ID   ASC3_DIDFA              Reviewed;         331 AA.
AC   A0A5C1RDG7;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=2-oxoglutarate-dependent dioxygenase {ECO:0000303|PubMed:31554725};
DE            EC=1.14.-.-;
DE   AltName: Full=Ascochitine biosynthesis cluster protein 3 {ECO:0000303|PubMed:31554725};
GN   ORFNames=orf3 {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: 2-oxoglutarate-dependent dioxygenase; 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   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:31554725}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; MN052624; QEN17971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C1RDG7; -.
DR   SMR; A0A5C1RDG7; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.330; -; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Virulence.
FT   CHAIN           1..331
FT                   /note="2-oxoglutarate-dependent dioxygenase"
FT                   /id="PRO_0000448986"
FT   DOMAIN          186..292
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         214
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         216
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         272
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         283
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   331 AA;  37120 MW;  C8962B634F93BB3E CRC64;
     MPAATTSIFY LPDINIAPWL ESPTSPSGQQ VVDQVRKACT STGFFQLTGH GLSQDVVEDI
     FAASAKFFAL PKDVKQGLNF TKNLGFRGYE LIGAQVYESD VLPDLKEGFL AGIDLPFEDM
     RVQNKRFFAG QNVWPPPDVL PYAEFREPVE KYYKSIMQLC FTVMDLVAAT LPYGPDVFDE
     WKSHEPACPL RLLHYPPTPA HVAGKTRQLG SSAHTDFGAL TLLLQDSHEG LEVLNHDTGD
     WVLVPPKPGA FVVNIADMMT MVTVGEYKSS KHRVINRNET EDRYSVVFFM DGNVDYKLRR
     LDKIGQPIGD DEDLLTVEDY MLGKRNSTYV K