ELCA_PHANO
ID ELCA_PHANO Reviewed; 1906 AA.
AC Q0UI00;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Non-reducing polyketide synthase elcA {ECO:0000303|PubMed:28251756};
DE EC=2.3.1.- {ECO:0000269|PubMed:28251756};
DE AltName: Full=Elsinochrome C biosynthesis cluster protein A {ECO:0000303|PubMed:28251756};
DE Flags: Fragment;
GN Name=elcA {ECO:0000303|PubMed:28251756}; ORFNames=SNOG_08614;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
RN [2]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=28251756; DOI=10.1111/1462-2920.13711;
RA Chooi Y.H., Zhang G., Hu J., Muria-Gonzalez M.J., Tran P.N., Pettitt A.,
RA Maier A.G., Barrow R.A., Solomon P.S.;
RT "Functional genomics-guided discovery of a light-activated phytotoxin in
RT the wheat pathogen Parastagonospora nodorum via pathway activation.";
RL Environ. Microbiol. 19:1975-1986(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=30809363; DOI=10.1039/c8sc02870b;
RA Hu J., Sarrami F., Li H., Zhang G., Stubbs K.A., Lacey E., Stewart S.G.,
RA Karton A., Piggott A.M., Chooi Y.H.;
RT "Heterologous biosynthesis of elsinochrome A sheds light on the formation
RT of the photosensitive perylenequinone system.";
RL Chem. Sci. 10:1457-1465(2019).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of elsinochrome C, a perelyenequinone
CC phytotoxin structurally similar to cercosporin (PubMed:28251756,
CC PubMed:30809363). The first step of elsinochrome C biosynthesis is
CC performed by the polyketide synthase elcA which catalyzes the formation
CC of nor-toralactone (PubMed:28251756, PubMed:30809363). The starter unit
CC acyltransferase (SAT) domain of elcA initiates polyketide extension by
CC the selective utilization of acetyl-CoA, which is elongated to the
CC heptaketide in the beta-ketoacyl synthase (KS) domain by successive
CC condensations with six malonyl units introduced by the malonyl
CC acyltransferase (MAT) domain (By similarity). The product template (PT)
CC domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations
CC to a trihydroxynaphthalene, which is thought to be delivered to the
CC thioesterase (TE) domain for product release (By similarity). The
CC bifunctional enzyme elcB then methylates nor-toralactone to toralactone
CC before conducting an unusual oxidative aromatic ring opening
CC (PubMed:28251756, PubMed:30809363). The next step in perylenequinone
CC biosynthesis is an O-methylation at the nascent OH-6 of the elcB
CC product performed by the O-methyltransferase elcD (PubMed:30809363).
CC The oxidative coupling of the two monomeric naphthol units in
CC perylenequinone biosynthesis is catalyzed by the FAD-dependent
CC monooxygenase elcE and the multicopper oxidase elcG (PubMed:30809363).
CC ElcG might catalyze the first intermolecular coupling in a regio- and
CC stereo-selective manner via a phenol radical coupling mechanism and the
CC elcE could forge the second C-C bond intramolecularly via a hydride
CC transfer mechanism (PubMed:30809363). The fasciclin domain-containing
CC protein elcF might also play a role duting this step (Probable). The
CC last piece of the puzzle in the biosynthesis of elsinochrome C is the
CC additional annulation by enolate coupling to afford the
CC dihydrobenzo(ghi)perylenequinone system, catalyzed by the FAD-dependent
CC monooxygenase elcH (PubMed:30809363). {ECO:0000250|UniProtKB:Q6DQW3,
CC ECO:0000269|PubMed:28251756, ECO:0000269|PubMed:30809363,
CC ECO:0000305|PubMed:30809363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + 2 H2O +
CC nor-toralactone; Xref=Rhea:RHEA:62892, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:146018;
CC Evidence={ECO:0000269|PubMed:28251756};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62893;
CC Evidence={ECO:0000269|PubMed:28251756};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:28251756, ECO:0000269|PubMed:30809363}.
CC -!- INDUCTION: Expression is up-regulated during the late stage of
CC P.nodorum wheat leaf infection and is controlled by the cluster
CC specific transporter elcR. {ECO:0000269|PubMed:28251756}.
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; 2 acyl-carrier protein (ACP) domains that
CC serve as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm; and a C-terminal thioesterase (TE) domain that
CC facilitates the release of the final product from the enzyme.
CC {ECO:0000305|PubMed:28251756}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of elsinochrome C.
CC {ECO:0000269|PubMed:28251756}.
CC -!- CAUTION: The sequence probably misses the N-terminal part since the N-
CC terminal acylcarrier protein transacylase domain (SAT) is absent. The
CC correct gene model with the complete protein sequence could not be
CC recovered from the submitted genomic sequence. {ECO:0000305}.
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DR EMBL; CH445337; EAT83782.2; -; Genomic_DNA.
DR RefSeq; XP_001798923.1; XM_001798871.1.
DR AlphaFoldDB; Q0UI00; -.
DR SMR; Q0UI00; -.
DR STRING; 13684.SNOT_08614; -.
DR EnsemblFungi; SNOT_08614; SNOT_08614; SNOG_08614.
DR GeneID; 5975822; -.
DR KEGG; pno:SNOG_08614; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR InParanoid; Q0UI00; -.
DR OrthoDB; 68112at2759; -.
DR PHI-base; PHI:7000; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 2.
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; 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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
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; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Virulence.
FT CHAIN <1..1906
FT /note="Non-reducing polyketide synthase elcA"
FT /id="PRO_0000449849"
FT DOMAIN 1441..1518
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1552..1630
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 137..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..605
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 706..1006
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1081..1397
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1695..1893
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255"
FT MOD_RES 1478
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1589
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT NON_TER 1
SQ SEQUENCE 1906 AA; 205334 MW; 7BFF37CA378ED43B CRC64;
MKHVSAPPPV LDELLKTTAL SKAIKFDLPI TAPYHAPHLY TAENVNTILC GVDDVVATTI
IPIVSSSTGT VVTSATFRDA LRVAVEACLQ LMIRSDLIAP GIASHVQHAD GFAIRHIATA
PDGLALAVQT ALSQAGGRSQ SGRVNAPDQN DTTSIPNALS TPRAKAKIAI LSMSGRFPQA
PSMEAFWHVL ENGIDTHELA LASRWNTRTH VGDLSLKELP KNTSGTGFGC WLHDAAQFDA
RYFNMSPREA PQVDPAQRLA LLTATEALEQ AGIVPGRTSS TQKDRVGVYF GSTSNDWMET
NSAQNIDTYF IPGGNRAFIP GRINYHFKFS GPSYTIDTAC SSSFTALHLA CNALWKGEVD
TAIVGGTNVL TNPDMTVGLD RGHFLSRTGN CSTFDDGADG YCRGEAVATL VLKRLDDAVA
DKDPVQACIL AIATNHSAEA ASITRPHVGA QQDLFASVLA DAGVKHTDIS YCEMHGTGTQ
AGDAGETTSV LQSLAPIEPP NAVRKQHQPL YIGAAKSNVG HGEAAAGVTS LAKVLLMLKK
STIPPHCGIK TKINHKLPDL PSRNTAIAME AVSWPRPVNG KRQVLLNNFS AAGGNTALIL
EDAPEVPTLD VPDIRQCHLV AVSAKTPASL ENNVKNMLAW LDEKSDASNL TLARLSYTST
ARRIHHPHRV MINATSLDSV KASLRTALDL KKGSSRPKGT PRFVFAFTGQ GAQYAGMGAD
LFAQFTGFRA DISRYDQICR QLNFPPVRQL FEDPTTFCDA TPTTLQLAMV CFQMALYRMW
VTLGVTPSAV VGHSLGEYAA LYAASVLTQA DVINIVGSRA QLLEKHCEQG SHTMLAVRSN
AEDLEAALGP SGLTYELSCH NGRESVVLGG TKSQIETIRP TLQRSRMSNR VLEVPYAYHT
SQVEPILASL AAVARGVHFA KPAIPVISPA FGTVLTQSED FGSDFIVKHC RNKVNMLGAL
QAARQMSLLD EKMMGIELGP EPVVIKMVKE VAGPAFQTFA SSRKDEPALN ILASALSAFY
TAGTDVKWTA YHADFPSAQV VLELPAYAWD LKEYWIQYVN DWSLRKGDAP LVIERTTLEG
TCIHKVVSNS LGVSGGELLV EADLSREDLH PMVQGHKVYG VPLCTPSVYA DIALTIGEYA
KQFSGEGSTK LGVEIANMNI QSALVATSDG KPQMLRTHAS YDAKQKSLYC TFSTLDDAGK
VKEQHSNCLI KLFDVEAART ALKSSAPAIK SRISILQLQL NEFGNTFRYS KAMIYKMVGQ
LADFDPKYRA LEEITLDSDA LEALGRVNFT KVSAEGKFHT NPAYIDALSQ LGGFVMNGNE
GVDLDKELFV NHGWASLKLL EAIDPTKTYT THVKMTEGTD KLWTGDITIL DGEAVVGVFG
GVALQGVPKR LMSYIVHAAS KRTNGVAPRT AGEPQTQRVT APEVVSAVVK TTTKQLVTQA
PVEDRSITTA ISIISQESGV EAADLTDDTS FDDIGVDSLL GIMVSSRIRD ELGIDVDSAA
FLEVRTVGSF KTFLRGLTGT TEQFTTVTKT VTKEITPTEL RESSFAQSAV AGDSFGVWTN
VLAILAEESG IDVSDLTGDT YFSDIGVDSL LSLVVVSRLR DEFDLDLPEQ SLFIDYPTVA
SLKARITGCT RSPSVFSDSD ATTDVPSVFS PSLEVETTSE DFQPLAFSKK EALVAVAEVA
LTPLEKADPF MSIGLASYVE SLQRHQPHGP YHLAGWSAGG VLAYAVAQEL MATGEEIATL
TLIDSPPPTD GLDRLPRRFF DHCSAVGIFG GEMSAINPSN KRAKLPEWLM PHFEATIELL
HDYCAPPMPL TTNAPKKINL IWAGGCAFGG KYAPLPPASM VGEDTEGMKF LTEQRTDFGP
DKWTDLFPGR HIDIDVVEGE HHFSMMRGKG AQQLGGFLRK TLGLLA
