ELCE_PHANO
ID ELCE_PHANO Reviewed; 332 AA.
AC Q0UI06;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 3.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=FAD-dependent monooxygenase elcE {ECO:0000303|PubMed:28251756};
DE EC=1.-.-.- {ECO:0000305|PubMed:28251756};
DE AltName: Full=Elsinochrome C biosynthesis cluster protein E {ECO:0000303|PubMed:28251756};
DE Flags: Fragment;
GN Name=elcE {ECO:0000303|PubMed:28251756}; ORFNames=SNOG_08608;
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, 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: FAD-dependent monooxygenase; part of the gene cluster that
CC 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 -!- 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 -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC -!- CAUTION: The sequence probably misses the N-terminus part since the N-
CC terminal FAD-binding PCMH-type is absent. The correct gene model with
CC the complete protein sequence could not be recovered from the submitted
CC genomic sequence. {ECO:0000305}.
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DR EMBL; CH445337; EAT83776.2; -; Genomic_DNA.
DR RefSeq; XP_001798917.1; XM_001798865.1.
DR AlphaFoldDB; Q0UI06; -.
DR SMR; Q0UI06; -.
DR STRING; 321614.Q0UI06; -.
DR GeneID; 5975816; -.
DR KEGG; pno:SNOG_08608; -.
DR InParanoid; Q0UI06; -.
DR OrthoDB; 733611at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR SUPFAM; SSF56176; SSF56176; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN <1..332
FT /note="FAD-dependent monooxygenase elcE"
FT /id="PRO_0000449870"
FT NON_TER 1
SQ SEQUENCE 332 AA; 37705 MW; 80C8FFB7C4A7991B CRC64;
GVSYFSPRFG FTCNMVENFE VVLANGDIVN ANATSHRKLW KALRGGSNNF GIVTAITLRV
FSQGKFWGGQ TFHPISTRKD HFHALENLIA AVPYDKYAHF INTIVITNAS YGNWFIGNSL
QYTKSDPPTP FPETFKPFTD IPRVALFPGA PDNTLRVDNH TAFTLEYAAL NVYPKRWQFA
TISFGNSAEM MEDFFQMANE TIQPFLTLPG FLLSVAYQPL PTLMSERYGE VDSLGPIQTQ
GNMFYIHWAM SVDGSEVETD RKFEKVTRDL FQRAEAKARE KGLRRDFLQL TSNGTLKELW
RVSKEYDPTG MFQKQVPGGF KLSEMDEDSM EL
