PYVF_ASPV1
ID PYVF_ASPV1 Reviewed; 629 AA.
AC A0A2V5GRB0; A0A7M4B5C5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Dehydrogenase pyvF {ECO:0000303|PubMed:33117309};
DE EC=1.1.-.- {ECO:0000305|PubMed:33117309};
DE AltName: Full=Pyranoviolin A biosynthesis cluster protein F {ECO:0000303|PubMed:33117309};
DE Flags: Precursor;
GN Name=pyvF {ECO:0000303|PubMed:33117309}; ORFNames=BO99DRAFT_396251;
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: Dehydrogenase; 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E4QP00};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:33117309}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q12062}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; BR001648; FAA01296.1; -; Genomic_DNA.
DR EMBL; KZ825234; PYI13689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5GRB0; -.
DR SMR; A0A2V5GRB0; -.
DR STRING; 1450538.A0A2V5GRB0; -.
DR Proteomes; UP000249829; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..629
FT /note="Dehydrogenase pyvF"
FT /id="PRO_5015976897"
FT ACT_SITE 552
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 82..83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 144..147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 586
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 597..598
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 629 AA; 68339 MW; 0D9F93E98EA39A96 CRC64;
MAGSPFTTAL LSAWTLSTVA VGYPNGPWYQ TPLGPDVVRD PTRYPGAIEK TVDYVVVGGG
ASGLTVAARL SEDPSVTVAI VEAGSFYQEV SNASVVPGYA ADYLTGHIPP ELDWGFNTEP
QAGADGRVKH YTNAKTLGGN SAFNLMAYMT TSVGAMQKWA EEVDDDSWTY ANVTRYFQKS
LNFTGIDPHK RRANSTPELN PADVGYGGPL DVTYPNYAQP FSSWVKKAFD QVGMRPVGGF
MSGELFGSSW VLDTINHTDG QRASSAKTFL EPILHRRENL FLYNRTLAER VLFDADRTAT
GVQASRGKTV FNLTATKEVV LTAGGLMTPQ LLQVSGVGNA ALLQELRIPV VLDAPQVGQQ
MEDHISFGVA HRVDVETNSA LKYAGPRQHA VEEFNEAQAG ILSSPGPDFG GFADIPSELR
NFSASTHADL AGLPKDWPEG FFISFPVDVG FPQDGYNYAM IVCTLMTPMS RGHISIRSPS
MHDRPVIDPR WLTSTSDVEI AVAAVRRIRQ YLQMPVLERN VLVGGEVAPG PEVQTFAEIH
DYLKKNFNSM SHPACTCRMG KKGDPDAVVD PKGRVFGVKN LRIADASVFR FLPPGLPLGV
VYMVAEKIAD DIKHDQKHGA GEEGLRTEF
