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Database: UniProt
Entry: L7X8J4
LinkDB: L7X8J4
Original site: L7X8J4 
ID   CURS1_ASPTE             Reviewed;        2387 AA.
AC   L7X8J4;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Highly reducing polyketide synthase curS1 {ECO:0000303|PubMed:23335766};
DE            EC=2.3.1.- {ECO:0000269|PubMed:23335766};
DE   AltName: Full=Dehydrocurvularin biosynthesis protein 1 {ECO:0000303|PubMed:26493380};
GN   Name=curS1 {ECO:0000303|PubMed:23335766};
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=AH-02-30-F7;
RX   PubMed=23335766; DOI=10.1128/aem.03334-12;
RA   Xu Y., Espinosa-Artiles P., Schubert V., Xu Y.M., Zhang W., Lin M.,
RA   Gunatilaka A.A., Sussmuth R., Molnar I.;
RT   "Characterization of the biosynthetic genes for 10,11-dehydrocurvularin, a
RT   heat shock response-modulating anticancer fungal polyketide from
RT   Aspergillus terreus.";
RL   Appl. Environ. Microbiol. 79:2038-2047(2013).
RN   [2]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=26493380; DOI=10.1002/cbic.201500428;
RA   Cochrane R.V., Gao Z., Lambkin G.R., Xu W., Winter J.M., Marcus S.L.,
RA   Tang Y., Vederas J.C.;
RT   "Comparison of 10,11-dehydrocurvularin polyketide synthases from Alternaria
RT   cinerariae and Aspergillus terreus highlights key structural motifs.";
RL   ChemBioChem 16:2479-2483(2015).
CC   -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of 10,11-dehydrocurvularin, a prevalent
CC       fungal phytotoxin with heat shock response and immune-modulatory
CC       activities (PubMed:23335766, PubMed:26493380). The highly reducing
CC       polyketide synthase curS1 is responsible for biosynthesis up to the
CC       tetraketide stage (PubMed:23335766). The non-reducing polyketide
CC       synthase curS2 then conducts four additional chain extension cycles,
CC       producing the unreduced part of the nascent octaketide from C-1 to C-8
CC       in 10,11-dehydrocurvularin (PubMed:23335766).
CC       {ECO:0000269|PubMed:23335766, ECO:0000305|PubMed:26493380}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:23335766}.
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DR   EMBL; JX971534; AGC95324.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7X8J4; -.
DR   SMR; L7X8J4; -.
DR   VEuPathDB; FungiDB:ATEG_07282; -.
DR   GO; GO:0016746; F:acyltransferase 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: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; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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; 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; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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; 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; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS52019; PKS_MFAS_DH; 1.
PE   1: Evidence at protein level;
KW   Multifunctional enzyme; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW   Transferase.
FT   CHAIN           1..2387
FT                   /note="Highly reducing polyketide synthase curS1"
FT                   /id="PRO_0000438387"
FT   DOMAIN          10..433
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348,
FT                   ECO:0000305|PubMed:23335766, ECO:0000305|PubMed:26493380"
FT   DOMAIN          940..1259
FT                   /note="PKS/mFAS DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   DOMAIN          2302..2379
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:23335766, ECO:0000305|PubMed:26493380"
FT   REGION          551..891
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT                   ECO:0000305|PubMed:26493380"
FT   REGION          940..1075
FT                   /note="N-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          942..1256
FT                   /note="Dehydratase (DH) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT                   ECO:0000305|PubMed:26493380"
FT   REGION          1103..1259
FT                   /note="C-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          1673..1987
FT                   /note="Enoylreductase (ER) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT                   ECO:0000305|PubMed:26493380"
FT   REGION          2011..2191
FT                   /note="Catalytic ketoreductase (KRc) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT                   ECO:0000305|PubMed:26493380"
FT   ACT_SITE        182
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        316
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        356
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        641
FT                   /note="For malonyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        972
FT                   /note="Proton acceptor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        1169
FT                   /note="Proton donor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   MOD_RES         2339
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2387 AA;  259800 MW;  26F6149D396901FA CRC64;
     MPSAQHSVGD VPIAVVGLSC RFPGDASTPS KFWDMLKNGK DAYSPTSTRW NSDAFYHPGD
     GRLNSLPTKG GHFLKEDPYV FDAAFFNITA AEAIALDPKQ RIAMEVTYEA FENAGMSLQQ
     ISGSQTACYI GSGPSDYRGA VERDFLHNPK YHLLGTGDEM ISNRISHFLD IHGPSATVQT
     ACSSSLMATH LACQSLRSGE SEMAITGGIS LMLTPDFTTH LNNLTFLNPE GLSKAFDESA
     GGYGRGEGCG IIILKRLADA IQDGDDIRAV IRGTGANSDG FTQGVTMPSF EAQAALIRQV
     YSSNGLDYST QYVEAHGTGT KAGDPIETRA IYSTIGKGSP KPRKLFVGSV KPNIGHLESA
     AGVSGIIKGI LSMEHNLIPP NLHFTKANPA IPFDEWNMAV PTKLTPWPVA ATKRMSVSGF
     GMGGTNGHVV LESFDSTRST NGSGYSGGFS TFEKTRTKKR LFVFSSHDQA GFKRNANALA
     EHLDTVGSVA SSSDFMANLA HTLSGARSSL SWRATCIAEN KIELRDYLTT KPGDGASRDA
     TNATRAPRIG FVFTGQGAQW ARMGVEMLDR PVFRDSVAQS THYLQAMGCV WDPVAELKKT
     QADSRLSQPE ISQPICSVLQ IALVDELRSW GVTPSKVVGH SSGEIAAAYS IGALSHRDAI
     AAAYFRGVAT VRLRADAPDL KGGMMAVGCS RDEAEELIEQ SKLDGTAAVA CVNSPSSVTL
     SGDVDTLEQL RAICDEHKVF VRRLKVEMAY HSRHMNRVSG TYAEFIADLQ PIPREYNENE
     DDDSIQTMLS SVTGQEVAPE LLGPYYWVRN LVSPVLFSDA VKEMVAPDEA EGDNTVDLLI
     EIGPHGALGG PVEQILGHHG VKHITYKSML TRGRNALETS LELASELFLK GVPIDISQVN
     SDLNPRRLTD LPPYQWNHSK VFRHETRIQR ELVMRQFPSK SIIGAQVPMM DESQHVWRNF
     LRLSDEPWIR GHKVGSTVLF PAAGLIGMAL EAAQQLVEPS KTARSLRLRD ISFFAAMALS
     EDVPTEVIMH LRPHLLATSG STPAAWWEFT ISSCAGIDNL RDNCRGLITI DYAETTSEQM
     ASEDASLEAS RIAHYHRVRE ESSYTYSKED FYSQFEKIAW NYGEAFRGVE KVYLGDGQAT
     YDVKLVDIGE TASKGQLDRP FLIHAGALDS ILQGCLGSTY RNGRFDMDKP VLPTFIGQME
     ISLDIPGDAG YVLPAVCESK RHGFKELSSN IYAFDSAVSK VNLSVVDYRV SELENDSGEQ
     DSQQLEVDPA EITSEVRWNY ALEVLEPEEI KKVVLAVAAE DRVVELIRLY LHNNPAATVI
     ELVPDYEALE RATMSLLPPG TILPSHIKYA VAATGSKSEN QVDIENVIGT PFDLGDLDDT
     LPTDIAAADL LVIPQSVNNH KDLGVLLTRL TSFGKPDASL VLAVNSSVNV SNSMLESKGF
     RRVFDLENSV ALYKSRQSGH TNGHTNGHTN GTSTRSELFI IEPLATSSRI NSFSGALQVT
     LREHGYPVFV TNWTEISARP AADLEGNTFI SLLELEQPLL DALSEPDFYS VRKLLLNSDR
     LLWITAGDNP SMGVVDGIRR TMRSEVAGLK FQVLHLSSLD TALQCGPALA GRIMTTDTKD
     DEFQERDGML QVARIFNSPE GNEGVRRCLE DSVRVERLGE QERALRLTIM KPGLMDTLTF
     IEDDRMTGPL GATEIEVDVK ATGVNFKDIM AAMGLVEVSL IGQEASGIVT ATGSTAASRF
     KPGDRVTLLW EGMHVTKLRI DHRLAVHIPD SMSFEEAAAL PMVHTTAYHA LVNVAKLRPG
     QSVLIHAAAG GVGQAALQLA THLGLVAYVT VGSEDKRRLL MEKYNVPEAH IFHSRDTSFA
     KAIKRVTGGR GVDCVLNSLS GELLRVSWTC LAPFGTFVEI GLRDITNNMR LDMRPFSRST
     TFAFINIANF FDPEGLDALG QILSDAFALV HKGVLGTAYP LTVYPVSELE TAFRTMQQGK
     HRGKLVLSFG DNAQAPVLCK ARDSLRLSPK STYLFIGGLG GLGRSLAREF VACGARHIAF
     ISRSGDSSAE AKATVQALTT LGANVKAYRA DVSEEAAFLS AMQQCATDLP PIAGVVQMAM
     LLRDTLFEKI SYTDWTQPMR PKIQGTLNLH NYFSATRPLD FFVICSSISG IFGYPGQTQY
     AAANTFQDAL ARHRRNQGLK GVAVDLGIMR DVGILAEQGT TGKLADWEAI LGIREKPFHA
     LMKSVINSEW KGAVPPPAQL CTGLGTADIM ARFGLERPEH FSDPRFGPLN VLSIESSSSL
     STDQDTASSP STRLAAATTL DEAVVIITDA LVHKMAEILQ MPLSEVDPGR PMYRYGVDSL
     VALEVRNWIT RELQANMALL EILAAEPMRV FAGKIAEKSK LVAGRKG
//
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