ID   ASC10_DIDFA             Reviewed;         128 AA.
AC   A0A5C1RFE1;
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=Glyoxylase-like domain-containing protein {ECO:0000303|PubMed:31554725};
DE   AltName: Full=Ascochitine biosynthesis cluster protein 10 {ECO:0000303|PubMed:31554725};
GN   ORFNames=orf10 {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: Glyoxylase-like domain-containing protein; part of the gene
CC       cluster that mediates the biosynthesis of the selective antifungal
CC       agent ascochitine, an o-quinone methide that plays a possible
CC       protective role against other microbial competitors in nature and is
CC       considered to be important for pathogenicity of legume-associated
CC       Didymella species (PubMed:31554725). The pathway probably begins with
CC       the synthesis of a keto-aldehyde intermediate by the ascochitine non-
CC       reducing polyketide synthase pksAC from successive condensations of 4
CC       malonyl-CoA units, presumably with a simple acetyl-CoA starter unit
CC       (Probable). Release of the keto-aldehyde intermediate is consistent
CC       with the presence of the C-terminal reductive release domain
CC       (Probable). The HR-PKS (orf7) probably makes a diketide starter unit
CC       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}.
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DR   EMBL; MN052631; QEN17978.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C1RFE1; -.
DR   SMR; A0A5C1RFE1; -.
DR   Gene3D; 3.10.180.10; -; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR041581; Glyoxalase_6.
DR   InterPro; IPR037523; VOC.
DR   Pfam; PF18029; Glyoxalase_6; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   4: Predicted;
KW   Virulence.
FT   CHAIN           1..128
FT                   /note="Glyoxylase-like domain-containing protein"
FT                   /id="PRO_0000448995"
FT   DOMAIN          6..125
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
SQ   SEQUENCE   128 AA;  13820 MW;  FECA752283F0BD8B CRC64;
     MVLHGQISGI EIPATDVERA AKFYSDTFGW KFQAPANGTI PASKMQTFTA PGDIFPDEGV
     VSKVEEIPKS GAKFYINVDD LKATIEAVTK NGGKQLSDVI SLGPHVPPFQ FFHDTEGNTH
     AICTRPGK