ID   DEP4_ALTBR              Reviewed;         581 AA.
AC   D2E9W9;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 33.
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};
OS   Alternaria brassicicola (Dark leaf spot agent).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Brassicicola.
OX   NCBI_TaxID=29001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION,
RP   INDUCTION, AND PATHWAY.
RC   STRAIN=MUCL 202097;
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).
CC   -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of depudecin, a highly oxidized eleven-carbon
CC       linear polyketide that acts as a histone deacetylase (HDAC) inhibitor
CC       and makes a small contribution to pathogenesis (PubMed:19737099). 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}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:19737099}.
CC   -!- INDUCTION: Expression is positively regulated by the depudecin
CC       biosynthesis cluster-specific transcription activator DEP6
CC       (PubMed:19737099). {ECO:0000269|PubMed:19737099}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of depudecin and
CC       accumulates an epoxide-containing metabolite of slightly higher
CC       retention factor than native depudecin (PubMed:19737099).
CC       {ECO:0000269|PubMed:19737099}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; FJ977165; ACZ57547.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2E9W9; -.
DR   SMR; D2E9W9; -.
DR   PHI-base; PHI:2378; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
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..581
FT                   /note="FAD-dependent monooxygenase DEP4"
FT                   /id="PRO_0000441941"
FT   BINDING         43..46
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         54..56
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         108
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         183..202
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         219..220
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         351..352
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         470
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
SQ   SEQUENCE   581 AA;  66051 MW;  761A4F00443A41BC CRC64;
     MESFDIVVVG AGWYGLMAAR TYLELAPETN LLIVDDSSTV GGVWSKERIY PSLFAQISHP
     LFEYSFYPMP KDDISPDGFV SGKTIHNYLT SFTRDHNLLP RLRLNTRVER VRRGPSDAGG
     WVLDIKEGNP LLCHKLIYAT GANSSPIIPT WPRQTFEQPV IHSLDLGKHQ DYIAKSVETA
     TVVGRSKSSY DAVYHLLCEG KRVNWVMRDG LSGPFSLYAP TFMGLWNIAD HISTRFASSF
     SPCIMNTSGF CYNFLQRNAV GRTLTNVYWR AANYLSVSHA EYWRTPNAEK LRPRPYSDGV
     FWGSGGIGIA TAPDFWKVFH RGNITIHSTE IDSLSHGDVV NLKNGYSLAT DIVIHCTGFD
     KGYTTFDPEL REELGLQYNS KSISRWSLLD AKAEQTVDEL LPYLRTAPLQ DMDPDASSRP
     EQGPNRHFRR LVVPELAARG DRSILFPGHI HSAFTPLAAE LQALWGVSWM LGWRELPPQE
     EMELEAATFN AWTRKRYLEQ GKKHSYFIYD YIPYIDTLMR DLGLNPYRKS SVFEEWFVRY
     KPSDYGTILD EYRDIRRLSL ECLQGTGGFA ERTNGHGVNM K