DPASA_ARTSH
ID DPASA_ARTSH Reviewed; 2159 AA.
AC P9WEX0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 8.
DE RecName: Full=Non-reducing polyketide synthase dpasA {ECO:0000303|PubMed:32286350};
DE EC=2.3.1.- {ECO:0000269|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein A {ECO:0000303|PubMed:32286350};
GN Name=dpasA {ECO:0000303|PubMed:32286350};
OS Arthrinium sacchari (Coniosporium sacchari).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Apiosporaceae; Apiospora.
OX NCBI_TaxID=166626;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND BIOTECHNOLOGY.
RX PubMed=32286350; DOI=10.1038/s41467-020-15664-4;
RA Tsukada K., Shinki S., Kaneko A., Murakami K., Irie K., Murai M.,
RA Miyoshi H., Dan S., Kawaji K., Hayashi H., Kodama E.N., Hori A., Salim E.,
RA Kuraishi T., Hirata N., Kanda Y., Asai T.;
RT "Synthetic biology based construction of biological activity-related
RT library of fungal decalin-containing diterpenoid pyrones.";
RL Nat. Commun. 11:1830-1830(2020).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of the diterpenoid pyrones subglutinols
CC A and B (PubMed:32286350). The first step of the pathway is the
CC synthesis of the alpha-pyrone moiety by the polyketide synthase dpasA
CC via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA
CC units and 2 methylations (PubMed:32286350). The alpha-pyrone is then
CC combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP
CC synthase dpasD through the action of the prenyltransferase dpasC to
CC yield a linear alpha-pyrone diterpenoid (PubMed:32286350). Subsequent
CC steps in the diterpenoid pyrone biosynthetic pathway involve the
CC decalin core formation, which is initiated by the epoxidation of the
CC C10-C11 olefin by the FAD-dependent oxidoreductase dpasE, and is
CC followed by a cyclization cascade catalyzed by the terpene cyclase
CC dpasB (PubMed:32286350). The FAD-linked oxidoreductase dpasF is then
CC involved in tetrahydrofuran (THF) ring formation at the C5 unit to
CC complete the formation of subglutinols A and B (PubMed:32286350). DpasF
CC possesses also an additional catalytic ability of multi-step oxidations
CC to generate a new DDP analog with an enone system at the C5 named FDDP
CC A (PubMed:32286350). {ECO:0000269|PubMed:32286350}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:32286350}.
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; a methyltransferase (CMeT) domain
CC responsible for methylations; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm. {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Diterpenoid pyrones display various biological
CC activities and subglutinol A shows insecticidal and anti-HIV
CC activities. {ECO:0000269|PubMed:32286350}.
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DR AlphaFoldDB; P9WEX0; -.
DR SMR; P9WEX0; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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; IPR041068; HTH_51.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Transferase.
FT CHAIN 1..2159
FT /note="Non-reducing polyketide synthase dpasA"
FT /id="PRO_0000451522"
FT DOMAIN 1651..1727
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 74..180
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 397..791
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 906..1210
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1290..1554
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1571..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1956..2142
FT /note="Methyltransferase (CMeT) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 1571..1602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 534
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 992
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1687
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2159 AA; 234512 MW; 4DC716E2CA93971B CRC64;
MPAESTSMLV CGSLIASHNV GSLSHLRSSL VHDPSFAGLR QQLTELPDVW SLLVDREPSL
AAVDAAPLFH SLSSWLQGNS SSEALSLPEG APKNILYAIL TVLTHILEYA TFLDRSNPTT
AGDDDAHSRR LEDFQDGGVQ GLCIGLLSGI AIACSKSRVE LGKNAAIAVR LAICAGACVD
LAELQSAEPT VCLSARWSRH EESQTNNDCV VAATLKYYPG AYISVRSDVC SATITTNKGS
VPALIKALEE KGAVAKRINL SGRYHHSMYT PMFEKLLDIC GSQPIFQFPQ TARPLVPLRR
SDSGELVAQD ETPLHEIALR CILVETADWH KTMVKTLETM AAKAASKSAG AESLKLQKFV
LGPMDCAPKP AFAPLPIHTI RPAAVPESSY SYPDDAIAVI GLSCRFPNAE TPAKFWEMLK
SKQTSTLLGP VDSFDCGLFR KSPREAEFLD PQQRLGLHLA YEALESGGYF QPSANSTDNV
GCYVGVSSCD YEANVNSHDP TAFSYTGTAR AFVGGRISHF FGLTGPSLAV DTACSSSGVA
IHTACRAIRA GECAMALAGG INLMTEEGRA HANLGAASFL SSTGECRPFD AAANGYRRGE
GGGFVLLKRL SAAVADNDKI LGVVAASAVN NSKGNKSITL PASGSQSDLY EQVLQAAGMQ
PSQISYVEAH GTGTTKGDPI ECESIRKVLG KSQRPNAPPL IFGSVKGNFG HSEAASGVSA
FIKTILMLQR GQIPPQANFT VLNPAIPCVE EANMEVSTRM QSWETPFRAA LVNNYGASGT
NAAMVVCQPP PQRVAKQQVI EAQSTRTHKY PVIISANSPT SIRKYCESVL ELVDTKQAAL
GESIVPAIAC KLARSQNHAH AYRRVFAAGS IEELKAGLRG DGQGRSAAAI FQMPPGSVAK
KPVVLVFAGQ TGREVRLSEE AYLGCALLRR RLDACDRALQ SLGLGDLIPR IFRAEPIDDL
AYLHCMHFSV QYAVAMSWID AGLQVSALVG HSLGQLTSLC ISGVLSLRDA LKLVAGRARL
IQTKWGPESG CMLSVDADAA TVEALIQSMP GDDRVEIACY NSSVHHILAG TETAIAAFAE
IAHAKGVSFQ RLEVTHGFHS HLVNSILPEY LELIEGLTLR KAKIPIEACS SSQQCWSKVT
PQMIANQSRQ SVYWSQAIAR VEERLGPNCV WLEAGSRAVG VTMARRALAA RPATIPESNS
SFHSARLYGA DSLDHLTQTA LDLWREGVQV QSWMFHGAQA HSYAPLELPS YCFENSHLWL
PLIENSKGSD GINTAAARPV QFVSLSELSE RGSEQVAKFE INQDNEEYSL FVQGRTVFGQ
TLAPSSVWME AASRALDLLP DQSADRTPAV VHQLRLHAPF GLDYQRKLIL VLRRSNTSSP
AWEFTVESQL LKDSSNSSDL HASGTVGRPA RQTDTRQYQS LLRHLRERCQ TLRQDPDASV
VNGAFISKMM AQVADYDKSY MGIRSIACKD FEAVGEVDIP AIAVEKCATT AFIPPLFDNL
LIVGELHASS LEGLVRDNFL ERESAKDLVS DMIVFRPDQK APVLSILGAR FTQISTRSLR
RALESVNGAP AETSNEFSAP TTTRFGLPSG INSGSQAYSN PGMIESDEGV RPRLNNPIRS
HSASDLILDN CSDTSALSST TSPSSVGIAT PEDEENVRIL TNLLSDHLNC SQGIPPDTPL
VMLGLDSLVM MQLKSDIKKA FGSHMNVSKI DENCTLSDLC SMLFPNEPTT QLLSSTTITE
KKAVLSQSAS KYEENPMPLM RALGTTSHTR SAFIERAAQE FATLKQSTSA VTRETQFANF
FAEVYPDQQR LVTTYILEAF SKLGCDLRNM QAGEILPPIA YLPKYEKLMS RFYAILEAAG
IISAYNCQKL RFKTINNGGG DKASSVDLYR DILAKHPYYH PDHKLLAVTG PYLAECLSGQ
DDGLQLIFQE AESRKLLEDV YRSSPMFATG NALLGHFMTQ LLEQQATFAD AADDVLRILE
IGGGTGGTAY LMMDLLLAQP NVKFHYTFTD ISAALVASTR KQFEARYGRS CLEKHMEFTV
LDAERPPPTE RVGVYHMVVS SNCIHATRDL RQSCGLIERL LRPDGGVLCL LELTRPLPWL
DCVFGLLDGW WRFDDGRSYA LQDEGHWKKA LLESGFGRVD WSDDGTRESQ QFRLITAWR
