ELCB_PHANO
ID ELCB_PHANO Reviewed; 931 AA.
AC Q0UI02;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Dual O-methyltransferase/FAD-dependent monooxygenase elcB {ECO:0000303|PubMed:28251756};
DE AltName: Full=Elsinochrome C biosynthesis cluster protein B {ECO:0000303|PubMed:28251756};
DE Includes:
DE RecName: Full=O-methyltransferase {ECO:0000303|PubMed:30809363};
DE EC=2.1.1.- {ECO:0000269|PubMed:30809363};
DE Includes:
DE RecName: Full=FAD-dependent monooxygenase {ECO:0000303|PubMed:30809363};
DE EC=1.-.-.- {ECO:0000269|PubMed:30809363};
GN Name=elcB {ECO:0000303|PubMed:28251756}; ORFNames=SNOG_08612;
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: Dual O-methyltransferase/FAD-dependent monooxygenase; part of
CC the gene cluster that mediates the biosynthesis of elsinochrome C, a
CC perelyenequinone phytotoxin structurally similar to cercosporin
CC (PubMed:28251756, PubMed:30809363). The first step of elsinochrome C
CC biosynthesis is performed by the polyketide synthase elcA which
CC 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 -!- CATALYTIC ACTIVITY:
CC Reaction=nor-toralactone + S-adenosyl-L-methionine = H(+) + S-adenosyl-
CC L-homocysteine + toralactone; Xref=Rhea:RHEA:62908,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:78029, ChEBI:CHEBI:146018;
CC Evidence={ECO:0000269|PubMed:30809363};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62909;
CC Evidence={ECO:0000269|PubMed:30809363};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + toralactone = 1-(3,4,5-trihydroxy-7-
CC methoxynaphthalen-2-yl)propan-2-one + CO2 + NAD(+);
CC Xref=Rhea:RHEA:62912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78029, ChEBI:CHEBI:146020;
CC Evidence={ECO:0000269|PubMed:30809363};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62913;
CC Evidence={ECO:0000269|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: In the C-terminal section; belongs to the paxM FAD-
CC dependent monooxygenase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
CC binding methyltransferase superfamily. Cation-independent O-
CC methyltransferase family. COMT subfamily. {ECO:0000305}.
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DR EMBL; CH445337; EAT83780.2; -; Genomic_DNA.
DR RefSeq; XP_001798921.1; XM_001798869.1.
DR AlphaFoldDB; Q0UI02; -.
DR SMR; Q0UI02; -.
DR STRING; 13684.SNOT_08612; -.
DR EnsemblFungi; SNOT_08612; SNOT_08612; SNOG_08612.
DR GeneID; 5975820; -.
DR KEGG; pno:SNOG_08612; -.
DR eggNOG; KOG2614; Eukaryota.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_370883_0_0_1; -.
DR InParanoid; Q0UI02; -.
DR OrthoDB; 817726at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01494; FAD_binding_3; 2.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Methyltransferase; Monooxygenase;
KW Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..931
FT /note="Dual O-methyltransferase/FAD-dependent monooxygenase
FT elcB"
FT /id="PRO_0000449857"
FT REGION 1..463
FT /note="O-methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:Q2I0M6"
FT REGION 455..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..931
FT /note="FAD-dependent monooxygenase"
FT /evidence="ECO:0000250|UniProtKB:Q2I0M6"
FT COMPBIAS 457..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 520..523
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 654
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 664..668
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 718..720
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 817..825
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 931 AA; 100892 MW; 33B78F776BF63D8F CRC64;
MAASTGLSTV LKEIVQVCRE VESHLATESH LDSGEGAPGK NTFPIGLEGP RKQLANAAAQ
LSQLVTDPRE YLEQLSANHG SIAYTDLANR ASVPESQLKS VLRMTAAHGF LAEVTPLEIS
HSPTSALIAT NPSFYDWARW LTNYSVPSAY HFADATQKWG RTEVKNETAF NIAMNVEVPF
FGYLKENAKM NSMFSSYMRN VASSEATSFK HMISGFDWGG LTPGSKVIDV GGSGGHGSRA
LASAFPGLNF VVQDLPDTIE NAKAALNTDE SKLHADRVRF MSHDFFTPQP VVDGDIYFLR
MIIHDWPDET AITILAHLRD ALKKPGARIV IMDTILPQPG TVSLLQERQL RVRDLTMMQV
FNAKEREYDT WKALVEKVGL RIIHVEQPEG SNMGLLELGL ADATDLKAGG NARLVFNGNM
KTPSVNLNIN GASTINEFAH GSTPETFAVN GIHTTDKARP NGDTTHSGQA SIPNGVSARI
STRPMYARDV LPVLIIGAGI SGLCLAQYLH KHAIPFVVFE RDPSSEHRPQ GYRLKLEADA
AAALRESLTA EVYSAFEASC AESAIGETDF DPISGACIKS RAGGGLAGAQ GLRASYTVDR
TVFRRILMTG ISDKIYFGRE ITRYDICEDN VQSYVVATFK DGATAEGRFL VGADGTRSAI
RKQLVPEHKF LDTGATCIYG KTVMTPELLA RYPARALRWM TVVADRAPLI QSILIGESPL
TLLSEPIRFS RDEPTASLPE DYVYWVLIGR RELFTDATNT SASSTGHGVN SDKAYNTESA
QASAAQSLAL TEEWHPSLRS LFELQDVSQA STMRVVSAPP KLPVWPSNSC VTLLGDAVHA
MSPCGGVGAN VALRDAAELG KVFASTAASN EEDAIQSVGG KASDQHDMAQ QIASFEGELR
KRAFGGIMRS FVGSKAMFGQ RTFEELDVAE L
