ID   ASC2_DIDFA              Reviewed;         186 AA.
AC   A0A5C1RFS2;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Ascochitine biosynthesis cluster protein 2 {ECO:0000303|PubMed:31554725};
GN   ORFNames=orf2 {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: Part of the gene cluster that mediates the biosynthesis of
CC       the selective antifungal agent ascochitine, an o-quinone methide that
CC       plays a possible protective role against other microbial competitors in
CC       nature and is considered to be important for pathogenicity of legume-
CC       associated Didymella species (PubMed:31554725). The pathway probably
CC       begins with the synthesis of a keto-aldehyde intermediate by the
CC       ascochitine non-reducing polyketide synthase pksAC from successive
CC       condensations of 4 malonyl-CoA units, presumably with a simple acetyl-
CC       CoA starter unit (Probable). Release of the keto-aldehyde intermediate
CC       is consistent with the presence of the C-terminal reductive release
CC       domain (Probable). The HR-PKS (orf7) probably makes a diketide starter
CC       unit which is passed to the non-reducing polyketide synthase pksAC for
CC       further extension, producing ascochital and ascochitine (Probable). The
CC       aldehyde dehydrogenase (orf1), the 2-oxoglutarate-dependent dioxygenase
CC       (orf3) and the dehydrogenase (orf9) are probably involved in subsequent
CC       oxidations of methyl groups to the carboxylic acid of the heterocyclic
CC       ring (Probable). The ascochitine gene cluster also includes a gene
CC       encoding a short peptide with a cupin domain (orf2) that is often found
CC       in secondary metabolite gene clusters and which function has still to
CC       be determined (Probable). {ECO:0000269|PubMed:31554725,
CC       ECO:0000305|PubMed:31554725}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:31554725}.
CC   -!- SIMILARITY: Belongs to the oryJ family. {ECO:0000305}.
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DR   EMBL; MN052623; QEN17970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C1RFS2; -.
DR   SMR; A0A5C1RFS2; -.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR013096; Cupin_2.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF07883; Cupin_2; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Virulence.
FT   CHAIN           1..186
FT                   /note="Ascochitine biosynthesis cluster protein 2"
FT                   /id="PRO_0000448983"
SQ   SEQUENCE   186 AA;  20324 MW;  FBD2722E3D757476 CRC64;
     MSAQKPITHF GLRDITRYTT TVDSNGNGVF SRADQGDFEA TMGDGRVARF DLFQAGQVPL
     NINDGADIKW SGENQPGLHV PNGVAFRMMD FAPEGGSDWH RAALFAFVII VEGELELSLD
     GGETKVLLPG DTTLVRGPSH KVRNPSTAKP CRTLWVLLDI TPTHINGKLL KHEMGHHTGE
     YQEGSK