ELCH_PHANO
ID ELCH_PHANO Reviewed; 485 AA.
AC Q0UI13;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=FAD-dependent monooxygenase elcH {ECO:0000303|PubMed:30809363};
DE EC=1.-.-.- {ECO:0000269|PubMed:30809363};
DE AltName: Full=Elsinochrome C biosynthesis cluster protein H {ECO:0000303|PubMed:30809363};
DE Flags: Precursor;
GN Name=elcH {ECO:0000303|PubMed:30809363}; ORFNames=SNOG_08601;
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 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, 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30809363}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; CH445337; EAT83769.2; -; Genomic_DNA.
DR RefSeq; XP_001798910.1; XM_001798858.1.
DR AlphaFoldDB; Q0UI13; -.
DR SMR; Q0UI13; -.
DR STRING; 13684.SNOT_08601; -.
DR EnsemblFungi; SNOT_08601; SNOT_08601; SNOG_08601.
DR GeneID; 5975809; -.
DR KEGG; pno:SNOG_08601; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_6_5_1; -.
DR InParanoid; Q0UI13; -.
DR OrthoDB; 521070at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..485
FT /note="FAD-dependent monooxygenase elcH"
FT /id="PRO_5004177843"
FT BINDING 59..60
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 261..263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 348..352
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT SITE 249
FT /note="Involved in substrate activation for the transfer of
FT oxygen from the flavin hydroperoxide"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 485 AA; 53569 MW; C00DFA8633AFCFA9 CRC64;
MFTLRSLAIL AVFAATALAS KQSSNDRELV VAIYGGGLAS ATLAQALKGS SNLNVQYFDP
ALDLTPTSFR LFGFDPKVHD ALALVNEEAG GAIERSGWYP EEPSVVVVGQ GSDADTVVLD
WAQLKNTTHH PQVTVVDPKP FLQQMLNGTD ESRLHPNKTL VSITRKDLSA KYPLELKFQD
GSIQHADVLI GDDGPFGQMR SEVLGAKHPA NAPVFMNFLS AVAHVAPDDA EKLLGQKYGN
RDLGRRFERV GMGSWFLNAY LEGFSTCLGS FYTEEAYDLS QFTRTTSVKE LTARFSNLNE
ADNSQKILSG YSGLRLIPEI EHSPAPTYIN GLVAMQGNAA HFMTNFQQLG PSQQIEDAMI
LGTLLRSAHS RADVEAALYA YDTVRRPRSQ WVSEHGKRLG WLWTGMVEDV GIDAKKLKKA
MLQWKQDSEA FDLKAHKNEA VKIMKQTIKE RSGSEKIITQ EEKIKAGFQG LWEAMREKSG
EQVEL
