VDTD1_BYSSP
ID VDTD1_BYSSP Reviewed; 583 AA.
AC A0A443HK52;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Inactive carboxylesterase-like protein VdtD {ECO:0000303|PubMed:31304040};
DE AltName: Full=Viriditoxin biosynthesis cluster protein D {ECO:0000303|PubMed:31304040};
DE Flags: Precursor;
GN Name=VdtD {ECO:0000303|PubMed:31304040}; ORFNames=C8Q69DRAFT_510289;
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, 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: Inactive carboxylesterase-like protein; part of the gene
CC cluster that mediates the biosynthesis of viriditoxin, one of the
CC 'classical' secondary metabolites produced by fungi and that has
CC antibacterial activity (PubMed:31304040, PubMed:31045362). The first
CC step is performed by the polyketide synthase VdtA which condenses one
CC acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer
CC backbone of viriditoxin (PubMed:31304040). The product of VdtA is then
CC O-methylated on C7 by the O-methyltransferase VdtC (PubMed:31304040,
CC PubMed:31045362). The O-methyl group is important for the
CC stereoselective coupling of the monomers at the final step of
CC viriditoxin biosynthesis (PubMed:31304040, PubMed:31045362). The short-
CC chain dehydrogenase/reductase VdtF then acts as a stereospecific
CC reductase converting the pyrone to dihydropyrone via the reduction of
CC the C3-C4 double bond (PubMed:31304040, PubMed:31045362). The FAD-
CC binding monooxygenase VdtE then converts the ketone group into a
CC methyl-ester group to yield semi-viriditoxin (PubMed:31304040,
CC PubMed:31045362). Finally, the laccase VdtB is involved in dimerization
CC of 2 semi-viriditoxin molecules to yield the final viriditoxin
CC (PubMed:31304040, PubMed:31045362). VdtB is responsible for the
CC regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-
CC viriditoxin and (P)-viriditoxin at a ratio of 1:2 (PubMed:31304040,
CC PubMed:31045362). The non-catalytic carboxylesterase-like protein VdtD
CC affects the 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31045362, ECO:0000269|PubMed:31304040}.
CC -!- DISRUPTION PHENOTYPE: Alters the ratio of the 2 atropisomers of
CC viriditoxin by favoring the production of the P form instead of the M
CC form. {ECO:0000269|PubMed:31304040}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved active serine at position 228 and does not
CC have carboxylesterase activity. {ECO:0000305|PubMed:31304040}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RCNU01000014; RWQ92169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443HK52; -.
DR SMR; A0A443HK52; -.
DR ESTHER; byssn-VdtD; Fungal_carboxylesterase_lipase.
DR Proteomes; UP000283841; Unassembled WGS sequence.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..583
FT /note="Inactive carboxylesterase-like protein VdtD"
FT /id="PRO_0000448344"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 583 AA; 63962 MW; 851760FC8C70BABF CRC64;
MFMTQIVFGI APTLLKTFSH LTALDLWRPS APYVFDPVTS STYLGTIADG VEEFLGIFYG
QDTGGSNRFA PPKPYIPSRH SFINASTAGA ACPQPYVPLP ADPYTVLTNV SEDCLSLRIA
RPENTKSTAK LPVMVWLYGG GASVGTAYDV SYNPVGLIQQ SVVNGSPVIY VAINYRVNLF
GHAFSDALLK SKSTNLAMQD QRLGIEWIKN HISAFGGDPD NITLFGEDEG ATYIALHILS
NHEVPFHRAI LQSGAAITHH DVNGNRSARN FAAVAARCNC LSDGDRQVDS QDTVDCLRRV
PMEDLVNATF EVAHSVDPVN GFRAFMPAVD GYMIPDEPSN LLSRGQVPAN ISILAGWTRD
ESSMSVPTSI RTAADAASFI STQFPLLNAS TIHHFLTSLY PESDFTTNSP SSPEKVTPAW
RATSALHRDL TLTCPTIFQA WSLRLSSNCT TPVYLYELRQ SPFATALNNS GVGYLGIVHF
SDVPYVFNEL ERTYYITDPE ENKLAQRMSA SWTAFASGAF PLCERSERSL GRWEEAYGGD
RVCRDRMPEH VRVKGIGDNG DQDDGDEIGK LMARCGFINR LEY
