DHC3_ALTCI
ID DHC3_ALTCI Reviewed; 2389 AA.
AC A0A0N7D4P6;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Highly reducing polyketide synthase Dhc3 {ECO:0000303|PubMed:26493380};
DE EC=2.3.1.- {ECO:0000269|PubMed:26493380};
DE AltName: Full=Dehydrocurvularin biosynthesis protein 3 {ECO:0000303|PubMed:26493380};
GN Name=Dhc3;
OS Alternaria cinerariae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Sonchi.
OX NCBI_TaxID=216837;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 11784;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 11784;
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:26493380). The highly reducing polyketide synthase
CC Dhc3 is responsible for biosynthesis up to the tetraketide stage
CC (PubMed:26493380). The non-reducing polyketide synthase Dhc5 then
CC conducts four additional chain extension cycles, producing the
CC unreduced part of the nascent octaketide from C-1 to C-8 in 10,11-
CC dehydrocurvularin (PubMed:26493380). {ECO:0000269|PubMed:26493380}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:26493380}.
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DR EMBL; KT271472; AKQ49201.1; -; mRNA.
DR AlphaFoldDB; A0A0N7D4P6; -.
DR SMR; A0A0N7D4P6; -.
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 2: Evidence at transcript level;
KW Multifunctional enzyme; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Transferase.
FT CHAIN 1..2389
FT /note="Highly reducing polyketide synthase Dhc3"
FT /id="PRO_0000438389"
FT DOMAIN 2302..2379
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 12..436
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26493380"
FT REGION 551..861
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26493380"
FT REGION 946..1262
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26493380"
FT REGION 1673..1987
FT /note="Enoylreductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26493380"
FT REGION 2011..2191
FT /note="Catalytic ketoreductase (KRc) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26493380"
FT ACT_SITE 181
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 976
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 2389 AA; 260632 MW; C6B66D224A958ED4 CRC64;
MPSATPSLDV PIAVVGLACR FPGDASSPSK FWDMVKNGRD AYSPTSSRWN SDAFYHPVNG
KLNSLPTKGG HFLKEDPYVF DASFFNITAA EAIALDPKQR MALEVAYEAF ENANMPLQQI
SGTQTACYIG SGPSDYRGSV ERDFLHNPKY HLLGTGDEMI SNRISHFFDI HGPSATIQTA
CSSSLMATHL ACQSLKSGES DMAVTGGVSL MLTPDFTTHL NNLTFLNPQG RSKAFGESAG
GYGRGEGCGI IILKRLDRAI QDGDSIRAVI RATGANSDGF TQGITMPSYE AQAALIKYVY
ESHGLDYDST QYVEAHGTGT KVGDPIEMKA IYNTIGKGSS KPRKLYVGSV KPNIGHLESA
AGVSGIIKGI LAMEHNLIPP NIHFTKGNPN IPFHEWNVAV PLKPTAWPVS QTKRMSVSGF
GMGGTNGHAV LESFNPSRLA DAAVKHGDLT RFQKVRNKKR LFVFSSHDQA GFKRNADALV
HHIENLGSAA SSSEFLANLA HTLSGAKSSL SWRATCLAEN TTEICDYLSN KPGDGAFRAT
SIENTTPRIG FVFTGQGAQW ARMGVEMLDR QVFRDSIEQS ATYLRDMGCL WDPIAELEKA
QAESRLSYPE ISQPICSVLQ IALVDELQSW GVVPSRVVGH SSGEIAAAYS IGALSHRDAV
AAAYFRGIAA TKLQTDAPDL KGGMMAVGCS RDEADDVIEQ SNLSGTAVVA CVNSPSSVTL
SGDVDSLEQL RAIFDDRKIF ARRLKVEMAY HSRHMNRVFG TYSASIADLE PITQEETNED
GDFQIQTMVS SVTGQEVASE LLGPYYWVRN LISPVLFSDA VKELVSPDDY DENKGSSSAV
DLLIEIGPHS ALSGPVEQIL NHHGIRNVGY KSMLIRGRNA VETSLELASE LYLDGIPLDI
SKVNGDLKVR RLTDLPPYQW NHSKVFRHEN RIQTELMTRR FPSRSLIGAQ VPMMDESQHV
WRNFLRLADE PWLRGHKIGS TVLFPAAGLV SMAIEAARQL VEPGKTARSL RFREVSFSAA
MALSEDVATE VILHMRPHLI ATSGSTPSSW WELTISSCVG TSQLRDNCRG LITIDYADTT
SEQMAKENAN FENFMISEYY RVHNGCPDIC SKEDFYGQFE KITWSYGEAF QGVENVHPGD
GESTYDVRLV DIGETFSKDQ SDRPFLIHAG TLDSILQGCL GSTYKNGRFE TSKPVLPTFI
GEMEISLDIP GDVGYVMPGL CESKRHGFKE LSSNINIFDT GLSKVILSVV GYRVSELEND
TEAQDTQQLE VDPADITSVV RWNCSVAIAT QEELQKLMLA SAPEARVLEL VLLHIHNNPS
ATVIELTREI EPTNHTVMSQ LPNGTVQSNQ LHYAAISVET PLEGSTFNAL SSVNSFYLGE
SDDSSRRGVT TADLLIVPQA VSDCENIENL LDRLITLGKP DAALILESQK SFDQLASILK
TKGFQCVLEV QRSIALFKRQ ISQPTNGLPN CTSATRDFTI VDSLAPTEDT NAFSHNLRAT
LANQGYTVCV ATWTEISACT ETELEGKTII SLMELNKPML SSLSESDFHD FRKLVLSSER
LLWVNAGDDP SMGMIDGIRR TMRSEVAGIK FQVLRLSSLK TALQCGPSLV SRILTTESQD
DEYRERNGML EVARIYNNPE INADVRHCLT DSFRVQRLAD QVKPLRLTIG KPGLLDTLAF
IEDDRMKTAL GETEIQVDIK ATGINFKDIM AAMGLVGVSL IGQEASGIVT ATGSAAASRF
KPGDRVTLLW EGMHATKLQL DHRLAVHIPD SMSFEEASAL PMVHVTAYHA LINIAKLRRG
QSILVHAAAG GVGQAALQLA TYLGLTVYAT VGSDDKRSLL MTKYNIPDAH IFCSRDASFL
KAIKRVTGGH GVDCVLNSLS GELLRVSWAC LAPFGTFVEI GLRDITNNMR LDMRPFSQST
TFAFINIANF FCAESLDALG NIISDTFDLV HQGVLRSPYP LTVYPVSELG TAFRTMQQGK
HRGKLVLSFE GNAQVPVLCK AKDALHLKPD ATYLFVGGLG GLGRSLAQEF IACGARHIAF
VSRSGDTSKK AKATVDHLTA LGAVVKAYQA DIANEDAFLS AMQQCAADLP PIAGVLQMAM
LLRDTLFEKM SYEDWTGPTR PKIQGTLSLH RYFSATRPLD FFLICSSISG IFGYAGQTAY
AAANTFQDAL AQHRRNQGLK AVAVDLGIMR DVGILAEQGT TGKLALWEAV LGIREKAFHA
LMKSIINREC KGEACPAQIC TGLGTADVMK KFGLERPEHF ADPRFGPLDV LNIDATSSPN
ADDSAVVSSP STRLASASTF QEAVSIITDA LVHKTAEILL MPVSEVDPSR PMYRYGVDSL
VALEVRNWIA RELQANMALL EILTAVPMRE FAEKIAEKSK LVTMGNGER
