ID   PGMF_ASPTE              Reviewed;         356 AA.
AC   A0A1W5SKT4;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Trans-enoyl reductase pgmF {ECO:0000303|PubMed:35351612};
DE            EC=1.-.-.- {ECO:0000305|PubMed:35351612};
DE   AltName: Full=Pigmented naphthoquinones biosynthesis cluster protein F {ECO:0000303|PubMed:35351612};
GN   Name=pgmF {ECO:0000303|PubMed:28471414};
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND INDUCTION.
RC   STRAIN=MUCL38669;
RX   PubMed=28471414; DOI=10.3390/microorganisms5020022;
RA   Palonen E.K., Raina S., Brandt A., Meriluoto J., Keshavarz T., Soini J.T.;
RT   "Melanisation of Aspergillus terreus-is butyrolactone I involved in the
RT   regulation of both DOPA and DHN types of pigments in submerged culture?";
RL   Microorganisms 5:0-0(2017).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=35351612; DOI=10.1016/j.fgb.2022.103690;
RA   Tang S., Men P., Zhang W., Li H., Li Z., Huang X., Lu X.;
RT   "Identification of a polyketide biosynthesis gene cluster by
RT   transcriptional regulator activation in Aspergillus terreus.";
RL   Fungal Genet. Biol. 160:103690-103690(2022).
CC   -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC       mediates the biosynthesis of pleosporalin A, ascomycone A, as well as a
CC       third cryptic naphthoquinone derived pigment, all responsible for the
CC       coloration of conidia (PubMed:28471414, PubMed:35351612). The pathway
CC       begins with the biosynthesis of the cyclized heptaketide 3-acetonyl-
CC       1,6,8-trihydroxy-2-naphthaldehyde by the NR-PKS pgmA. The C-6 hydroxyl
CC       group is further methylated by the O-methyltransferase pgmB to yield
CC       fusarubinaldehyde which is in turn oxidized by the cytochrome P450
CC       monooxygenase pgmC at C-9. The C-1 hydroxyl group is then methylated
CC       spontaneously. Although pgmE, pgmD and pgmH are essential for the
CC       production of pleosporalin A, it is not the case for the 2 other final
CC       products and it remains difficult to assign a specific function to each
CC       enzyme. PgmF and pgmG seem not to be involved in pigment biosynthesis
CC       although they were regulated by the cluster-specific transcription
CC       factor pgmR (PubMed:35351612) (Probable). {ECO:0000269|PubMed:28471414,
CC       ECO:0000269|PubMed:35351612, ECO:0000305|PubMed:35351612}.
CC   -!- INDUCTION: Expression is significantly up-regulated at the end of late
CC       growth phase, in the presence of Butyrolactone I (PubMed:28471414).
CC       Expression is positively regulated by the pgm cluster-specific
CC       transcription factor pgmR (PubMed:35351612).
CC       {ECO:0000269|PubMed:28471414, ECO:0000269|PubMed:35351612}.
CC   -!- DISRUPTION PHENOTYPE: Does not affect the production of the
CC       naphthoquinones derived pigments. {ECO:0000269|PubMed:35351612}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; KX470750; ARB51367.1; -; mRNA.
DR   VEuPathDB; FungiDB:ATEG_06209; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NADP; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..356
FT                   /note="Trans-enoyl reductase pgmF"
FT                   /id="PRO_0000456011"
FT   BINDING         57..60
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         175..178
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         198..201
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         216
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         261..262
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         342..343
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ   SEQUENCE   356 AA;  38320 MW;  A25B965D70DED462 CRC64;
     MASTVPSTMK AWQFSSASPT IEANLKLNNN APLPDGANNL GPDQVLVKVI AAGLNPVDFK
     FAEIPWLGRL IVGSPSTPGM DFAGRVVATG PNTKSVAVED LKPGQLVFGR LDSPSKFGTL
     AEYTIAPRKG CVAIPPGARV IETACVASVG LTAYQSIVYR LKDHTGKRIF LNGGSGGCGT
     FGIQIAKQMG CHVTTSCSTP NVDLCRSLGA DTVIDYKKTD VIAELKKMQP FDLVVDNVGV
     PTDLYWAAPS FTNPGAPYVQ VGALAVTPGF ILGNFFKARW PGWLGGGKRP WEFMHIESNV
     QDYEQLGRWM QEGKLRAVVD EVFGMQDDGP VKAYQKLRTG RAKGKIIVKI DETWED