CURS1_ASPTE
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 03-AUG-2022, entry version 42.
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:0009058; P:biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 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; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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 Pfam; PF00698; Acyl_transf_1; 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; 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; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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 2302..2379
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:23335766, ECO:0000305|PubMed:26493380"
FT REGION 13..436
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT 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 942..1256
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT ECO:0000305|PubMed:26493380"
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:PRU10022"
FT ACT_SITE 641
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 972
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
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
