VDTB1_BYSSP
ID VDTB1_BYSSP Reviewed; 685 AA.
AC A0A443HK79;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Multicopper oxidase VdtB {ECO:0000303|PubMed:31304040};
DE EC=1.-.-.- {ECO:0000269|PubMed:31045362};
DE AltName: Full=Laccase vdtA {ECO:0000303|PubMed:31304040};
DE AltName: Full=Viriditoxin biosynthesis cluster protein B {ECO:0000303|PubMed:31304040};
DE Flags: Precursor;
GN Name=VdtB {ECO:0000303|PubMed:31304040}; ORFNames=C8Q69DRAFT_480050;
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075;
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Maekelae M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
RN [2]
RP IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=31304040; DOI=10.1186/s40694-019-0072-y;
RA Urquhart A.S., Hu J., Chooi Y.H., Idnurm A.;
RT "The fungal gene cluster for biosynthesis of the antibacterial agent
RT viriditoxin.";
RL Fungal Biol. Biotechnol. 6:2-2(2019).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=31045362; DOI=10.1021/jacs.9b03354;
RA Hu J., Li H., Chooi Y.H.;
RT "Fungal dirigent protein controls the stereoselectivity of multicopper
RT oxidase-catalyzed phenol coupling in viriditoxin biosynthesis.";
RL J. Am. Chem. Soc. 141:8068-8072(2019).
CC -!- FUNCTION: Multicopper oxidase; part of the gene cluster that mediates
CC the biosynthesis of viriditoxin, one of the 'classical' secondary
CC metabolites produced by fungi and that has antibacterial activity
CC (PubMed:31304040, PubMed:31045362). The first step is performed by the
CC polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-
CC CoA units to form the heptaketide monomer backbone of viriditoxin
CC (PubMed:31304040). The product of VdtA is then O-methylated on C7 by
CC the O-methyltransferase VdtC (PubMed:31304040, PubMed:31045362). The O-
CC methyl group is important for the stereoselective coupling of the
CC monomers at the final step of viriditoxin biosynthesis
CC (PubMed:31304040, PubMed:31045362). The short-chain
CC dehydrogenase/reductase VdtF then acts as a stereospecific reductase
CC converting the pyrone to dihydropyrone via the reduction of the C3-C4
CC double bond (PubMed:31304040, PubMed:31045362). The FAD-binding
CC monooxygenase VdtE then converts the ketone group into a methyl-ester
CC group to yield semi-viriditoxin (PubMed:31304040, PubMed:31045362).
CC Finally, the laccase VdtB is involved in dimerization of 2 semi-
CC viriditoxin molecules to yield the final viriditoxin (PubMed:31304040,
CC PubMed:31045362). VdtB is responsible for the regioselective 6,6'-
CC coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-
CC viriditoxin at a ratio of 1:2 (PubMed:31304040, PubMed:31045362). The
CC non-catalytic carboxylesterase-like protein VdtD affects the
CC stereochemistical outcome of the coupling (PubMed:31304040,
CC PubMed:31045362). The highly reducing polyketide synthase VdtX is not
CC involved in viriditoxin synthesis, but might possibly play a role in
CC the production of additional metabolites not identified yet
CC (PubMed:31304040, PubMed:31045362). {ECO:0000269|PubMed:31045362,
CC ECO:0000269|PubMed:31304040}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 4 semiviriditoxin = 2 (M)-viriditoxin + 2 H2O;
CC Xref=Rhea:RHEA:62884, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:146007, ChEBI:CHEBI:146008;
CC Evidence={ECO:0000269|PubMed:31045362};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62885;
CC Evidence={ECO:0000269|PubMed:31045362};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31045362, ECO:0000269|PubMed:31304040}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impairs the dimerization of 2 semi-viriditoxin
CC molecules to yield the final viriditoxin.
CC {ECO:0000269|PubMed:31304040}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; RCNU01000014; RWQ92167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443HK79; -.
DR SMR; A0A443HK79; -.
DR Proteomes; UP000283841; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Glycoprotein; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..685
FT /note="Multicopper oxidase VdtB"
FT /id="PRO_5019211757"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 26..139
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 168..368
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 466..585
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 77
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 500
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 685 AA; 78142 MW; B1B3630A337411EC CRC64;
MPAYLLLLAC NVLLVLGAHV QRELVLTWEE GAPNGQSRQM IKTNGQFPSP TLIFDEGDDV
EIVVRNYMHE NTTIHWHGIL MQDTPWSDGV PGLSQKPIEP GESYVYRFTA YPPGQYWYHS
HSRATLLDGL YGALFIRRKP GTAGPWAMIS EDPEDIAAME RASNNPHIMM LSDWDYYNST
QYKEADANSR LQIFCVDSIL LNGKGSVYCP GHQWLIDKQI PFMHKSWPND TITDKGCFPF
VPSTEGPWLA DGNVSAIPPG LQEGCVPYSG PTEAIEVDPA DRWASVNWIG GSTFKTLQPT
IDEHEMWIYE VDGHYIEPRR ADTFLIWAGE RYSAMIRLDK KPMDYSIRVP DGGYSQMIAA
FGILRYKNGD PNARQKPDRF GVTTISKPYF DYNAWPMRDA VFLDKLDLPP WPRKVPAAHG
DDMHVLYLGK ANSTWEFTLS GKKKYPPDRS AYEPLLYNVN SEQAHDDDLI IRTQNGTWQD
IVLQVGHSPL WPVDFPHAVH KHANKYWRIG GGQGLWNYSS VEEAMADQPE SFNMVNPPYR
DTFLTEFTGA MWVVLRYQVT SPGAWLLHCH FEMHLDNGMA MAILDGVDKW PHVPPEYTQG
FHGFREHELP GPAGFWGLVS KILRPESLVW AGGAAVVLLS LFIGGLWRLW QRRMQGTYYV
LSQEDERDRF SMDKEAWKSE ETKRM
