ELCD_PHANO
ID ELCD_PHANO Reviewed; 437 AA.
AC Q0UI04;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=O-methyltransferase elcB {ECO:0000303|PubMed:28251756};
DE EC=2.1.1.- {ECO:0000305|PubMed:28251756};
DE AltName: Full=Elsinochrome C biosynthesis cluster protein D {ECO:0000303|PubMed:28251756};
GN Name=elcD {ECO:0000303|PubMed:28251756}; ORFNames=SNOG_08610;
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: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of elsinochrome C, a perelyenequinone phytotoxin
CC structurally similar to cercosporin (PubMed:28251756, PubMed:30809363).
CC The first step of elsinochrome C biosynthesis is performed by the
CC polyketide synthase elcA which catalyzes the formation of nor-
CC 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 class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
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DR EMBL; CH445337; EAT83778.1; -; Genomic_DNA.
DR RefSeq; XP_001798919.1; XM_001798867.1.
DR AlphaFoldDB; Q0UI04; -.
DR SMR; Q0UI04; -.
DR STRING; 13684.SNOT_08610; -.
DR EnsemblFungi; SNOT_08610; SNOT_08610; SNOG_08610.
DR GeneID; 5975818; -.
DR KEGG; pno:SNOG_08610; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_1_4_1; -.
DR InParanoid; Q0UI04; -.
DR OMA; LSFEHCA; -.
DR OrthoDB; 817726at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..437
FT /note="O-methyltransferase elcB"
FT /id="PRO_0000449855"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 269
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 437 AA; 48108 MW; 91AC8091485FB6D5 CRC64;
MSLLQLTASI TKAAADLDDA TNNAAKASEI ESKAKTALLD AAERLVLAYR SPRQWLIDLS
FQHCATASLQ MIMKYRLHHA VPKQGSRSFA EIAEIITTPD QPGKLPESLV GRLLQHAMSF
GLFTPAASGR VAHNDASLLL VTDPDLEAWV YLCSNVAYPA GAQLPKAIEQ YGASSEPSET
AYSVSIGRRI SQFERFREPD GHAEHEMFAR AMKGISAGGA YDVGHVVDGG YPWHELPEGT
LVVDVGGGPG HVAIALARKY PQLLFEVQDL VETVEFGAKN CPKDLQHRVS FRAQDFFKPQ
PQRETDSRTI VYFARFILHD WSDKYAGQIV EPLAQAMRPQ DRLILNEVVV PEPSVEQRIE
RKSHDRDLLM LMNLNGRERT LVAFEGLFEV VSPRLRVEKV HKPTTGGELS LITASVDKLT
GRKSAGGDIF GANVDEA
