ASC4_DIDFA
ID ASC4_DIDFA Reviewed; 270 AA.
AC A0A5C1RHX3;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=Esterase {ECO:0000303|PubMed:31554725};
DE EC=3.1.2.- {ECO:0000305|PubMed:31554725};
DE AltName: Full=Ascochitine biosynthesis cluster protein 4 {ECO:0000303|PubMed:31554725};
GN ORFNames=orf4 {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: Esterase; 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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:31554725}.
CC -!- SIMILARITY: Belongs to the LovG family. {ECO:0000305}.
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DR EMBL; MN052625; QEN17972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C1RHX3; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005645; FSH_dom.
DR Pfam; PF03959; FSH1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase; Virulence.
FT CHAIN 1..270
FT /note="Esterase"
FT /id="PRO_0000448987"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
FT ACT_SITE 244
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
SQ SEQUENCE 270 AA; 29361 MW; 0F1988295B8CDFAF CRC64;
MPSSEASPAA GLSEDSTRHL PRILCLHGGG TNARIFKAQC RQLSAQLKRD FRFIYAEAPW
ISIAGPDVLA VYGQWGPFKR WLRWSPEQPD ITTQETVKEL DQCLARAVEA DNACGTTGEV
VAILGFSQGA KVAASVLYWQ QRSGQSLGLR ASNSGYRFGV LLAGSSPLVD LSTCEGDSNG
LSENAWPGDD MIGPRALDCD THKLIIPTLH VHGLQDRGLR LHRALMEDFC APESTTLIEW
DGVHRVPLNR AEVSRVAGQI RKLAGLTSNS
