ID   ANDH_EMEVA              Reviewed;         337 AA.
AC   A0A097ZPD4;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Oxidoreductase andH {ECO:0000303|PubMed:25216349};
DE            EC=1.-.-.- {ECO:0000305|PubMed:25216349};
DE   AltName: Full=Anditomin synthesis protein H {ECO:0000303|PubMed:25216349};
GN   Name=andH {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, CATALYTIC ACTIVITY, AND
RP   DISRUPTION PHENOTYPE.
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: Oxidoreductase; 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   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:25216349}.
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 NmrA-type oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; AB981314; BAP81862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A097ZPD4; -.
DR   SMR; A0A097ZPD4; -.
DR   BioCyc; MetaCyc:MON-19055; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase.
FT   CHAIN           1..337
FT                   /note="Oxidoreductase andH"
FT                   /id="PRO_0000436584"
SQ   SEQUENCE   337 AA;  37041 MW;  319B0E178ACE14D3 CRC64;
     MPSLSQIRQA NELLEDSHSE IVAAFVGGTS GVGEEAAKRL ASCVRKPEIF IVGRNEESAA
     RVLAELRNAN PQGSYQFVKV DISLLRNVDR ACEAIRHKTQ TLDLLFISAG SALVAREDTE
     EGLEKNLVER YYARMRFTQS LLPLLQASNK SPRVVSVLLG GFEIELETDN LDLTKPRTAI
     YSTRHAATMT SLSMEHLATV YRSISFVHIY PGMVKTPLLD KGLGRFLARI AWILYWPFSI
     TLEQSGQYNV YMATSAAYPP LSPENQQGAG ASLAEGGEIC IGSTGKVGAG SYILNYDGAN
     RTNVKLMEGY RVRDYAQHIW THTLSTFQTV TGSAEPA