DPCHA_COLHI
ID DPCHA_COLHI Reviewed; 2224 AA.
AC A0A1B7YCC9; H1VL15;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Non-reducing polyketide synthase dpchA {ECO:0000303|PubMed:32286350};
DE EC=2.3.1.- {ECO:0000305|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein A {ECO:0000303|PubMed:32286350};
GN Name=dpchA {ECO:0000303|PubMed:32286350};
GN ORFNames=CH063_11355, CH63R_05473;
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063;
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063;
RA O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, PATHWAY, 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 higginsianins
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 dpchA
CC via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA
CC units and 2 methylations (Probable). The alpha-pyrone is then combined
CC with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase
CC dpchD through the action of the prenyltransferase dpchC to yield a
CC linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the
CC diterpenoid pyrone biosynthetic pathway involve the decalin core
CC formation, which is initiated by the epoxidation of the C10-C11 olefin
CC by the FAD-dependent oxidoreductase dpchE, and is followed by a
CC cyclization cascade catalyzed by the terpene cyclase dpchB (Probable).
CC The short chain dehydrogenase/reductase dpchG then oxidizes the 8S
CC hydroxy group to a ketone and the short chain dehydrogenase/reductase
CC dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin
CC B (PubMed:32286350). Finally, the FAD-dependent oxidoreductase dpchF
CC converts higginsianin B into higginsianin A (PubMed:32286350).
CC {ECO:0000269|PubMed:32286350, ECO:0000305|PubMed:32286350}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|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 higginsianin A shows anti-HIV activity.
CC {ECO:0000269|PubMed:32286350}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCF40918.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CACQ02004382; CCF40918.1; ALT_SEQ; Genomic_DNA.
DR EMBL; LTAN01000004; OBR09781.1; -; Genomic_DNA.
DR RefSeq; XP_018158298.1; XM_018300448.1.
DR AlphaFoldDB; A0A1B7YCC9; -.
DR SMR; A0A1B7YCC9; -.
DR EnsemblFungi; CCF40918; CCF40918; CH063_11355.
DR GeneID; 28864555; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_005712_0_0_1; -.
DR OrthoDB; 93381at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR Proteomes; UP000092177; Chromosome 4.
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; 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; 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; Reference proteome; Transferase.
FT CHAIN 1..2224
FT /note="Non-reducing polyketide synthase dpchA"
FT /id="PRO_0000451523"
FT DOMAIN 1713..1789
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 74..183
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 429..825
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 941..1245
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1327..1620
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1635..1664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2022..2207
FT /note="Methyltransferase (CMeT) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 567
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1027
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1749
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2224 AA; 240092 MW; 24ACD0E52A7883C3 CRC64;
MSAETPSLLV CGPLISDPDA THLARIRSAL VHTPQLAELR QAVTELPGVW SLLAGGEPSL
ERVHAAPLLQ AFAEWINKGN SSGLLAAGQS SRNTRLAVLT VLSHLAEYVT FLRGLDAGAE
EDLAGELDEH TKTLGGLRDG GVQGLCVGML SASALACARN TSEVAELGAV AVRLAMCSAA
FVDLDQIQSS DPTVCVSARL PRNAGEGDEQ DRQPFQEALE SYPEVRIQHS QSSQSWVQKE
KAWLTCALRR QAYIGVRMDV AGTTITATKS ITGPLTRHLE GQGAMTKEID LKGRFHYPGH
EDALQKLVRL CESTPMLQFP QNRYPLVPLR QTITGDVVTD ETPLHETVLR CILTETADWH
TTMTRAVSAL AGSPETKSSP AGNRTRLLVQ LGIAECIPRS VLAGIPSIRV LQPTTGKPAR
PGHYPDDAIA VIGMSCRFPD AETPEHFWEI IQSGAKAGSV FPDVGSFDCG LFRKSPREAE
YMDPQHRLAL HLAYEALEAA GHFSPSSSST DDVGCYVGMS SCDYEDHVNA RPPTAFSFTG
TARAFASGRI SHFFGLTGPS VVVDTACSSS GVAIHTACRA VLSGECAVAL AGGVNLMTDE
GQAHQNLAGA SFLSPTGQCR PFDAAADGYR RGQGGGFVLL KRLSAAVADN DRVLGVIAAS
AVNNSKGNRS ITLPSSESQS RLYRQVLGSA NVHPSHVSYV EAHGTGTQKG DPVECQSIRS
VFGGSSRAGS SSPIRLGSVK GNLGHGEAAS GIASLVKVLL MLQHGVITPQ ANFSMLNPAI
PPLEGDNMEI VVSPASWRGP FRTALVNNYG ASGANAAMVV CQAPSTHLSQ IASTRTAAMT
TTHRYPFVIT ANTASSLHRS CLALLRFIET LPAGLNNDSL PSLAFHLAQR QNHALVHRIV
FSARSVAELK AHLLAQVEGG NIPSDTSSQA QKTGTKPVVL LFSGQTGRRA HLNRDAYTSF
HLLRHHLDRC DRTLQTLGLR SLFPRIFDAD PLEDLVDLHC MQFALQYSVA ASWTDSGLEI
KALVGHSLGQ LTALCVSGAL SLADSLRMVS GRALLIQTAW KQERGCMLSV DADAATVETL
AQSVSAEDKV EIACYNAALH QVVAGTEAAV AAFENAAGSS GISTKRLAVT HAFHSKLLDD
ILPEYHRLLR SLEFRPAKIP IEPCSEFGGG WDSVTPDIVG RQSREPVYFA AAMARVEQRL
GSCVWLEVGS GSAAITMARR ALESQKPSSQ AMVSHSFYAA QLHSPEPVSS VADSTVGLWN
EGVRVQFWLY HASQRQSFVP MDLPSYQFDK TQYWLPFIER NKGSDSNDQS ASSQAAPDLV
TLVGSLGSAE PQAYEFSINQ ESDEYALFVK GRTVFGHFLA PGSVYAESAA RAFALLPTDN
TPQPPASVEL GQMKLHAPFG LDLQRRLRLV LRQQTASSWE FVVESCPLHD DKEISPKPQA
SGTVRLQGQG RSPFGTSQSI LRRLFDRCGE LREDRGASVV QGAYVKKIMS RVASYDDRYF
GIRFVASRGL EAVGDVDALP IVSECRAGTA LSPPVFDNFL LVAEMHAGSL GDLADDHLYI
CGGFEAIVPG DQTSQTDGPW TVLSTLEREN DKTLVSDILV FHAGSKKLAL SILGARLTQI
PARSLQKTLD DMNAARPAKV SNSEDVLTPP LPAVESPPTD LSNGQIHCDL RSALSPLIRS
TTSLSQLTSS DDTKDSLGLS SRPSITPASS ATSENDQDTT ALYNLLAEHL DCSNGIPPDM
PLGNIGLDSL ISIQLQSDLE KLFGKSPALK LIDENTTFLE LCGMVLQQDL SSQLKSRLSP
VDSANARTTL NEPLQAYGGY GHAMSVVAPA PVSPQDTPPF LPLAVEAFKR VKKDTGAFAQ
KTGFAGFYPD VQQKQTSLVL SYILEAFATL GCDLGTLQLK DRLPGIPHPA KYQRLMGRLH
DILEEAGIIS PPDAQLFRYR TDAPLPPPTP SEDLYRQILD ECPLYRPDHQ LLGVTASRLA
DCISGRADPL QLLFQDQASL KLLEDVYVSS PMFSTGNSML GEMLRGLFSQ ARFQREGGSE
KLRILEIGAG TGATTRRVLD QLIQSGVDFS YTFTDISLAL VNGSKRKFTA SYGRQRVDSD
MEFTVLDIER PPPASMLQAF HLVISSNCIH ATRDLRTSCG NIEKLVRRGD GMLCLLELTR
PLAWLDCVFG LLDGWWRFED GRKYALAHED EWRARLESAG FQNVDWTGDG SRESEHFRLI
TAWH
