ID   CLAG_PASFU              Reviewed;        1790 AA.
AC   P0CU67;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Atrochrysone carboxylic acid synthase {ECO:0000303|PubMed:27274078};
DE            Short=ACAS {ECO:0000250|UniProtKB:Q5BH30};
DE            EC=2.3.1.- {ECO:0000269|PubMed:27274078};
DE   AltName: Full=Cladofulvin biosynthesis cluster protein G {ECO:0000303|PubMed:27274078};
DE   AltName: Full=Non-reducing polyketide synthase claG {ECO:0000303|PubMed:27274078};
GN   Name=claG {ECO:0000303|PubMed:27274078};
GN   Synonyms=pks6 {ECO:0000303|PubMed:24465762}; ORFNames=Clafu184395;
OS   Passalora fulva (Tomato leaf mold) (Cladosporium fulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Fulvia.
OX   NCBI_TaxID=5499;
RN   [1]
RP   INDUCTION.
RX   PubMed=24521437; DOI=10.1111/mmi.12535;
RA   Okmen B., Collemare J., Griffiths S., van der Burgt A., Cox R.,
RA   de Wit P.J.;
RT   "Functional analysis of the conserved transcriptional regulator CfWor1 in
RT   Cladosporium fulvum reveals diverse roles in the virulence of plant
RT   pathogenic fungi.";
RL   Mol. Microbiol. 92:10-27(2014).
RN   [2]
RP   IDENTIFICATION, FUNCTION, DOMAIN, AND INDUCTION.
RX   PubMed=24465762; DOI=10.1371/journal.pone.0085877;
RA   Collemare J., Griffiths S., Iida Y., Karimi Jashni M., Battaglia E.,
RA   Cox R.J., de Wit P.J.;
RT   "Secondary metabolism and biotrophic lifestyle in the tomato pathogen
RT   Cladosporium fulvum.";
RL   PLoS ONE 9:E85877-E85877(2014).
RN   [3]
RP   INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=27274078; DOI=10.1073/pnas.1603528113;
RA   Griffiths S., Mesarich C.H., Saccomanno B., Vaisberg A., De Wit P.J.,
RA   Cox R., Collemare J.;
RT   "Elucidation of cladofulvin biosynthesis reveals a cytochrome P450
RT   monooxygenase required for anthraquinone dimerization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:6851-6856(2016).
RN   [4]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27997759; DOI=10.1111/mpp.12527;
RA   Griffiths S., Mesarich C.H., Overdijk E.J.R., Saccomanno B.,
RA   de Wit P.J.G.M., Collemare J.;
RT   "Down-regulation of cladofulvin biosynthesis is required for biotrophic
RT   growth of Cladosporium fulvum on tomato.";
RL   Mol. Plant Pathol. 19:369-380(2018).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of the bianthraquinone cladofulvin, a
CC       conidial pigment not required for virulence but that plays a role in
CC       fitness and resistance to environmental stresses including UV light and
CC       low-temperature stress (PubMed:24465762, PubMed:27274078,
CC       PubMed:27997759). The pathway begins with the synthesis of atrochrysone
CC       thioester by the polyketide synthase (PKS) claG. The atrochrysone
CC       carboxyl ACP thioesterase claF then breaks the thioester bond and
CC       releases the atrochrysone carboxylic acid from claG (PubMed:27274078).
CC       This compound is decarboxylated by claH to yield emodin, which is
CC       further converted to chrysophanol hydroquinone by the reductase claC
CC       and the dehydratase claB (PubMed:27274078). The cytochrome P450
CC       monooxygenase claM then catalyzes the dimerization of nataloe-emodin to
CC       cladofulvin (PubMed:27274078). {ECO:0000269|PubMed:24465762,
CC       ECO:0000269|PubMed:27274078, ECO:0000269|PubMed:27997759}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8 H(+) + holo-[ACP] + 8 malonyl-CoA = atrochrysone carboxyl-
CC         [ACP] + 8 CO2 + 8 CoA + 2 H2O; Xref=Rhea:RHEA:64232, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:149712;
CC         Evidence={ECO:0000269|PubMed:27274078};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64233;
CC         Evidence={ECO:0000269|PubMed:27274078};
CC   -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:27274078}.
CC   -!- INDUCTION: Expression is positively regulated by the transcriptional
CC       regulator wor1 (PubMed:24521437, PubMed:27274078). Exhibits high
CC       expression at the early stages of infection when runner hyphae were
CC       growing on the tomato leaf surface (PubMed:24465762). Expression drops
CC       after penetration when the fungus is colonizing the apoplastic space
CC       between mesophyll cells (PubMed:24465762, PubMed:27997759). The
CC       expression is induced at later stages of infection when conidiophores
CC       emerge from the plant and produce conidia (PubMed:24465762).
CC       {ECO:0000269|PubMed:24465762, ECO:0000269|PubMed:24521437,
CC       ECO:0000269|PubMed:27274078, ECO:0000269|PubMed:27997759}.
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. {ECO:0000305|PubMed:24465762}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of cladofulvin
CC       (PubMed:27274078). Does not affect virulence (PubMed:27997759).
CC       {ECO:0000269|PubMed:27274078, ECO:0000269|PubMed:27997759}.
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DR   AlphaFoldDB; P0CU67; -.
DR   SMR; P0CU67; -.
DR   OMA; CKTWDAT; -.
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   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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   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; IPR032821; PKS_assoc.
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; IPR009081; PP-bd_ACP.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
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; 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   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   1: Evidence at protein level;
KW   Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Transferase.
FT   CHAIN           1..1790
FT                   /note="Atrochrysone carboxylic acid synthase"
FT                   /id="PRO_0000445887"
FT   DOMAIN          1715..1789
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:24465762"
FT   REGION          27..265
FT                   /note="N-terminal acylcarrier protein transacylase domain
FT                   (SAT)"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24465762"
FT   REGION          402..836
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24465762"
FT   REGION          934..1254
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24465762"
FT   REGION          1357..1631
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24465762"
FT   REGION          1644..1667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        572
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   1790 AA;  195585 MW;  244F0580BEE1C41E CRC64;
     MTTNHLENKV HAATESLFYF SNEFPKRDLQ DLFRQAHTRS KLAQHKCLAQ FIQDATQTVK
     QEIQGLSMKL QHLFKPLESV LTWAEDHELR EGALSGAIDG VLLIVAQMTT LIGYLENNTA
     KMDDIATASL AGLGVGLLTA CAVSSASTIA DLSATGADAV RTAFRLGVHV YYVSQTLEAL
     DPSARPETWA YVINNVTPTE AQEQLDTLYA NSTQPATSKV FISALSRSSV TVSGPPARLK
     ALVTGSEFFR TSRYIALPVY GGLCHAPHVY GQDDVDMVMQ SRAFSVQKAP ATHLKSVWST
     SSGYPYLVED SKSLFASVVA ELLTKAICWD SVVSSIVKYT GLTDASEMII YNYGNSIPLN
     ELESALKSSP AKLKVVNSNL LSWMGHNSPT SVKPRNTLQS KLAIVGMSCR LPGGATSNEL
     FWDVLRRGVD TSQVIPADRF DVATHYDPAG KQLNKSMTQY GCFIDEPGLF DAPFFNMSPR
     EAQTVDPQMR LALVTAYEAL EQAGYVANRT ASTRLERIGT YYGQAADDYR EVNQGQEVST
     YYIPGGCRAF GPGRINYFFK FAGPSYSIDT ACSSGLAAVE VACQALWRGD VDTAVTGGVN
     ILTNPDGFTG LCSGHFLSKG HNACKTWDAT ADGYCRADGV GSLVIKRLED AEDDNDNILG
     VILGAGTNHS AQAVSITHPH AGHQAYLARQ VLRQAGVDPL DVSYVELHGT GTQAGDSEEM
     QGILDVYAPL SKRRSQSQPL HIGAVKANMG HSESSAGTTA LVKVLLMLQN NVIPPHIGIT
     TEMNPKFGHD FKKRNLHIPF ELTPWEHTDD KRRIAVVNNF GAAGGNTTMI LEDAPMRSIS
     QSDTRKTHVV VLSAKTKTSL VANVDRLISY IDSHPDTQIA NVSYTTTARR YQHVLRVAIS
     TSEIAHLQKQ LYSHREKIEY IQPVRKAEPP PVAFSFTGQG ASHKSMNLEL YRDVPTFREF
     VHQLDSLTRA QGFESFICAL DGSHDKDHQH SPVVTQLALV CSEIALAKYW ASIGVLPNIV
     IGHSLGEYAA MHIAGVISAS DAIFLVGRRA QLLQERCKIG SHLMMAVRAS VDQITQSAAG
     KPFTVACVNG PADTVLAGTK EEIEVIKTPL ESSGLQCIKL DVAFAFHSEQ TDPLLDDFEA
     LAKSGVIFAE PKLPVISPLL GKVIFDAKTI NATYVRRATR EAVDFLAALN NAQEIGAIGG
     DTVWVEIGPH PVCTGFVRST IPSVKLALPS FRRGEENWKT LSDSIAQLYT VGVDIDWTEL
     HRPFEKNLRL LDLPTYAFNE KTYWLQYKGD WCLTKGNTFY ADEQKIVRGQ LPSVSELHTS
     TVQQIVEQVF DTDTGSCTVV IESDMMQPDF LAAAHGHRMN DCGVATSSIH GDIAFTLAEH
     IHKKLGVHGK DTRYNVANLQ VTKALVARKN TANPQVIRVT ASTTDVRSGI DLVWQNINAN
     GDSAEPFATS SIHAGISTDW ISSWSSLTHL VRDRIETLDR LVAEGKANRL SHNMAYTLFA
     SNLVDYADKY RGMQSVVMHG LEGCADVELS TKESGVWTVP PYFIDSVAHL AGFIMNCSDA
     IDAKKFFCIT PGWKTMRFAR PLVPGARYQS YVKMIPTVED DTAYFGDVYI LQDGVIIGLV
     EGIEFHRYRR ILLERLFSAP DSTNLDDTTE TKDISSSTQH SVPVSRQVPP AAKSSAQTVF
     ESSLPFAVPG PRKSTARPAV DEIAAREKPV ASQSSSITNR AMQLIADEVG VELADLCDDV
     GFSDLGVDSL MSLVIADTFR ATLDIKVNGS LFLDYETIGD LRNWLEETYA