ID   DEP4_FUSLA              Reviewed;         580 AA.
AC   A0A0M9ER62;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=FAD-dependent monooxygenase DEP4 {ECO:0000303|PubMed:19737099};
DE            EC=1.-.-.- {ECO:0000305|PubMed:19737099};
DE   AltName: Full=Depudecin biosynthesis cluster protein 1 {ECO:0000303|PubMed:19737099};
GN   Name=DEP4 {ECO:0000303|PubMed:19737099}; ORFNames=FLAG1_09233;
OS   Fusarium langsethiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=179993;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fl201059;
RA   Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA   Frandsen R.J., Nielsen K., Thrane U.;
RT   "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT   producer.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=19737099; DOI=10.1094/mpmi-22-10-1258;
RA   Wight W.D., Kim K.-H., Lawrence C.B., Walton J.D.;
RT   "Biosynthesis and role in virulence of the histone deacetylase inhibitor
RT   depudecin from Alternaria brassicicola.";
RL   Mol. Plant Microbe Interact. 22:1258-1267(2009).
RN   [3]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=28460114; DOI=10.1093/molbev/msx145;
RA   Reynolds H., Slot J.C., Divon H.H., Lysoee E., Proctor R.H., Brown D.W.;
RT   "Differential retention of gene functions in a secondary metabolite
RT   cluster.";
RL   Mol. Biol. Evol. 34:2002-2015(2017).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       depudecin, a highly oxidized eleven-carbon linear polyketide that acts
CC       as a histone deacetylase (HDAC) inhibitor and makes a small
CC       contribution to pathogenesis (PubMed:19737099, PubMed:28460114). The
CC       reducing polyketide synthase DEP5 is the central enzyme in depudecin
CC       biosynthesis by yielding the backbone polyketide chain
CC       (PubMed:19737099). The monooxygenases DEP2 and DEP4, as well as the
CC       uncharacterized protein DEP1, then act as tailoring enzymes to modify
CC       the intermediate polyketide chain into depudecin (PubMed:19737099).
CC       {ECO:0000269|PubMed:19737099, ECO:0000269|PubMed:28460114}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:28460114}.
CC   -!- INDUCTION: Expression correlates with the production of depudecin with
CC       high levels on oat grain medium, and minimal levels on oat flower
CC       medium and complete medium (PubMed:28460114).
CC       {ECO:0000269|PubMed:28460114}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; JXCE01000338; KPA37942.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9ER62; -.
DR   SMR; A0A0M9ER62; -.
DR   EnsemblFungi; KPA37942; KPA37942; FLAG1_09233.
DR   OrthoDB; 405736at2759; -.
DR   Proteomes; UP000037904; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN           1..580
FT                   /note="FAD-dependent monooxygenase DEP4"
FT                   /id="PRO_0000441942"
FT   BINDING         47..50
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         58..60
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         112
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         186..205
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         222..223
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         354..355
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         473
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
SQ   SEQUENCE   580 AA;  66534 MW;  73BE8ECE8E19C866 CRC64;
     MSQPLETFDV IVIGAGWYGL MAARTFLELA PDTNLLILDD GKTVGGVWSK ERIYPSLFAQ
     ISHPLFEYSF YPMPEEDISP DGFVSGKTIQ KYLEAFAKDH GLILHLRLET RVEKVKRGVN
     SNEWILEIKG DKPLACSKLI YATGANSSPI IPKWPREGFE KPVIHSLDLG RYQDYIANNV
     QKAVVVGRSK SSYDAVYHLL CAGKKVNWVM RDGQSGPFSL YAPTFMGLWN IADHISTRFA
     SSFSPCIMST DGFCYNFFQR SALGRVLTNM YWRTANYLSV SHAEYWRTEN SEKLRPRPYS
     DGVFWGSGGI GIATAPDFWE TFHRGDVTIH STEIESVSHK DVTNLKNGYS IATDIIIHCT
     GFDKGYGAFD PQLRNELGLE YNTKEFSRWT MLDEKADQTV DRLLPYICDS PNQYGDSEAS
     RSTGQGPNRH YRRLVVPELA ARGDRSILFP GHIHSAFTPL AAELQALWGV SWMLGWRDLP
     SKEEMETEAA NFNAWTRKRY LEQGRKHSYF IYDYIPYIDT LMKDLGLDPF RKSNVFEEWF
     VRYKPSDYKT ILEEYRSVRR HEREMERSGE ESVARMKRCD