ID   ASC8_DIDFA              Reviewed;         379 AA.
AC   A0A5C1RGL7;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Ascochitine biosynthesis cluster protein 8 {ECO:0000303|PubMed:31554725};
DE   AltName: Full=SAT domain-containing protein {ECO:0000303|PubMed:31554725};
GN   ORFNames=orf {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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
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DR   EMBL; MN052629; QEN17976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C1RGL7; -.
DR   SMR; A0A5C1RGL7; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   Gene3D; 3.40.366.10; -; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR032088; SAT.
DR   Pfam; PF16073; SAT; 1.
PE   3: Inferred from homology;
KW   Membrane; Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..379
FT                   /note="Ascochitine biosynthesis cluster protein 8"
FT                   /id="PRO_0000448984"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   379 AA;  40977 MW;  4FBB58A3C811EB8B CRC64;
     MVLQKLGDAQ RILVFGDSTI ENKLPVIRAL WEASESHPLL KAFLQQAVEI IQEETQKLAS
     HEGSLFLHCI DVLEVAEVYA EADEPDELIA SVLALVARFG ALVLDLERDD SNKRSVGPVS
     ILGFCTGLLA GAVAACAEDM IKVFDLACEV LAISFRLVVA LVRRSKAIEP NAGLWATTFI
     RISKEELEMQ LDDYNLHHGL SQDKKAYIGV SSQSWNSVFA PPSVILHIAR QCPILSQISQ
     VPTTAAMAVH ASHLSRPDVN WILGSLPGLE TPVLPDRLIV STSTGKPFLA KTLRELIQSI
     IADISMNILD IDGTIHGICS GLDMTKPVVI SAMGPSPNIP ALTRRLASGG VQLKTFAVIA
     GDRPRRVVPR RPSSSGYSS