CURS2_ASPTE
ID CURS2_ASPTE Reviewed; 2083 AA.
AC L7XAV2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Non-reducing polyketide synthase curS2 {ECO:0000303|PubMed:23335766};
DE EC=2.3.1.- {ECO:0000269|PubMed:23335766};
DE AltName: Full=Dehydrocurvularin biosynthesis protein 2 {ECO:0000303|PubMed:23335766};
GN Name=curS2 {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: Non-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}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (By similarity).
CC {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DOMAIN: The release of the polyketide chain from the non-reducing
CC polyketide synthase is mediated by the thioesterase (TE) domain
CC localized at the C-ter of the protein (By similarity).
CC {ECO:0000250|UniProtKB:Q5ATJ7}.
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DR EMBL; JX971534; AGC95321.1; -; Genomic_DNA.
DR AlphaFoldDB; L7XAV2; -.
DR SMR; L7XAV2; -.
DR PRIDE; L7XAV2; -.
DR VEuPathDB; FungiDB:ATEG_00145; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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 Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
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; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..2083
FT /note="Non-reducing polyketide synthase curS2"
FT /id="PRO_0000438388"
FT DOMAIN 1637..1714
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 9..246
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT ECO:0000305|PubMed:26493380"
FT REGION 369..801
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT ECO:0000305|PubMed:26493380"
FT REGION 895..1201
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT ECO:0000305|PubMed:26493380"
FT REGION 1285..1581
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT ECO:0000305|PubMed:26493380"
FT REGION 1710..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..2058
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23335766,
FT ECO:0000305|PubMed:26493380"
FT COMPBIAS 1717..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 543
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 986
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2065
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7"
FT MOD_RES 1674
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2083 AA; 226314 MW; B768DF9911078809 CRC64;
MDSNRPAVLL FGDVTDPWVD GIDYVYSQAA TTPWLRSFLR DLFTVLKVEM RTMDRTLQES
FRDCGSFQEL AERYRHTGDD FGMAHAMLTY VIRAVVLLET ISAEPHLLDS NRPRPELIGV
SGGLFSAAVV SVSTNFQSLY DTCLEAGRVW ARLCNLTLVK SRAIEERPGT WGWAVLGIPA
GKLSQTLEQF QNDMGVPSAK RARVGVTGDR WSTVIGPPSI LELVLNECPT LKNLPKNELD
IHALQHTLDI SNADIDYIVG DSSLLDTPLP QGYRIYGLDD DRPEATYPSW SHLLRASASQ
TLARPLNIVQ AVSKLNAALG TSTHVDFKIM GPSSHAAYIA KVLQTAGREV SLQDRITAKP
PTPDSRDGIA IVGMAGKGPG SDDLEEFWDV LLKGLDLHQE VPPDRYDLDE YYSPKHPPAG
PGKCTMTCRH GCFMNNPGHF DSKFFHISPR EALLMDPAHR LFLMNAYEAL EMAGYSDGQT
KMTDPTKIAT FFGQCNDDWH VVGHRTLGCD AYTLQAVQRA FGPGRLAFQF NWEGPTYALD
SACAATSSCI HLACMSLIAR DIDMAVAGAA NVLSTPHSFT SLSRSGVLSD SGNCKTYRDD
ADGYCRADFS GAVVLKRLDD AIAHNDNILA VISSSARNHS GNSTSITTSD AAAQERLFHK
VLRNARVTPE DISYVEMHGT GTQVGDKAEM GAVSSVFSKR RDGELLPVGA IKANLGHSEA
AAGMSSLLKS ILMFQKGTIP PQAGMPHTLN PNFPPLHEIN IKIPEEPLEF KSVGGKPRRI
LLNNFDAAGG NACLLLEDYT HTKEREADVR SAHTIVTSAR TQASHLLNKQ RLLKWLRSNP
NTRIEDLAYT TTARRMHHPI RFALTASTTQ EAISKLESEI ERNTNSPASR HVPVVFVFTG
QGSHYAGMGA ELYRTSSAFR ERVDLCVDIC AGNNFAPFVD IITDEGVDVS SKTAAQVQLA
VLTLEMALTH FWRLAGIEPA MVMGHSLGEY AALHAAGVLS LADALYLVGH RALILQERCE
SGSCSMLSVS TSVANVREQL SQLQSSSCGV ACINSPSSTV VSGIAEDLAE FQANITAQDA
KVRTKTLSIP FAFHSFQMDP ILQDYGTIAA GVTFSAPKIP VASTLLGSIV GEPGVFDHDY
LVQQTRQPVN FVGGLNAVQS KLSDPLWLEI GPSPVCVSFV RDTLSPSLSK LTHTLQPNTH
NWASISKSLA AAYINGVDID WVALHAPYET NLQLLTLPSY AWDVKDYWIT HTDRVTEAVP
EQSPVTGSGP LVSTCAQYLV SKSSSPKVQV VFRASISDPG FMELIDGHKM QGIGLCSGSV
FCEAAFAAAK YALEYSGRRN VTQPWLTLQK PELLLPLTKK LAGADGSLIT TAVMDSPSAH
RISVTFKLTS GSESHELGSC IVNFRDPAKT QADWDRVSYF IQARMDEVIK NAKEGPGHRM
QPEVFYALFA NAVEFSTDFQ GVDEAYIAKD FQEAAALVTL PHDPAGTKFT FSPYWGEALV
HLAGFMVNGN PSKSPQKTFI VMGFESVEQT VPLVPGKKYM AYTRISKWVK ETAYCDAVVF
DPETSNIILQ CIDLRYQELP RVTWKHVLDG PHGGSSAHGH KAPVQETKKA VEVSRQAVAV
APVQPQPAEV GEDDDDDFDE GLVDAILDSI SKATGSDPSE FTDDTIVADL GVDSIMAIEV
VATVKEQSGL DLPATFVLEH PTIGDLRRAF GANKPKTSKP QPGSTTPSSS QSSIPSSPNP
EPTSMSDTAS SLGSSLVDIE KDQTFTPPPE LEPKPNHHLG KMDETDTSPA PTVRITLLQG
RPSPKRTPFY MMADGTGTIA TYIHLPAFKS KMPVYGIDSP FLRCPSRLTK DVGIPGVAKL
IVDALVTAQP TGPLMIGGFS AGSIVAYEVT RQLGALGRQV TGLVLIDMCC PRSSLLDEDA
MNSEDDASFA IFENAVSKDG LWSLASTTQD HFRAYHVAMH AYHPPYMTAQ ERPSHTAVIW
AEKGMVNRVV GNDRLMQMLA DQGIPTTSYP GYMEDPRLGA FACLVPDRTA ADLGPNGWEK
YTAGEVLALS VAGDHLDLPM PGHVHLLQRE MEKAFAYFEG EST
