ID   ELCX_PHANO              Reviewed;          81 AA.
AC   Q0UI01;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Elsinochrome C biosynthesis cluster protein SNOG_08613 {ECO:0000303|PubMed:28251756};
GN   ORFNames=SNOG_08613;
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, AND FUNCTION.
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.
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: Part of the gene cluster that mediates the biosynthesis of
CC       elsinochrome C, a perelyenequinone phytotoxin structurally similar to
CC       cercosporin (PubMed:28251756, PubMed:30809363). The first step of
CC       elsinochrome C biosynthesis is performed by the polyketide synthase
CC       elcA which catalyzes the formation of nor-toralactone (PubMed:28251756,
CC       PubMed:30809363). The starter unit acyltransferase (SAT) domain of elcA
CC       initiates polyketide extension by the selective utilization of acetyl-
CC       CoA, which is elongated to the heptaketide in the beta-ketoacyl
CC       synthase (KS) domain by successive condensations with six malonyl units
CC       introduced by the malonyl acyltransferase (MAT) domain (By similarity).
CC       The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol
CC       cyclizations and dehydrations to a trihydroxynaphthalene, which is
CC       thought to be delivered to the thioesterase (TE) domain for product
CC       release (By similarity). The bifunctional enzyme elcB then methylates
CC       nor-toralactone to toralactone before conducting an unusual oxidative
CC       aromatic ring opening (PubMed:28251756, PubMed:30809363). The next step
CC       in perylenequinone biosynthesis is an O-methylation at the nascent OH-6
CC       of the elcB product performed by the O-methyltransferase elcD
CC       (PubMed:30809363). The oxidative coupling of the two monomeric naphthol
CC       units in 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   -!- 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}.
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DR   EMBL; CH445337; EAT83781.1; -; Genomic_DNA.
DR   RefSeq; XP_001798922.1; XM_001798870.1.
DR   AlphaFoldDB; Q0UI01; -.
DR   EnsemblFungi; SNOT_08613; SNOT_08613; SNOG_08613.
DR   GeneID; 5975821; -.
DR   KEGG; pno:SNOG_08613; -.
DR   HOGENOM; CLU_2574642_0_0_1; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
PE   2: Evidence at transcript level;
KW   Reference proteome.
FT   CHAIN           1..81
FT                   /note="Elsinochrome C biosynthesis cluster protein
FT                   SNOG_08613"
FT                   /id="PRO_0000449877"
SQ   SEQUENCE   81 AA;  9452 MW;  201E0D7240A8E805 CRC64;
     MALMIEKLAP PSKRSMTKFT QHCTGNCGQF WPKTWFWSRS SFIHWRLVSR HWPLAPFQLP
     KTTMAYALVN TKLSALRDIG N