ID   DEP2_ALTBR              Reviewed;         528 AA.
AC   D2E9W7;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=FAD-dependent monooxygenase DEP2 {ECO:0000303|PubMed:19737099};
DE            EC=1.-.-.- {ECO:0000305|PubMed:19737099};
DE   AltName: Full=Depudecin biosynthesis cluster protein 2 {ECO:0000303|PubMed:19737099};
DE   Flags: Precursor;
GN   Name=DEP2 {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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}.
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 paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; FJ977165; ACZ57545.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2E9W7; -.
DR   SMR; D2E9W7; -.
DR   PHI-base; PHI:2376; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..528
FT                   /note="FAD-dependent monooxygenase DEP2"
FT                   /id="PRO_0000441937"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         38..39
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         133
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         321..325
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   CARBOHYD        521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   528 AA;  59158 MW;  5179A8E54D171F3F CRC64;
     MEDGRSTFKV IIIGAGVTGL TLAHCLAKAC IDYVLLDKGI VAPSFGTTIT LQPHGCRILH
     QLGCLDAVLA SCDVMSGAQC RDPSGKTFAS NDFFRVVKKF TGYDTRTLDR KVFLRTMYEQ
     LPDQSRVHER ARVEEIIEDN EKTRVVLQDG QEFVGNLVIG TDGVHSKVRE IMWDNANTAK
     PGMITVEEKR AMVTQYNAIV MACSPVPGLG SHDMEVTSND KFSFLLLCQP DWISIIVHNK
     LPEDQQCTWP TRRRYTESDM EALVSRILEC PITETVVFGE LWKRRLKAQM ISLEEGVLEH
     WFFGRIVLAG DAIHKVTPNS ALGGNTAMED AVTVANTLHT LLAAHPNKKP STVELQDAFR
     DNYQNARMDR VRAIVKVGGD LTRQQAYDGW KRYLIQRWLT PIVGLDTLAK NIAGLCVTAP
     KLSYIDFEEK RGMLNWQDTV AADKELEMHH ENVGGVRAEY HKSKWLLTSA DWSGGFEAVF
     PQILGVLMVM WSSVWLFHLA FSRHCISGFG GEVWRTFGAD NETSCVAK