ID   ANDF_EMEVA              Reviewed;         285 AA.
AC   A0A097ZPD9;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Dioxygenase andF {ECO:0000303|PubMed:25216349};
DE            EC=1.14.11.- {ECO:0000269|PubMed:25216349};
DE   AltName: Full=Anditomin synthesis protein F {ECO:0000303|PubMed:25216349};
GN   Name=andF {ECO:0000303|PubMed:25216349};
OS   Emericella variicolor (Aspergillus stellatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1549217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP   CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX   PubMed=25216349; DOI=10.1021/ja508127q;
RA   Matsuda Y., Wakimoto T., Mori T., Awakawa T., Abe I.;
RT   "Complete biosynthetic pathway of anditomin: nature's sophisticated
RT   synthetic route to a complex fungal meroterpenoid.";
RL   J. Am. Chem. Soc. 136:15326-15336(2014).
CC   -!- FUNCTION: Dioxygenase; part of the gene cluster that mediates the
CC       biosynthesis of anditomin, a fungal meroterpenoid (PubMed:25216349).
CC       The first step of the pathway is the synthesis of 3,5-
CC       dimethylorsellinic acid (DMOA) by the polyketide synthase andM
CC       (PubMed:25216349). DMOA is then converted to the phthalide compound
CC       5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by the cytochrome P450
CC       monooxygenase andK, which is further prenylated by the
CC       prenyltransferase andD to yield farnesyl-DHDMP (PubMed:25216349).
CC       Further epoxidation by the FAD-dependent monooxygenase andE leads to
CC       epoxyfarnesyl-DHDMP (PubMed:25216349). The next step involves the
CC       terpene cyclase andB that converts epoxyfarnesyl-DHDMP into preandiloid
CC       A through opening of the epoxide ring followed by the cyclization of
CC       the farnesyl moiety (PubMed:25216349). Preandiloid A is in turn
CC       oxidized at the C-3 hydroxyl group to yield preandiloid B by the
CC       dehydrogenase andC (PubMed:25216349). The dioxygenase andA is solely
CC       responsible for the dehydrogenation of preandiloid B leading to the
CC       enone preandiloid C, as well as for the intriguing structural
CC       rearrangement to generate the bicyclo[2.2.2]octane core, transforming
CC       preandiloid C into andiconin (PubMed:25216349). FAD-binding
CC       monooxygenase andJ then produces andilesin D which is reduced by
CC       dehydrogenase andI to yield andilesin A (PubMed:25216349). Action of
CC       acetyltransferase andG followed by a spontaneous acetate elimination
CC       leads then to andilesin B, which is in turn substrate of the short
CC       chain dehydrogenase andH to yield andilesin C (PubMed:25216349).
CC       Finally, the dioxygenase andF catalyzes the transformation of andilesin
CC       C to anditomin (PubMed:25216349). {ECO:0000269|PubMed:25216349}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:25216349};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:25216349}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WAW9}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the synthesis of anditomin but
CC       accumulates andilesin A (PubMed:25216349).
CC       {ECO:0000269|PubMed:25216349}.
CC   -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR   EMBL; AB981314; BAP81860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A097ZPD9; -.
DR   SMR; A0A097ZPD9; -.
DR   BioCyc; MetaCyc:MON-19056; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..285
FT                   /note="Dioxygenase andF"
FT                   /id="PRO_0000436582"
FT   BINDING         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         130
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         205
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
SQ   SEQUENCE   285 AA;  32447 MW;  7EF0A1355EE5DBE7 CRC64;
     MTVPQLHYVP YDTPVEDVMR ILEECGTLVI RNFLDQKTVQ NVQNEVDDYV RNWNPGPKYN
     HDIKTVGSKT KQPSNLSLMS KTYRCEVLNH PWMHAICERM FGPTYGDYWF NGGSILHLEP
     GEHTQPIHQD HVFYHISKWR RPTDPDLTIN FAMALTEFTV ENGGTRVCPG SHLWENGHAP
     PAEEDMVPAL MQPGDALILP GSMWHSAGAN RSSEYRRGFA ASFHPCHFTP IESHHHLPRE
     MVEEMSPLVQ KMLGFRTLNL HNNVKVWKAG EGNLEDATGL KSIAV