ELCG_PHANO
ID ELCG_PHANO Reviewed; 624 AA.
AC Q0UHZ8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Multicopper oxidase elcG {ECO:0000303|PubMed:28251756};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Elsinochrome C biosynthesis cluster protein G {ECO:0000303|PubMed:28251756};
DE AltName: Full=Laccase elcG {ECO:0000303|PubMed:28251756};
DE Flags: Precursor;
GN Name=elcG {ECO:0000303|PubMed:28251756}; ORFNames=SNOG_08616;
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: Multicopper oxidase; 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 multicopper oxidase family. {ECO:0000305}.
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DR EMBL; CH445337; EAT83784.1; -; Genomic_DNA.
DR RefSeq; XP_001798925.1; XM_001798873.1.
DR AlphaFoldDB; Q0UHZ8; -.
DR SMR; Q0UHZ8; -.
DR STRING; 13684.SNOT_08616; -.
DR EnsemblFungi; SNOT_08616; SNOT_08616; SNOG_08616.
DR GeneID; 5975824; -.
DR KEGG; pno:SNOG_08616; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_5_0_1; -.
DR InParanoid; Q0UHZ8; -.
DR OMA; WHGVREP; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..624
FT /note="Multicopper oxidase elcG"
FT /evidence="ECO:0000255"
FT /id="PRO_5004177841"
FT DOMAIN 48..160
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 216..373
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 474..603
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 98
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 140
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 142
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 511
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 514
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 516
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 585
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 586
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 587
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 591
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 624 AA; 69719 MW; 322048006EB24D14 CRC64;
MACNILNFLT GLLSLSSTLP STYFPSCIKP SNSHVSQNPV RFEVHLTPGR ANPTGAGFRD
VILVNGTFTG PTLRLSRGDN VEFLVRNHLR EDTAVHFHGI TQSLSPWADG TPGIAQRPIR
PGAAYLYRWR ADESGVFFYH AHSRGQLMDG MYGAIVIERG EDEPSPFHMI SHEASDWELM
REAEREVQTL MISDWSQFSF GEVMGVEREA NIDFTCMDAI VVNGAGSEYC LERELLNEYT
NPLVKFILSH TDEKEITDKG CVPPLRLFQG NYSLHLDTLP PEAFRKCIPG VGGGANHTVT
VHSSNRWAAL TFINPGGLYP LKVTIDNHPM HVFAVDGHYI YPQIVDQILV NNGERYSVFV
KLDQEVGRYT IRIANDLLGQ VLGGFAALSY NGVMDDPPHP KPLMNYAGGS LVKNIRVFDE
FNTRPYPPKP PASVADRTHK FMVRKLAQPH GAYEWTMSGI EGLNMTTEDV ASPFLFQDPS
QIETSELMLT TKKNEWVDLI IEVEGPFAQS HPMHKHGNKA FIVGRGVGFF PWATVEEAEK
HLPRGTFNFI DPPYKDTFKT LEGVNNNAWL ALRYHANSPG AWLFHCHIQT HLAGGMGVVI
LDGVDEWPEL PEAYAEWNGF EAPV
