASADGYAR GEAVNAIYIK KLSDAIRDKD PIRAVIRSAC
INSDGKTAGW SLPNPRCHEA LIRRSHQIAG ITDLSQTAMI ECHGTGTPVG DPLEAGAVAN
VFGDWGILIG SVKSNLGHSE GAAGLTGVIK MILALENKAI PPNINFKTPN PKIPFERARM
RVPVECEAWP EGKAERVGVS SYGIGGANAH VLLDSAASFG IETTKNGLQH DRLPHLLVFS
ATHVESLRRN IQNIEQYVQS HPSSIRDLSY TLCCRRERFR HRAFAISNAT EDASLDISGL
KKASQSPTIV FVFTGQGAQY AQMGKDLFLH NAVFVETIKK LDAALKSIDA SISWSLEEEL
LRAEDESRLS EALFSQPCCT AIQIALVDVL RSINVHPTAV VGHSSGEIAA AYACGSLSAA
DAIAVAYHRG QVSAKMEKEG KGGMLAVGLS RDAVLKYLTK GIAVGCENSP DNVTLTGESD
VLDSVAQSIQ NEHPDVLIRR LRVKCAYHSS RMKGVEDEYL SRMNVKTRNL TATFFSSVTG
EKVMSGDLLG PSYWCSNLTS PVLFSRAVSR LLEDVSPNSV FVEVGPHSAL SGPLRQISQH
VVRPIQCIST LVRKTNSHEA ILRTAGQLFQ VGAPIDLSPL NPEGGRVLHD LPTYAWNHEG
RYWSESRLMR GWRMREFPRH DLLGIRITDG SDLEPTWRNV LRLNDTPWLR DHDIMGETVF
PAAGYVSIAG EAIRQLTGSS DFSVRNVNIL TAMVLQKDAS AEIVTQFRPV RLTTTLNSSS
WYDFTIASLL DGKWTRNCTG QARPGRDFAI PAAHPEPGVR LVEPDVWYRV MKKFGFNYGP
RFHGLRDITS SITERKATAR VDDFVDVDNL ESPYTMHPCT IDCIFQLFSV AQCQAIPRLF
DHLAVPTSIE ELYVCSPSST ISVQASANPM PKGGFFGDAV GFCGDQVVFH LRNMRLSRLT
DGEERRGVDL HAGAQLVWKP DVDFMDVTSL IRPLQDSAAD NTHLLIEELA LTCMIETEYR
VQNKVASQPH YAKFQGWLRL QRSNAEQGLY EHVPGCAGIV TMSSEKRVQH VHKLLEKALL
TEGKKAATAI SSVFEEVVNI FDDKVNPLEL LLKDDLLADI YHFRPLCDYA DFFRLLAHSK
PNMKILEIGA GTGGMTATIL PVLKNSSPRG ERMYGSYTYT DLSAGFFVAA KERFKDYDAI
TYRVLDISAD PIVQGFDSES YDLIVASNEL SPTTKWVNYV MGLLPGWWLG EADNRPTEPY
VSPARWDIEL RNSGFSGAEA VVYDGYLNAH IISSPRKESQ NALEKRVTIL RQSKPSSVAD
SLHVYLENNG FQINIRFLGG EKVPFGQPVV SVLDLEEEPF IHSLTSDRFD QFKALLLSEL
EGCPATLWVT RPCQVACTDP RYAMILGLAR TIRTELAMNF ATLELDSFDE AAWSACTKVI
DKLMERSPDE VLNPVMEFVY SSGTVLTGRF YPVVVGDELL DKAPSTKSVI KKLDIGKRGF
LQTLAWKQST IEPPQHDDWV EVETRAVGLN FRDVLTAMGV VEAKDLGVEC SGIVTRIGPE
VKALAPGDHV VVFSGGTFSS ALMTTERLCA KIAANLSFVE AAALPCVFAT VIHSLMDVAR
LKKGHIYCTV GSAAKVEYLQ NTLGIPRERI FNSRDNTFLR DVLAATDGRG VDVVLNSLSG
ELLHASWKCV AEFGTMVEIG KRDFIGKASL AMDAFESNRS FVGVDFTRIC AQRPEITQEL
LKRCMEYFQQ GSITPLPTKE FEAAHVEQAF RYMQKGTHIG KVVVTMPESS AELPSTPAVK
QLSFRSEGCH IIVGGLGGLG RPVSAWMVMH GARHLVFFSR SSGKNPHHEA FVSELRSQNC
RVDLVAGDVS SADDVDSLVR DLDVNVAGVM QASMVLKALT GRQDVSLSKM TFNDWQTVVS
PKVQGTWNLH NALEKCQKKP DYFVLFSSTS GLVGQWGQAN YAAGNTFWTH SSSFDIRVME
DVGYVSRNDY LLEHFRSTAT HTLQEQDLLE SLHLMIDRSL PSAPEEFDSS AYTSKSQLCI
GLRTTLPLSL PNNRTVWKRD PRMAIYHNLS SQDRAKSDTH RDDDEALKQF LVEANRRPAM
LQTPGSAEFL AQHIGRMLFG FMLRDLSDID YDVSLPALGV DSLVAIELRN WFKLKLGLDV
TVLEILGGAS LTQLGQMSAN NLAKRAAATS STDPSESVGV M
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