ID   ASC9_DIDFA              Reviewed;         621 AA.
AC   A0A5C1RDA6;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Dehydrogenase {ECO:0000303|PubMed:31554725};
DE            EC=1.1.-.- {ECO:0000305|PubMed:31554725};
DE   AltName: Full=Ascochitine biosynthesis cluster protein 9 {ECO:0000303|PubMed:31554725};
GN   ORFNames=orf9 {ECO:0000303|PubMed:31554725};
OS   Didymella fabae (Leaf and pod spot disease fungus) (Ascochyta fabae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=372025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=AF247/15;
RX   PubMed=31554725; DOI=10.1128/msphere.00622-19;
RA   Kim W., Lichtenzveig J., Syme R.A., Williams A.H., Peever T.L., Chen W.;
RT   "Identification of a polyketide synthase gene responsible for ascochitine
RT   biosynthesis in Ascochyta fabae and its abrogation in sister taxa.";
RL   MSphere 4:0-0(2019).
CC   -!- FUNCTION: Dehydrogenase; part of the gene cluster that mediates the
CC       biosynthesis of the selective antifungal agent ascochitine, an o-
CC       quinone methide that plays a possible protective role against other
CC       microbial competitors in nature and is considered to be important for
CC       pathogenicity of legume-associated Didymella species (PubMed:31554725).
CC       The pathway probably begins with the synthesis of a keto-aldehyde
CC       intermediate by the ascochitine non-reducing polyketide synthase pksAC
CC       from successive condensations of 4 malonyl-CoA units, presumably with a
CC       simple acetyl-CoA starter unit (Probable). Release of the keto-aldehyde
CC       intermediate is consistent with the presence of the C-terminal
CC       reductive release domain (Probable). The HR-PKS (orf7) probably makes a
CC       diketide starter unit which is passed to the non-reducing polyketide
CC       synthase pksAC for further extension, producing ascochital and
CC       ascochitine (Probable). The aldehyde dehydrogenase (orf1), the 2-
CC       oxoglutarate-dependent dioxygenase (orf3) and the dehydrogenase (orf9)
CC       are probably involved in subsequent oxidations of methyl groups to the
CC       carboxylic acid of the heterocyclic ring (Probable). The ascochitine
CC       gene cluster also includes a gene encoding a short peptide with a cupin
CC       domain (orf2) that is often found in secondary metabolite gene clusters
CC       and which function has still to be determined (Probable).
CC       {ECO:0000269|PubMed:31554725, ECO:0000305|PubMed:31554725}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:E4QP00};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:31554725}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q12062}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; MN052630; QEN17977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C1RDA6; -.
DR   SMR; A0A5C1RDA6; -.
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.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Virulence.
FT   CHAIN           1..621
FT                   /note="Dehydrogenase"
FT                   /id="PRO_0000448994"
FT   ACT_SITE        562
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         23..24
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         44..45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         102..105
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         590
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         601..602
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
SQ   SEQUENCE   621 AA;  67086 MW;  D859844DB952F1F0 CRC64;
     MPYTTIDDLV NSALDYVIIG GGTAGLVLAA RLSEKDSVNV GVIEAGLSRL GDPKVDMPTG
     AALMLGNEDY DWNFKSVPQA ASKDRVYHIP RGKMLGGSSA INFMAYGRPC AADIDDWSSK
     LGLPGWSWNE LLPYLKKSQK LESDLPNIKQ RDANLFPFLA DSQGTDGAIH TSASPWHVPF
     EDDLLPALDK TSGYARPKDP YSGSHVGFYR SLWAIDRSKK PVRSYSASGF LAPIIDRPNL
     KVVTNTVACR VLTDSNEDGS MRATGVEVQH DGAIHVLSAQ REVILSAGAF QSPQILEQSG
     IGDPAILHQL KIPCIIGNRN VGNNLQEKLL SAVVYELAPG TMSLDSVLRD PELRKEHQKL
     YTEAHSGALS GCINLTGFLP YSSLVTSDDI DDTIGDILSL KILSGSPQSP NQNGPFQRWQ
     REAIAARMKS LNSADLQFVC TPANFDTANG YGNLARLSPG SPAGYNACYS LVVSQMYPLS
     RGSVHSTSSN PLDAPEIDPG FLSHPADVDV IAAGIQFADR VLSSEALRGK VGRRVVPPPS
     LDLQDRDQVR DFVREHIVTY HHSLGTCAMG QVVDERLRVK GVRSLRVVDA SVMPMQVSTA
     ILATVYAVAE KAADMILADH P