DHC5_ALTCI
ID DHC5_ALTCI Reviewed; 2079 AA.
AC A0A0N7D745;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Non-reducing polyketide synthase Dhc5 {ECO:0000303|PubMed:26493380};
DE EC=2.3.1.- {ECO:0000269|PubMed:26493380};
DE AltName: Full=Dehydrocurvularin biosynthesis protein 5 {ECO:0000303|PubMed:26493380};
GN Name=Dhc5 {ECO:0000303|PubMed:26493380};
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}.
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; KT271474; AKQ49203.1; -; mRNA.
DR AlphaFoldDB; A0A0N7D745; -.
DR SMR; A0A0N7D745; -.
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; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
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; PF14765; PS-DH; 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 SMART; SM00824; PKS_TE; 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 2: Evidence at transcript level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..2079
FT /note="Non-reducing polyketide synthase Dhc5"
FT /id="PRO_0000438390"
FT DOMAIN 1641..1718
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:26493380"
FT REGION 369..801
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26493380"
FT REGION 895..1199
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26493380"
FT REGION 1304..1581
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26493380"
FT REGION 1613..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1721..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1812..2057
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26493380"
FT COMPBIAS 1613..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1784
FT /note="Basic and acidic 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 2064
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7"
FT MOD_RES 1678
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2079 AA; 227696 MW; E8EDFE088E2AD791 CRC64;
MKTGHRTVLL FGDVTDPWIE GIDHVYVQAA KKPWIRSFLE DLFSAIKTET KAMDRVLQEG
FKDSSSFQEL AERYRHAGDD FGMAHAMMIY AIRAVVLLET LSREPHILDE SRPRPEVIGI
SGGLFSAAVM SISINFETLY AACIEAGRVW SRLCNLTLVR SRAMEESPGT WGWAILGIPA
ADLGKTLEQF QSSMGIHCSK RAKVGVIGDR WSTVIGPPSV LELTLSECPN LKNLPKDELN
IHALQHTLSV SNSDIDYIVG NSPLLETPLP PGYRIHGLDD DFPEANYAEW RHLLRASAYQ
TLSRPLDIVQ AVSNLNAALG VSKDIDAKII GPSSHTTYLV KCLQTAGKEV LIQNGFPASP
QTSGTNDGIA IVGMAGKGPG SDDLEEFWNV ILKGLDLHEE VPSDRFNLEE YYSPKHPPAG
PGRCTMTCRH GCFMNNPGHF DSKFFHISPR EAMLMDPAHR LFLMNAYEAL EMAGYSNGQT
KSTNPTKIAT FFGQCNDDWH VVGHRALGCD AYTLQAVQRA FGPGRLAFQF NWEGPTYALD
SACAATSSCI HLACMSLITR DIDMAVAGAA NVLSTPHSFT SLSRSGVLSD SGNCKTYRDD
ADGYCRADFS GAVVLKRLDD AIAQNDNILA VISSSARNHS GNSTSITTSD AAAQERLFQK
VLRNARVTPQ DISYVEMHGT GTQVGDKAEI GAVSSVFSKR IDGRPLNVGA IKANIGHSEA
AAGMSSLLKS ILMFQNSTIP PQAGMPHTLN PNFPPLHEIN IQIPSEPLEF KTTDNKPRRI
LLNNFDAAGG NACLLLEDYT DTKERNADVR SAHTIVMSAR TQSSQLLNKK RLLRWLRSKP
NTRVEDLAYT TTARRMHHPI RSAIIASTTQ EVIAKLEAEI ERNDSSLVQR ASPLVFVFTG
QGSHYGGMGS ELYGSSPIFR ERVDLCASIC AGYDFPPFLD IITNETVNVS TKNASQVQLA
VLTLEMALTH FWRSAGIEPT MVIGHSLGEY AALHAAGVLS LADALYLVGH RSLLLLERCE
SDSCSMLSVS MSVDEVQAQL TRIRSSCNVA CINSSTSTVV SGTAEDLAEF QSSITAQNAK
VRAKKLSLPF AFHSFQMDPI LEDYSRIAAG VTYSAPKIPV ASTLLGSVVN REGIFTQEYM
VQQTRQAADF MGGLVAVKSE LADPLWLEVG PAPVCMSFVR DTLSTPASKM THSLQPKTSN
WMSLSKTLAA MYTSGVDIDW LAFHAPYESD LKLLTLPSYA WDVRNFWITH TDNATEVVSE
QSPVTSSEPL ISTCAQYLVA KSSSPNIRVA LRASIADPGF MGLMDGHKMQ GIGLCSGSVF
CEAAFAATKY ALEYSGRKNI TQPWLTLHDP KLLLPLTKKS VGPDGDLVTT AVMYSSSAET
ISITFQVTSA SASYDLGTCV VKVRDPTRSQ VEWDRISYFI KARMDETIKN AKEGRGHRMQ
PEVFYALFGN AVEFAPDFQG INEAYIAKDF QEAAAVVTLP HDPSGTRFTF SPYWGEALVH
LAGFMVNGNP SKSPKTTFIV MGFASVEQTA PLIPGKQYMT YTRISKWVKD TAYCDAIVFD
PESFTIVLQC VDIRYQELPR ATWKHVLEGP HETPIVHAQR PPVRNSKKYV ETRELQQPSS
ATVPAQETTI DEPEQQEGEP AAGARLFNAI LDSISKATGT DPSEFRDDTM IADLGVDSIM
AIEVVATVKD VSGLELPAAF VFEYPTIGDL RKEFRANEPT VENPRFSATP SSAEASIPSS
PSSLAHPMSD SASSLSPSDR EEALPLERQS MTKREQKRPV KIDDDASPEP VVRIMLLQGR
PGSKRIPFYM MADGTGTIAT YIHLPPFKSK MPVYGIDSPF LRCPKRLTKE VGIEGVAKLI
VDALMKTQPE GPLMIGGFSA GSIVAYEVCR QLGRAGRQVE GLVLIDMCCP RSSLLDEDKM
NSEDDASFAI FESAVTKDGL WSSSETTQQH FRAYHVAMHA YHPPYMLEEE RPTRTAVIWA
EKGMVNRVMG NEKLMKMLVE QGIPMTSYPG YMEDPKLGAF ACLVPDRTKA DLGPNGWEKY
TAGEVLTLSV AGDHLDLPMP GHVHLLHAQM EKAFAYIKG
