ID   PYVD_ASPV1              Reviewed;         245 AA.
AC   A0A2V5GSC6; A0A7M4B3V2;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Hydrolase pyvD {ECO:0000303|PubMed:33117309};
DE            EC=3.1.1.- {ECO:0000305|PubMed:33117309};
DE   AltName: Full=Pyranoviolin A biosynthesis cluster protein D {ECO:0000303|PubMed:33117309};
GN   Name=pyvD {ECO:0000303|PubMed:33117309}; ORFNames=BO99DRAFT_371772;
OS   Aspergillus violaceofuscus (strain CBS 115571).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=33117309; DOI=10.3389/fmicb.2020.562063;
RA   Wei X., Chen L., Tang J.W., Matsuda Y.;
RT   "Discovery of pyranoviolin A and its biosynthetic gene cluster in
RT   Aspergillus violaceofuscus.";
RL   Front. Microbiol. 11:562063-562063(2020).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115571;
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolase; part of the gene cluster that mediates the
CC       biosynthesis of pyranoviolin A, a pyranonigrin analog with a C-3
CC       methoxy group (PubMed:33117309). Initially, the PKS portion of pyvA
CC       synthesizes C-10 carbon chain from 5 molecules of malonyl-CoA, which is
CC       then condensed with the thiolation (T) domain-bound glycine activated
CC       by the adenylation (A) domain (PubMed:33117309). The subsequent chain
CC       release by Dieckmann condensation (DKC) could be catalyzed by the TE
CC       domain present at the C-terminus of pyvA and/or the alpha/beta
CC       hydrolase pyvD, installing the tetramic acid moiety (Probable). The
CC       FAD-dependent monooxygenase pyvC next epoxidizes one of the olefins of
CC       the polyketide part, and the epoxide ring-opening induces the dihydro-
CC       gamma-pyrone ring formation (Probable). The cytochrome P450
CC       monooxygeanse pyvB would be responsible for the 2 consecutive
CC       reactions, in which the dihydro-gamma-pyrone is oxidized to gamma-
CC       pyrone and C-7 is hydroxylated to yield pyranonigrin F (Probable).
CC       Finally, the O-methyltransferase pyvH methylates the C-3 hydroxy group
CC       to complete the biosynthesis (Probable). {ECO:0000269|PubMed:33117309,
CC       ECO:0000305|PubMed:33117309}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:33117309}.
CC   -!- SIMILARITY: Belongs to the dienelactone hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; BR001648; FAA01294.1; -; Genomic_DNA.
DR   EMBL; KZ825234; PYI13691.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5GSC6; -.
DR   SMR; A0A2V5GSC6; -.
DR   Proteomes; UP000249829; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   Pfam; PF01738; DLH; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..245
FT                   /note="Hydrolase pyvD"
FT                   /id="PRO_0000452819"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000250|UniProtKB:P0A114"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250|UniProtKB:P0A114"
FT   ACT_SITE        211
FT                   /evidence="ECO:0000250|UniProtKB:P0A114"
SQ   SEQUENCE   245 AA;  27280 MW;  4A6CDB4ABAAA90E4 CRC64;
     MTSLPPSQCC IGGSLHEGET QGELTKFGDI PVYVSYPPDK STHNAILFLS DIFGLALVNS
     KLIADLFAAN GYLVVMPDLF QGDPVPVDHS PSFQIMDWLQ GHLPPQTDPI VTATLREMRE
     RLGCQRIGGV GYCYGGKYVV RYLHPGQLDV GFVAHPTFIE PDELKAIEGP LSISASAQDN
     LFPPEKRHES ETILAQLDVP YQINIFSDVE HGFAVRCDLN KTRHRFAKEQ SFSQGVTWFN
     QYLKK