CTB12_CERBT
ID CTB12_CERBT Reviewed; 636 AA.
AC A0A2G5I8N8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Multicopper oxidase CTB12 {ECO:0000303|PubMed:29844193};
DE EC=1.-.-.- {ECO:0000305|PubMed:29844193};
DE AltName: Full=Cercosporin toxin biosynthesis cluster protein 12 {ECO:0000303|PubMed:29844193};
DE AltName: Full=Laccase CTB12 {ECO:0000303|PubMed:29844193};
DE Flags: Precursor;
GN Name=CTB12 {ECO:0000303|PubMed:29844193}; ORFNames=CB0940_00845;
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RC STRAIN=09-40;
RX PubMed=29844193; DOI=10.1073/pnas.1712798115;
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M. II, Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Gene cluster conservation provides insight into cercosporin biosynthesis
RT and extends production to the genus Colletotrichum.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E5459-E5466(2018).
RN [2]
RP REVIEW ON CERCOSPORIN.
RX PubMed=11701851; DOI=10.1146/annurev.phyto.38.1.461;
RA Daub M.E., Ehrenshaft M.;
RT "The photoactivated cercospora toxin cercosporin: contributions to plant
RT disease and fundamental biology.";
RL Annu. Rev. Phytopathol. 38:461-490(2000).
CC -!- FUNCTION: Multicopper oxidase; part of the gene cluster that mediates
CC the biosynthesis of cercosporin, a light-activated, non-host-selective
CC toxin (PubMed:29844193). The perylenequinone chromophore of cercosporin
CC absorbs light energy to attain an electronically-activated triplet
CC state and produces active oxygen species such as the hydroxyl radical,
CC superoxide, hydrogen peroxide or singlet oxygen upon reaction with
CC oxygen molecules (PubMed:11701851). These reactive oxygen species cause
CC damage to various cellular components including lipids, proteins and
CC nucleic acids (PubMed:11701851). The first step of cercosporin
CC biosynthesis is performed by the polyketide synthase CTB1 which
CC catalyzes the formation of nor-toralactone (Probable). The starter unit
CC acyltransferase (SAT) domain of CTB1 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. The product template (PT) domain
CC catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a
CC trihydroxynaphthalene, which is thought to be delivered to the
CC thioesterase (TE) domain for product release (Probable). The
CC bifunctional enzyme CTB3 then methylates nor-toralactone to toralactone
CC before conducting an unusual oxidative aromatic ring opening
CC (Probable). The O-methyltransferase CTB2 further methylates the nascent
CC OH-6 of the CBT3 product, blocking further oxidation at this site
CC before the reductase CTB6 reduces the 2-oxopropyl ketone at position
CC C7, giving naphthalene (Probable). The FAD-dependent monooxygenase CTB5
CC in concert with the multicopper oxidase CTB12 are responsible for
CC homodimerization of naphthalene with CTB7 installing the dioxepine
CC moiety, finally producing cercosporin (Probable). The fasciclin domain-
CC containing protein CTB11 might act with CTB5 and CTB12 whereas the
CC roles of CTB9 and CTB10 have still to be elucidated (By similarity).
CC {ECO:0000250|UniProtKB:Q0UHZ9, ECO:0000269|PubMed:29844193,
CC ECO:0000303|PubMed:11701851, ECO:0000305|PubMed:29844193}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:29844193}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of cercosporin.
CC {ECO:0000269|PubMed:29844193}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; LKMD01000100; PIB01155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5I8N8; -.
DR SMR; A0A2G5I8N8; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000230605; Chromosome 1.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Repeat; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..636
FT /note="Multicopper oxidase CTB12"
FT /id="PRO_5013929045"
FT DOMAIN 62..168
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 318..381
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 486..613
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 104
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 148
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 150
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 519
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 522
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 524
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 595
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 596
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 597
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 601
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 636 AA; 70180 MW; 3133FFD36B4F80A8 CRC64;
MWSVRLYPLA LTLLFQCVSP AAARPSGCVD DVEVVQEIGS KEIQAPVVRF EISLTTQSID
AAGIGFREAI FINDAFIGPT LYAKQGDRIE FVVHNYMQQD TSIHFHGIDQ RSTPWSDGVP
GLTQSQIRPG ASFLYNWTAH DAGTYFYHSH AKSQMMDGLY GAVVIAPDDE APRPFHLISS
GEADQAAMLA AEKLMRPIFV SDWSQYTSAE YHGIQHAANI DFSCMDSILV QGVGSQYCLS
EEELDDMTNP IVLQLLKELA GGHMTPKGCI PPLQMFNGDF ELHLENVPEL AYNKCKGGQS
SKGNYTIDVD TSIGWAALTF VNPGGLYPLQ LSIDSHELYV YAVDGQYVYP IVADRVLVNT
GSRISVMIKL DQEKARHVVR VANDYLNQIL GGFAELAYDG ATNAPKHPHP KTNYGGKLIS
SEMVSFVPED SSPYPALRPA QSADSTFKLR LKKLGQPYRA YEWTQTGSLG YNISHEHDDP
PLLLQNVEDV PATELTLKTQ IGDWVDLVLV TAGPFAQAHP MHKHGNKVFL IGSGSGSFPW
ESVEEAIPHL PEGTFNFQDP PYLDTFNTVE MEGQANDTWT AVRYKAEYAG AWLFHCHVQT
HLSGGMGMVV LDGVDAWPEV PLAYQEWNGF EPPALS
