ID   ASC1_DIDFA              Reviewed;         494 AA.
AC   A0A5C1REZ4;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000303|PubMed:31554725};
DE            EC=1.2.1.3 {ECO:0000255|PROSITE-ProRule:PRU10007};
DE   AltName: Full=Ascochitine biosynthesis cluster protein 1 {ECO:0000303|PubMed:31554725};
GN   ORFNames=orf1 {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: Aldehyde dehydrogenase; part of the gene cluster that
CC       mediates the biosynthesis of the selective antifungal agent
CC       ascochitine, an o-quinone methide that plays a possible protective role
CC       against other microbial competitors in nature and is considered to be
CC       important for pathogenicity of legume-associated Didymella species
CC       (PubMed:31554725). The pathway probably begins with the synthesis of a
CC       keto-aldehyde intermediate by the ascochitine non-reducing polyketide
CC       synthase pksAC from successive condensations of 4 malonyl-CoA units,
CC       presumably with a simple acetyl-CoA starter unit (Probable). Release of
CC       the keto-aldehyde intermediate is consistent with the presence of the
CC       C-terminal reductive release domain (Probable). The HR-PKS (orf7)
CC       probably makes a diketide starter unit which is passed to the non-
CC       reducing polyketide synthase pksAC for further extension, producing
CC       ascochital and ascochitine (Probable). The aldehyde dehydrogenase
CC       (orf1), the 2-oxoglutarate-dependent dioxygenase (orf3) and the
CC       dehydrogenase (orf9) are probably involved in subsequent oxidations of
CC       methyl groups to the carboxylic acid of the heterocyclic ring
CC       (Probable). The ascochitine gene cluster also includes a gene encoding
CC       a short peptide with a cupin domain (orf2) that is often found in
CC       secondary metabolite gene clusters and which function has still to be
CC       determined (Probable). {ECO:0000269|PubMed:31554725,
CC       ECO:0000305|PubMed:31554725}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10007};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:31554725}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; MN052622; QEN17969.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C1REZ4; -.
DR   SMR; A0A5C1REZ4; -.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Virulence.
FT   CHAIN           1..494
FT                   /note="Aldehyde dehydrogenase"
FT                   /id="PRO_0000448982"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         223..228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q28399"
SQ   SEQUENCE   494 AA;  53651 MW;  40EBCC2830B5592E CRC64;
     MSASKHIICE YSSEDPSKDF EVHNPATGAV IAIVRAGDAT TLDKAVQVAH KAFLEWKKVP
     LTRRSQLMFK CAEEVEKHAE ELAELLTTEN GKLLSDGRMV DVNFVSQVYR YFGSLIDKLP
     GEFHDSGSVY RYVTREPHGV CGGILPFNWP PIHTAGKSAP CIAMGNTIII KPGEQAPLTS
     MRIVDILNTV LPKGVVQYVP GVGPEVPQAL TAHPLVKMVS ITGSTTAGKA VVMAASALVK
     PTVLELGGKN ALVVFPDADL HRAARDALEG AFFNKGEACT ATSRLLIHND IYDAFIEKYA
     AAVCKLQAGN GLKKGTHVGP CVTQAQKERV LDFIRIGEEE GATIAAQGRL PDDAEEKDGF
     FVAPTLFTNV KHSMRIAQEE IFGPVVTACK FDSEEEAVSI INGARWGLTC AIYSGNQELA
     LRMCRQVDVG MTFINNYFRN TLGIPFGGVK ETGYGREHCI DTLKDWSTSK VIQMPSGLAP
     VPSWPPVNEL LPWQ